Genetics and Pathogenicity Factors of Group C and G Streptococci

Horst Malke

doi:10.1128/9781555816513.ch16

Chapter 16 : Genetics and Pathogenicity Factors of Group C and G Streptococci

Author: Horst Malke

Content Type: Reference

Publication Year: 2006

Category: Bacterial Pathogenesis

Book DOI: 10.1128/9781555816513

Chapter DOI: 10.1128/9781555816513.ch16

MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price.

Preview this chapter:

Genetics and Pathogenicity Factors of Group C and G Streptococci, Page 1 of 2

< Previous page | Next page > /docserver/preview/fulltext/10.1128/9781555816513/9781555813437_Chap16-1.gif /docserver/preview/fulltext/10.1128/9781555816513/9781555813437_Chap16-2.gif

Abstract:

The application of recombinant DNA techniques has advanced one's understanding of group C streptococci (GCS) and group G streptococci (GGS) in diverse areas, and this chapter concentrates on the structure and function of pathogenetically relevant genes and proteins studied at the molecular level in recent years. On the basis of 16S rRNA comparative sequence analysis, GCS and GGS fall into two species groups, the pyogenic and the anginosus group; the latter is also known as “Streptococcus milleri” group. One hallmark of the gram-positive pathogens is the synthesis of specific cell wall-associated proteins that enable them to interact in various ways with proteins present in the body fluids or extracellular tissue matrix of their mammalian hosts. Such interactions may facilitate colonization, lead to molecular host mimicry, or interfere with various host defenses against invasion. The cell wall-associated proteins discussed are M and M-like proteins, immunoglobulin G (IgG)-binding proteins, fibronectin-binding proteins, and plasmin(ogen)-binding proteins. Other covered topics are cytoplasmic membrane-associated enzymes such as hyaluronan synthase and cytoplasmic membrane lipoprotein acid phosphatase, and extracellular proteins. The chapter ends with a discussion on the stringent and relaxed responses of Streptococcus dysgalactiae subsp. equisimilis.

Citation: Malke H. 2006. Genetics and Pathogenicity Factors of Group C and G Streptococci, p 196-212. In Fischetti V, Novick R, Ferretti J, Portnoy D, Rood J (ed), Gram-Positive Pathogens, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816513.ch16

Key Concept Ranking

Two-Component Signal Transduction Systems: 0.5697347
Restriction Fragment Length Polymorphism: 0.42488477
Nuclear Magnetic Resonance Spectroscopy: 0.42272794

0.5697347

Highlighted Text: Show | Hide

Full text loading...

Figures

Genetics and Pathogenicity Factors of Group C and G Streptococci

[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/10.1128/9781555816513.chap16-1,webId=/content/author/10.1128/9781555816513.chap16-1,properties={foaf_givenname=Horst, foaf_name=Horst Malke, foaf_surname=Malke}]]

/content/10.1128/9781555816513.chap16.fig16-1

FIGURE 1

Schematic representation of the domain organization of protein G. S, signal sequence; E, α2-macroglobulin-binding; A and B, human serum albumin-binding; C, IgG-binding; W, cell wall-associated region; M, cell membrane-associated region. (Adapted from reference 124 )

10.1128/9781555816513/fig16-1_thmb.gif

10.1128/9781555816513/fig16-1.gif

FIGURE 1

/content/10.1128/9781555816513.chap16.fig16-2

FIGURE 2

Organization of the streptokinase-M protein gene region in the S. dysgalactiae subsp. equisimilis H46A chromosome based on references 38 and 98 . Arrows represent the genes and their orientation: nrdI, ribonucleotide reductase; mgc, multigene regulator of GCS; emm, M protein; cpdB, 2′,3′-cyclic nucleotide 2′-phosphodiesterase; rel, bifunctional (p)ppGppase and (p)ppGpp synthetase; dtd, D-tyrosyl-tRNATyr deacylase; skc, streptokinase; lrp, leucine-rich protein of unknown function; abc, ATP-binding cassette transporter; dexB, α-glucosidase.

10.1128/9781555816513/fig16-2_thmb.gif

10.1128/9781555816513/fig16-2.gif

FIGURE 2

/content/10.1128/9781555816513.chap16.fig16-3

FIGURE 3

Sequence comparison of E. coli and S. pyogenes σ factors ( 5 ) between region 2.4 and the start of region 3. Identical and similar amino acids are marked by asterisks and dots, respectively. The residues identified in E. coli as contacting the TG extension of the −10 promoter hexamer are indicated by open boxes.

10.1128/9781555816513/fig16-3_thmb.gif

10.1128/9781555816513/fig16-3.gif

FIGURE 3

/content/10.1128/9781555816513.chap16.fig16-4

FIGURE 4

Bootstrapped (1,000 trials) neighbor-joining phylogenetic tree of the FasA-BlpRComE family of streptococcal response regulators graphed by the MEGA2 software ( 72 ) based on ClustalX multiple alignment (http://www.ncbi.nlm.nih.gov). Species abbreviations and sources of the proteins are as follows: Sag1, S. agalactiae, AF390107; San1, S. anginosus, AJ000864; Sau1, identical to AgrA from Staphylococcus aureus, AY082629; Sdy1, S. dysgalactiae subsp. equisimilis, AY075107; Seq1, Seq2, Seq3, S. equi subsp. equi, http://www.sanger.ac.uk/Projects/S_equi; Sgo1, S. gordonii, http://www.tigr.org/tdb/mdb/mdbinprogress.html; Sgo2, X98109; Sin1, S. infantis, AF498313; Smi1, S. mitis, AJ000871; Smi2, http://www.tigr.org/tdb/mdb/mdbinprogress.html; Smu1, S. mutans, AE015016; Sor1, S. oralis, AJ240794; Spn1, S. pneumoniae, AJ278302; Spn2, AJ240793; Spy1, S. pyogenes, AE009971; Spy2, AE009991; Sso1, Sso2, S. sobrinus, http://www.tigr.org/tdb/mdb/mdbinprogress.html; Ssu1, S. suis, AY125957; Sub1, S. uberis, http://www.sanger.ac.uk/Projects/S_uberis; Szo1, Szo2, S. equi subsp. zooepidemicus, http://www.sanger.ac.uk/Projects/S_zooepidemicus. When sets of sequences >90% identical were identified in the same species, only one sequence was included to avoid analysis of duplicate sequences. For taxonomic reasons, the exception was S. equi, for which both subspecies are included in spite of Seq1 and Szo1 on one hand, and Seq2 and Szo2 on the other, being >90% identical. Bootstrap confidence estimates (%) are given next to the tree nodes: groups found in >95% of trials are considered well supported, those found in >50% are considered suggestive.

10.1128/9781555816513/fig16-4_thmb.gif

10.1128/9781555816513/fig16-4.gif

FIGURE 4

/content/10.1128/9781555816513.chap16.fig16-5

FIGURE 5

(See the separate color insert for the color version of this illustration.) Structure of Rel Seq 1-385. (A) ppGpp Hydrolase-OFF/synthetase-ON conformation, in complex with Mn2+ (blue sphere) and GDP (stick rendering). The hydrolase domain is highlighted in green α-helices and blue β-strands, the synthetase domain is in yellow α -helices and orange β -strands, and the central 3-helix bundle is in red. Part of the substrate-binding cleft comprising the hydrolase site (downregulated) is disordered (red arrow). The small synthetase/hydrolase interdomain contact interface involved in signal transmission is labeled with a red star. (B) Hydrolase-ON/synthetase-OFF conformation, in complex with Mn2+, ppG′:3′p (which locks the enzyme in the hydrolase-ON/synthetase-OFF conformation) and GDP. The coloring and rendering schemes are the same as for (A). The disordered synthetase site (down-regulated) is illustrated as dashed lines with a red arrow. (C) Primary and secondary structure of Rel Seq 1-385. Secondary structure is color-coded according to (A) and (B). Unique secondary structure assignments for (A) are placed immediately below the corresponding assignments for (B). Residues absolutely conserved throughout the mono- and bifunctional RelA and SpoT homologs are underlaid with blue boxes. Residues conserved in SpoT and the bifunctional enzymes but mutated in the hydrolase-incompetent RelA homologs are underlaid with red boxes. Upright and inverted black triangles above the sequence indicate residues which, when substituted experimentally by missense mutations, lead to defective hydrolase and synthetase activities, respectively. (Reproduced from reference 51 , with permission.)

10.1128/9781555816513/fig16-5_thmb.gif

10.1128/9781555816513/fig16-5.gif

FIGURE 5

References

/content/book/10.1128/9781555816513.chap16

1. Achari, A.,, S. P. Hale,, A. J. Howard,, G. M. Clore,, A. M. Gronenborn,, K. D. Hardman,, and M. Whitlow. 1992. 1.67-A X-ray structure of the B2 immunoglobulin-binding domain of streptococcal protein G and comparison to the NMR structure of the B1 domain. Biochemistry 31: 10449– 10457.

2. Akerström, B.,, E. Nielsen,, and L. Björck. 1987. Definition of IgG- and albumin-binding regions of streptococcal protein G. J. Biol. Chem. 262: 13388– 13391.

3. Anzai, T.,, J. F. Timoney,, Y. Kuwamoto,, Y. Fujita,, R. Wada,, and T. Inoue. 1999. In vivo pathogenicity and resistance to phagocytosis of Streptococcus equi strains with different levels of capsule expression. Vet. Microbiol. 67: 277– 286.

4. Artiushin, S. C.,, J. F. Timoney,, A. S. Sheoran,, and S. K. Muthupalani. 2002. Characterization and immunogenicity of pyrogenic mitogens SePE-H and SePE-I of Streptococcus equi. Microb. Pathog. 32: 71– 85.

5. Barne, K. A.,, J. A. Bown,, S. J. W. Busby,, and S. D. Minchin. 1997. Region 2.5 of the Escherichia coli RNA polymerase σ 70 subunit is responsible for the recognition of the ‘extended-10’ motif at promoters. EMBO J. 16: 4034– 4040.

6. Ben Nasr, A.,, A. Wistedt,, U. Ringdahl,, and U. Sjöbring. 1994. Streptokinase activates plasminogen bound to human group C and G streptococci through M-like proteins. Eur. J. Biochem. 222: 267– 276.

7. Bentley, R. W.,, J. A. Leigh,, and M. D. Collins. 1991. Intrageneric structure of Streptococcus based on comparative analysis of small-subunit rRNA sequences. Int. J. Syst. Bacteriol. 41: 487– 494.

8. Bert, F.,, B. Picard,, N. Lambert-Zechovsky,, and P. Goullet. 1995. Identification and typing of pyogenic streptococci by enzyme electrophoretic polymorphism. J. Med. Microbiol. 42: 442– 451.

9. Bert, F.,, B. Picard,, C. Branger,, and N. Lambert- Zechovsky. 1996. Analysis of genetic relationships among strains of groups A, C and G streptococci by random amplified polymorphic DNA analysis. J. Med. Microbiol. 45: 278– 284.

10. Bert, F.,, C. Branger,, and N. Lambert-Zechovsky. 1997. Pulsed-field gel electrophoresis is more discriminating than multilocus enzyme electrophoresis and random amplified polymorphic DNA analysis for typing pyogenic streptococci. Curr. Microbiol. 34: 226– 229.

11. Bisno, A. L.,, C. M. Collins,, and J. C. Turner,. 1997. M proteins of group C streptococci isolated from patients with acute pharyngitis, p. 745– 748. In T. Horaud,, M. Sicard,, A. Bouvet,, R. Leclerq,, and H. DeMonclos (ed.), Streptococci and the Host. Plenum Press, New York, N.Y.

12. Boxrud, P. D.,, and P. E. Bock. 2004. Coupling of conformational and proteolytic activation in the kinetic mechanism of plasminogen activation by streptokinase. J. Biol. Chem. 279: 36642– 36649.

13. Broeseker, T. A.,, M. D. Boyle,, and R. Lottenberg. 1988. Characterization of the interaction of human plasmin with its specific receptor on a group A streptococcus. Microb. Pathog. 5: 19– 27.

14. Calvinho, L. F.,, R. A. Almeida,, and S. P. Oliver. 1998. Potential virulence factors of Streptococcus dysgalactiae associated with bovine mastitis. Vet. Microbiol. 61: 93– 110.

15. Chanter, N.,, N. Collin,, N. Holmes,, M. Binns,, and J. Mumford. 1997. Characterization of the Lancefield group C streptococcus 16S-23S RNA gene intergenic spacer and its potential for identification and sub-specific typing. Epidemiol. Infect. 118: 125– 135.

16. Cleary, P. P.,, J. Peterson,, C. Chen,, and C. Nelson. 1991. Virulent human strains of group G streptococci express a C5a peptidase enzyme similar to that produced by group A streptococci. Infect. Immun. 59: 2305– 2310.

17. Cohen-Poradosu, R.,, J. Jaffe,, D. Lavi,, S. Grisariu,, R. Nir-Paz,, L. Valinsky,, M. Dan-Goor,, C. Block,, B. Beall,, and A. E. Moses. 2004. Group G streptococcal bacteremia in Jerusalem. Emerg. Infect. Dis. 10: 1455– 1460.

18. Collins, C. M.,, A. Kimura,, and A. L. Bisno. 1992. Group G streptococcal M protein exhibits structural features analogous to those of class I M protein of group A streptococci. Infect. Immun. 60: 3689– 3696.

19. Conejero-Lara, F.,, J. Parrado,, A.I. Azuaga,, C. M. Dobson,, and C. P. Ponting. 1998. Analysis of the interactions between streptokinase domains and human plasminogen. Protein Sci. 7: 2190– 2199.

20. Crater, D. L.,, and I. van de Rijn. 1995. Hyaluronic acid synthesis operon ( has) expression in group A streptococci. J. Biol. Chem. 270: 18452– 18458.

21. D’Costa, S. S.,, H. Wang,, D. W. Metzger,, and M. D. P. Boyle. 1997. Group A streptococcal isolate 64/14 expresses surface plasmin-binding structures in addition to Plr. Res. Microbiol. 148: 559– 572.

22. Derrick, J. P.,, and D. B. Wigley. 1992. Crystal structure of a streptococcal protein G domain bound to an Fab fragment. Nature 359: 752– 754.

23. Efstratiou, A. 1997. Pyogenic streptococci of Lancefield groups C and G as pathogens in man. J. Appl. Microbiol. Symp. Suppl. 83: 72S– 79S.

24. Espinosa-Urgel, M.,, and R. Kolter. 1998. Escherichia coli genes expressed preferentially in an aquatic environment. Mol. Microbiol. 28: 325– 332.

25. Facklam, R. 2002. What happened to the streptococci: overview of taxonomic and nomenclature changes. Clin. Microbiol. Rev. 15: 613– 630.

26. Fahnestock, S. R.,, P. Alexander,, J. Nagle,, and D. Filpula. 1986. Gene for an immunoglobulin-binding protein from a group G streptococcus. J. Bacteriol. 167: 870– 880.

27. Falkenberg, C.,, L. Björck,, and B. Akerström. 1992. Localization of the binding site for streptococcal protein G on human serum albumin. Identification of a 5.5-kilodalton protein G binding albumin fragment. Biochem. 31: 1451– 1457.

28. Farrow, J. A. E.,, and M. D. Collins. 1984. Taxonomic studies on streptococci of serological groups C, G and L and possibly related taxa. Syst. Appl. Microbiol. 5: 483– 493.

29. Federle, M. J.,, K. S. McIver,, and J. R. Scott. 1999. A response regulator that represses transcription of several virulence operons in the group A streptococcus. J. Bacteriol. 181: 3649– 3657.

30. Fischetti, V. A. 1989. Streptococcal M protein: molecular design and biological behavior. Clin. Microbiol. Rev. 2: 285– 314.

31. Flanagan, J.,, N. Collin,, J. Timoney,, T. Mitchell,, J. A. Mumford,, and N. Chanter. 1998. Characterization of the haemolytic activity of Streptococcus equi. Microb. Pathog. 24: 211– 221.

32. Forsman, P.,, A. Tilsala-Timisjärvi,, and T. Alatossava. 1997. Identification of staphylococcal and streptococcal causes of bovine mastitis using 16S-23S rRNA spacer regions. Microbiology 143: 3491– 3500.

33. Frank, C.,, K. Steiner,, and H. Malke. 1995. Conservation of the organization of the streptokinase gene region among pathogenic streptococci. Med. Microbiol. Immunol. 184: 139– 146.

34. Franken, C.,, G. Haase,, C. Brandt,, J. Weber-Heynemann,, S. Martin,, C. Lämmler,, A. Podbielski,, R. Lütticken,, and B. Spellerberg. 2001. Horizontal gene transfer and host specificity of beta-haemolytic streptococci: the role of a putative composite transposon containing scpB and lmb. Mol. Microbiol. 41: 925– 935.

35. Gase, K.,, T. Ellinger,, and H. Malke. 1995. Complex transcriptional control of the streptokinase gene of Streptococcus equisimilis H46A. Mol. Gen. Genet. 247: 749– 758.

36. Gase, K.,, A. Gase,, H. Schirmer,, and H. Malke. 1996. Cloning, sequencing and functional overexpression of the Streptococcus equisimilis H46A gapC gene encoding a glyceraldehyde-3-phosphate dehydrogenase that also functions as a plasmin(ogen)-binding protein: purification and biochemical characterization of the protein. Eur. J. Biochem. 239: 42– 51.

37. Gase, K.,, G. Liu,, A. Bruckmann,, K. Steiner,, J. Ozegowski,, and H. Malke. 1997. The lppC gene of Streptococcus equisimilis encodes a lipoprotein that is homologous to the e (P4) outer membrane protein from Haemophilus influenzae. Med. Microbiol. Immunol. 186: 63– 73.

38. Geyer, A.,, and K.-H. Schmidt. 2000. Genetic organization of the M protein region in human isolates of group C and G streptococci: two types of multigene regulator-like ( mgrC) regions. Mol. Gen. Genet. 262: 965– 976.

39. Geyer, A.,, A. Roth,, S. Vettermann,, E. Günther,, A. Groh,, E. Straube,, and K.-H. Schmidt. 1999. M protein of a Streptococcus dysgalactiae human wound isolate shows multiple binding to different plasma proteins and shares epitopes with keratin and human cartilage. FEMS Immunol. Med. Microbiol. 26: 11– 24.

40. Gillespie, B. E.,, B. M. Jayarao,, and S. P. Oliver. 1997. Identification of Streptococcus species by randomly amplified polymorphic deoxyribonucleic acid fingerprinting. J. Dairy Sci. 80: 471– 476.

41. Gladysheva, I. P.,, R. B. Turner,, I. Y. Sazonova,, L. Liu,, and G. L. Reed. 2003. Coevolutionary patterns in plasminogen activation. Proc. Natl. Acad. Sci. USA 100: 9168– 9172.

42. Gräfe, S.,, T. Ellinger,, and H. Malke. 1996. Structural dissection and functional analysis of the complex promoter of the streptokinase gene from Streptococcus equisimilis H46A. Med. Microbiol. Immunol. 185: 11– 17.

43. Gronenborn, A. M.,, and G. M. Clore. 1993. Identification of the contact surface of a streptococcal protein G domain complexed with a human Fc fragment. J. Molec. Biol. 233: 331– 335.

44. Gronenborn, A. M.,, D. R. Filpula,, N. Z. Essig,, A. Achari,, M. Whitlow,, P. T. Wingfield,, and G. M. Clore. 1991. A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G. Science 253: 657– 660.

45. Gross, S.,, K. Gase,, and H. Malke. 1996. Localization of the sequence-determined DNA bending center upstream of the streptokinase gene skc. Arch. Microbiol. 166: 116– 121.

46. Guss, B.,, M. Eliasson,, A. Olsson,, M. Uhlén,, A. K. Frej,, H. Jörnvall,, J. I. Flock,, and M. Lindberg. 1986. Structure of the IgG-binding regions of streptococcal protein G. EMBO J. 5: 1567– 1575.

47. Hamilton, A.,, D. Harrington,, and I. C. Sutcliffe. 2000. Characterization of acid phosphatase activities in the equine pathogen Streptococcus equi. Syst. Appl. Microbiol. 23: 325– 329.

48. Hashikawa, S.,, Y. Iinuma,, M. Furushita,, T. Ohkura,, T. Nada,, K. Torii,, T. Hasegawa,, and M. Ohta. 2004. Characterization of group C and G streptococcal strains that cause streptococcal toxic shock syndrome. J. Clin. Microbiol. 42: 186– 192.

49. Hassan, A. A.,, I. U. Khan,, A. Abdulmawjood,, and C. Lämmler. 2003. Inter- and intraspecies variations of the 16S-23S rDNA intergenic spacer region of various streptococcal species. Syst. Appl. Microbiol. 26: 97– 103.

50. Heldermon, C.,, P. L. DeAngelis,, and P. H. Weigel. 2001. Topological organization of the hyaluronan synthase from Streptococcus pyogenes. J. Biol. Chem. 276: 2037– 2046.

51. Hogg, T.,, U. Mechold,, H. Malke,, M. Cashel,, and R. Hilgenfeld. 2004. Conformational antagonism between opposing active sites in a bifunctional RelA/SpoT homolog modulates (p)ppGpp metabolism during the stringent response. Cell 117: 57– 68.

52. House-Pompeo, K.,, Y. Xu,, D. Joh,, P. Speziale,, and M. Höök. 1996. Conformational changes in the fibronectin binding MSCRAMMs are induced by ligand binding. J. Biol. Chem. 271: 1379– 1384.

53. Humar, D.,, V. Datta,, D. J. Bast,, B. Beall,, J. C. Azavedo,, and V. Nizet. 2002. Streptolysin S and necrotising infections produced by group G streptococcus. Lancet 359: 124– 129.

54. Ikebe, T.,, S. Murayama,, K. Saitoh,, S. Yamai,, R. Suzuki,, J. Isobe,, D. Tanaka,, C. Katsukawa,, A. Tamaru,, A. Katayama,, Y. Fujinaga,, K. Hoashi,, and H. Watanabe. 2004. Surveillance of severe invasive group-G streptococcal infections and molecular typing of the isolates in Japan. Epidemiol. Infect. 132: 145– 149.

55. Jackson, K. W.,, H. Malke,, D. Gerlach,, J. J. Ferretti,, and J. Tang. 1986. Active streptokinase from the cloned gene in Streptococcus sanguis is without the carboxyl-terminal 32 residues. Biochemistry 25: 108– 114.

56. Jaffe, J.,, S. Natanson-Yaron,, M. G. Caparon,, and E. Hanski. 1996. Protein F2, a novel fibronectin-binding protein from Streptococcus pyogenes, possesses two binding domains. Mol. Microbiol. 21: 373– 384.

57. Joh, H. J.,, K. House-Pompeo,, J. M. Patti,, S. Gurusiddappa,, and M. Höök. 1994. Fibronectin receptors from gram-positive bacteria: comparison of active sites. Biochemistry 33: 6086– 6092.

58. Joh, D.,, P. Speziale,, S. Gurusiddappa,, J. Manor,, and M. Höök. 1998. Multiple specificities of the staphylococcal and streptococcal fibronectin-binding microbial surface components recognizing adhesive matrix molecules. Eur. J. Biochem. 258: 897– 905.

59. Jonsson, H.,, and H. P. Müller. 1994. The type-III Fc receptor from Streptococcus dysgalactiae is also an α 2-macroglobulin receptor. Eur. J. Biochem. 220: 819– 826.

60. Jonsson, H.,, L. Frykberg,, L. Rantamäki,, and B. Guss. 1994. MAG, a novel plasma protein receptor from Streptococcus dysgalactiae. Gene 143: 85– 89.

61. Jonsson, H.,, C. Burtsoff-Asp,, and B. Guss. 1995. Streptococcal protein MAG—a protein with broad albumin binding specificity. Biochim. Biophys. Acta 1249: 65– 71.

62. Jonsson, H.,, H. Lindmark,, and B. Guss. 1995. A protein G-related cell surface protein in Streptococcus zooepidemicus. Infect. Immun. 63: 2968– 2975.

63. Jorm, L. R.,, D. N. Love,, G. D. Bailey,, G. M. McKay,, and D. A. Briscoe. 1994. Genetic structure of populations of β-haemolytic Lancefield group C streptococci from horses and their association with disease. Res. Vet. Sci. 57: 292– 299.

64. Kakizaki, I.,, K. Takagaki,, Y. Endo,, D. Kudo,, H. Ikeya,, T. Miyoshi,, B.A. Baggenstoss,, V.L. Tlapak-Simmons,, K. Kumari,, A. Nakane,, P.H. Weigel,, and M. Endo. 2002. Inhibition of hyaluronan synthesis in Streptococcus equi FM100 by 4-methylumbelliferone. Eur. J. Biochem. 269: 5066– 5075.

65. Kalia, A.,, and D. E. Bessen. 2003. Presence of streptococcal pyrogenic exotoxin A and C genes in human isolates of group G streptococci. FEMS Microbiol. Lett. 219: 291– 295.

66. Kalia, A.,, and D. E. Bessen. 2004. Natural selection and evolution of streptococcal virulence genes involved in tissue-specific adaptations. J. Bacteriol. 186: 110– 121.

67. Kalia, A.,, M. C. Enright,, B. G. Spratt,, and D. E. Bessen. 2001. Directional gene movement from human-pathogenic to commensal-like streptococci. Infect. Immun. 69: 4858– 4869.

68. Kawamura, Y.,, X. G. Hou,, F. Sultana,, H. Miura,, and T. Ezaki. 1995. Determination of 16S rRNA sequences of Streptococcus mitis and Streptococcus gordonii and phylogenetic relationships among members of the genus Streptococcus. Int. J. Syst. Bacteriol. 45: 406– 408.

69. Klessen, C.,, K. H. Schmidt,, J. J. Ferretti,, and H. Malke. 1988. Tripartite streptokinase gene fusion vectors for gram-positive and gram-negative procaryotes. Mol. Gen. Genet. 212: 295– 300.

70. Kline, J. B.,, S. Xu,, A. L. Bisno,, and C. M. Collins. 1996. Identification of a fibronectin-binding protein (GfbA) in pathogenic group G streptococci. Infect. Immun. 64: 2122– 2129.

71. Kreikemeyer, B.,, M. D. P. Boyle,, B. A. Leonard Buttaro,, M. Heinemann,, and A. Podbielski. 2001. Group A streptococcal growth phase-associated virulence factor regulation by a novel operon (Fas) with homologies to two-component-type regulators requires a small RNA molecule. Mol. Microbiol. 39: 392– 406.

72. Kumar, S.,, K. Tamura,, I. B. Jakobsen,, and M. Nei. 2001. MEGA2: molecular evolutionary genetics analysis software. Bioinformatics 17: 1244– 1245.

73. Kumari, K.,, and P. H. Weigel. 1997. Molecular cloning, expression, and characterization of the authentic hyaluronan synthase from group C Streptococcus equisimilis. J. Biol. Chem. 272: 32539– 32546.

74. Kumari, K.,, V. L. Tlapak-Simmons,, B. A. Baggenstoss,, and P. H. Weigel. 2002. The streptococcal hyaluronan synthases are inhibited by sulfhydryl-modifying reagents, but conserved cysteine residues are not essential for enzyme function. J. Biol. Chem. 277: 13943– 13951.

75. Leigh, J. A.,, S. M. Hodgkinson,, and R. A. Lincoln. 1998. The interaction of Streptococcus dysgalactiae with plasmin and plasminogen. Vet. Microbiol. 61: 121– 135.

76. Lejon, S.,, I.-M. Frick,, L. Björck,, M. Wikström,, and S. Svensson. 2004. Crystal structure and biological implications of a bacterial albumin-binding module in complex with human serum albumin. J. Biol. Chem. 279: 42924– 42928.

77. Lindgren, P. E.,, P. Speziale,, M. McGavin,, H. J. Monstein,, M. Höök,, L. Visai,, T. Kostiainen,, S. Bozzini,, and M. Lindberg. 1992. Cloning and expression of two different genes from Streptococcus dysgalactiae encoding fibronectin receptors. J. Biol. Chem. 267: 1924– 1931.

78. Lindgren, P. E.,, M. J. McGavin,, C. Signäs,, B. Guss,, S. Gurusiddappa,, M. Höök,, and M. Lindberg. 1993. Two different genes coding for fibronectin-binding proteins from Streptococcus dysgalactiae: the complete nucleotide sequences and characterization of the binding domains. Eur. J. Biochem. 214: 819– 827.

79. Lindgren, P. E.,, C. Signäs,, L. Rantamäki,, and M. Lindberg. 1994. A fibronectin-binding protein from Streptococcus equisimilis: characterization of the gene and identification of the binding domain. Vet. Microbiol. 41: 235– 247.

80. Lindmark, H.,, and B. Guss. 1999. SFS, a novel fibronectin-binding protein from Streptococcus equi, inhibits the binding between fibronectin and collagen. Infect. Immun. 67: 2383– 2388.

81. Lindmark, H.,, K. Jacobsson,, L. Frykberg,, and B. Guss. 1996. Fibronectin-binding protein of Streptococcus equi subsp. zooepidemicus. Infect. Immun. 64: 3993– 3999.

82. Lindmark, H.,, M. Nilsson,, and B. Guss. 2001. Comparison of the fibronectin-binding protein FNE from Streptococcus equi subspecies equi with FNZ from Streptococcus equi subspecies zooepidemicus reveals a major and conserved difference. Infect. Immun. 69: 3159– 3163.

83. Lottenberg, R.,, C. C. Broder,, M. D. Boyle,, S. J. Kain,, B. L. Schroeder,, and R. Curtiss III. 1992. Cloning, sequence analysis, and expression in Escherichia coli of a streptococcal plasmin receptor. J. Bacteriol. 174: 5204– 5210.

84. Loy, J. A.,, X. Lin,, M. Schenone,, F. J. Castellino,, X. C. Zhang,, and J. Tang. 2001. Domain interactions between streptokinase and human plasminogen. Biochemistry 40: 14686– 14695.

85. Malke, H. 1998. Cytoplasmic membrane lipoprotein LppC of Streptococcus equisimilis functions as an acid phosphatase. Appl. Environ. Microbiol. 64: 2439– 2442.

86. Malke, H.,, and J. J. Ferretti. 1984. Streptokinase: cloning, expression, and excretion by Escherichia coli. Proc. Natl. Acad. Sci. USA 81: 3557– 3561.

87. Malke, H.,, and J. J. Ferretti,. 1991. Expression and properties of hybrid streptokinases extended by N-terminal plasminogen kringle domains, p. 184– 189. In G. M. Dunny,, P. P. Cleary,, and L. L. McKay (ed.), Genetics and Molecular Biology of Streptococci, Lactococci, and Enterococci. American Society for Microbiology, Washington, D.C.

88. Malke, H.,, and K. Steiner,. 2000. Functional properties of the cytoplasmic membrane lipoprotein acid phosphatase of Streptococcus dysgalactiae subsp. equisimilis, p. 879– 883. In D. R. Martin, and J. R. Tagg (ed.), Streptococci and Streptococcal Diseases—Entering the New Millennium. Securacopy, Porirua, New Zealand.

89. Malke, H.,, and K. Steiner. 2004. Control of streptokinase gene expression in group A & C streptococci by two-component regulators. Indian J. Med. Res. 119(Suppl.): 4– 56.

90. Malke, H.,, D. Lorenz,, and J. J. Ferretti,. 1987. Streptokinase: expression of altered forms, p. 143– 149. In J. J. Ferretti, and R. Curtiss III (ed.), Streptococcal Genetics. American Society for Microbiology, Washington, D.C.

91. Malke, H.,, B. Roe,, and J. J. Ferretti. 1985. Nucleotide sequence of the streptokinase gene from Streptococcus equisimilis H46A. Gene 34: 357– 362.

92. Malke, H.,, U. Mechold,, K. Gase,, and G. Gerlach. 1994. Inactivation of the streptokinase gene prevents Streptococcus equisimilis H46A from acquiring cell-associated plasmin activity in the presence of plasminogen. FEMS Microbiol. Lett. 116: 107– 112.

93. Malke, H.,, K. Steiner,, K. Gase,, U. Mechold,, and T. Ellinger. 1995. The streptokinase gene: allelic variation, genomic environment, and expression control. Dev. Biol. Stand. 85: 183– 193.

94. Malke, H.,, K. Steiner,, K. Gase,, and C. Frank. 2000. Expression and regulation of the streptokinase gene. Methods 21: 111– 124.

95. Martin, N. J.,, E. L. Kaplan,, M. A. Gerber,, M. A. Menegus,, M. Randolph,, K. Bell,, and P. P. Cleary. 1990. Comparison of epidemic and endemic group G streptococci by restriction enzyme analysis. J. Clin. Microbiol. 28: 1881– 1886.

96. McGavin, M.,, S. Gurusiddappa,, P. E. Lindgren,, M. Lindberg,, G. Raucci,, and M. Höök. 1993. Fibronectin receptors from Streptococcus dysgalactiae and Staphylococcus aureus. J. Biol. Chem. 268: 23946– 23953.

97. Mechold, U.,, and H. Malke. 1997. Characterization of the stringent and relaxed responses of Streptococcus equisimilis. J. Bacteriol. 179: 2658– 2667.

98. Mechold, U.,, K. Steiner,, S. Vettermann,, and H. Malke. 1993. Genetic organization of the streptokinase region of the Streptococcus equisimilis H46A chromosome. Mol. Gen. Genet. 241: 129– 140.

99. Mechold, U.,, M. Cashel,, K. Steiner,, D. Gentry,, and H. Malke. 1996. Functional analysis of a relA/spoT gene homolog from Streptococcus equisimilis. J. Bacteriol. 178: 1401– 1411.

100. Mechold, U.,, H. Murphy,, L. Brown,, and M. Cashel. 2002. Intramolecular regulation of the opposing (p)ppGpp catalytic activities of Rel Seq, the Rel/Spo enzyme from Streptococcus equisimilis. J. Bacteriol. 184: 2878– 2888.

101. Meehan, M.,, P. Nowlan,, and P. Owen. 1998. Affinity purification and characterization of a fibrinogen-binding protein complex which protects mice against lethal challenge with Streptococcus equi subsp. equi. Microbiology 144: 993– 1003.

102.. Meehan, M.,, D. A. Muldowney,, N. J. Watkins,, and P. Owen. 2000. Localization and characterization of the ligand-binding domain of the fibrinogen-binding protein (FgBP) of Streptococcus equi subsp. equi. Microbiology 146: 1187– 1194.

103. Meehan, M.,, Y. Lynagh,, C. Woods,, and P. Owen. 2001. The fibrinogen-binding protein (FgBP) of Streptococcus equi subsp. equi additionally binds IgG and contributes to virulence in a mouse model. Microbiology 147: 3311– 3322.

104. Meehan, M.,, S. M. Kelly,, N. C. Price,, and P. Owen. 2002. The C-terminal portion of the fibrinogen-binding protein of Streptococcus equi subsp. equi contains extensive α-helical coiled-coil structure and contributes to thermal stability. FEMS Microbiol. Lett. 206: 81– 86.

105. Molinari, G.,, and G. S. Chhatwal. 1999. Streptococcal invasion. Curr. Opin. Microbiol. 2: 56– 61.

106. Müller, H.-P., and L. K. Rantamäki. 1995. Binding of native alpha 2-macroglobulin to human group G streptococci. Infect. Immun. 63: 2833– 2839.

107. Nicholson, M. L.,, L. Ferdinand,, J. S. Sampson,, A. Benin,, S. Balter,, S. W. L. Pinto,, S. F. Dowell,, R. R. Facklam,, G. M. Carlone,, and B. Beall. 2000. Analysis of immune-reactivity to a Streptococcus equi subsp. zooepidemicus M-like protein to confirm an outbreak of poststreptococcal glomerulonephritis, and sequences of M-like proteins from isolates obtained from different host species. J. Clin. Microbiol. 38: 4126– 4130.

108. Nickel, V.,, S. Prehm,, M. Lansing,, A. Mausolf,, A. Podbielski,, J. Deutscher,, and P. Prehm. 1998. An ectoprotein kinase of group C streptococci binds hyaluronan and regulates capsule formation. J. Biol. Chem. 273: 23668– 23673.

109. Nikolskaya, A. N.,, and M. Y. Galperin. 2002. A novel type of conserved DNA-binding domain in the transcriptional regulators of the AlgR/AgrA/LytR family. Nucleic Acids Res. 30: 2453– 2459.

110. Nowicki, S. T.,, D. Minning-Wenz,, K. H. Johnston,, and R. Lottenberg. 1994. Characterization of a novel streptokinase produced by Streptococcus equisimilis of non-human origin. Thromb. Haemost. 72: 595– 603.

111. Nygren, P. A.,, C. Ljungquist,, H. Thromborg,, K. Nustad,, and M. Uhlén. 1990. Species-dependent binding of serum albumins to the streptococcal receptor protein G. Eur. J. Biochem. 193: 143– 148.

112. Okumura, K.,, A. Hara,, T. Tanaka,, I. Nishiguchi,, W. Minamide,, H. Igarashi,, and T. Yutsudo. 1994. Cloning and sequencing the streptolysin O genes of group C and group G streptococci. DNA Sequence 4: 325– 328.

113. Oliver, S. P.,, B. E. Gillespie,, and B. M. Jayarao. 1998. Detection of new and persistent Streptococcus uberis and Streptococcus dysgalactiae intramammary infections by polymerase chain reaction-based DNA fingerprinting. FEMS Microbiol. Lett. 160: 69– 73.

114. Olsson, A.,, M. Eliasson,, B. Guss,, B. Nilsson,, U. Hellman,, M. Lindberg,, and M. Uhlén. 1987. Structure and evolution of the repetitive gene encoding streptococcal protein G. Eur. J. Biochem. 168: 319– 324.

115. O’Neil, K. T.,, R. H. Hoess,, D. P. Raleigh,, and W. F. DeGrado. 1995. Thermodynamic genetics of the folding of the B1 immunoglobulin-binding domain from streptococcal protein G. Proteins 21: 11– 21.

115a.. Ouskova, G.,, B. Spellerberg,, and P. Prehm. 2004. Hyaluronan release from Streptococcus pyogenes: export by an ABC transporter. Glycobiology 14: 931– 938.

116. Pancholi, V.,, and V. A. Fischetti. 1992. A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity. J. Exp. Med. 176: 415– 426.

117. Pancholi, V.,, and V. A. Fischetti. 1998. α-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci. J. Biol. Chem. 273: 14503– 14515.

118. Parrado, J.,, F. Conejero-Lara,, R. A. G. Smith,, J. M. Marshall,, C. P. Ponting,, and C. M. Dobson. 1996. The domain organization of streptokinase: nuclear magnetic resonance, circular dichroism, and functional characterization of proteolytic fragments. Protein Sci. 5: 693– 704.

119. Perederina, A.,, V. Svetlov,, M. N. Vassylyeva,, T. H. Tahirov,, S. Yokoyama,, I. Artsimovitch,, and D. G. Vassylyev. 2004. Regulation through the secondary channel—structural framework for ppGpp-DksA synergism during transcription. Cell 118: 297– 309.

120. Podbielski, A.,, B. Melzer,, and R. Lütticken. 1991. Application of the polymerase chain reaction to study the M protein(-like) gene family in beta-hemolytic streptococci. Med. Microbiol. Immunol. 180: 213– 227.

121. Podbielski, A.,, I. Zagres,, A. Flosdorff,, and J. Weber-Heynemann. 1996. Molecular characterization of a major serotype M49 group A streptococcal DNase gene ( sdaD). Infect. Immun. 64: 5349– 5356.

122. Poyart, C.,, G. Quesne,, S. Coulon,, P. Berche,, and P. Trieu-Cuot. 1998. Identification of streptococci to species level by sequencing the gene encoding the manganese-dependent superoxide dismutase. J. Clin. Microbiol. 36: 41– 47.

123. Proft, T.,, P. D. Webb,, V. Handley,, and J. D. Fraser. 2003. Two novel superantigens found in both group A and group C Streptococcus. Infect. Immun. 71: 1361– 1369.

124. Rasmussen, M.,, H.-P. Müller,, and L. Björck. 1999. Protein GRAB of Streptococcus pyogenes regulates proteolysis at the bacterial surface by binding α 2-macroglobulin. J. Biol. Chem. 274: 15336– 15344.

125. Reilly, T. J.,, B. A. Green,, G. W. Zlotnick,, and A. L. Smith. 2001. Contribution of the DDDD motif of Haemophilus influenzae e(P4) to phosphomonoesterase activity and heme transport. FEBS Lett. 494: 19– 23.

126. Sachse, S.,, P. Seidel,, D. Gerlach,, E. Günther,, J. Rödel,, E. Straube,, and K.-H. Schmidt. 2002. Superantigen-like gene(s) in human pathogenic Streptococcus dysgalactiae subsp. equisimilis: genomic localisation of the gene encoding streptococcal pyrogenic exotoxin G ( speGdys). FEMS Immunol. Med. Microbiol. 34: 159– 167.

127. Schnitzler, N.,, A. Podbielski,, G. Baumgarten,, M. Mignon,, and A. Kaufhold. 1995. M or M-like protein gene polymorphisms in human group G streptococci. J. Clin. Microbiol. 33: 356– 363.

128. Schnitzler, N.,, G. Haase,, A. Podbielski,, A. Kaufhold,, C. Lämmler,, and R. Lütticken,. 1997. Human isolates of large colony-forming β-hemolytic group G streptococci form a distinct clade upon 16S rRNA gene analysis, p. 363– 365. In T. Horaud,, A. Bouvet,, R. Leclercq,, H. de Montclos,, and M. Sicard (ed.), Streptococci and the Host. Plenum Press, New York, N.Y.

129. Sharma, M.,, R. Khatib,, and M. Fakih. 2002. Clinical characteristics of necrotizing fasciitis by group G Streptococcus: case report and review of the literature. Scand. J. Infect. Dis. 34: 468– 471.

130. Schwarz-Linek, U.,, M. Höök,, and J. R. Potts. 2004. The molecular basis of fibronectin-mediated bacterial adherence to host cells. Mol. Microbiol. 52: 631– 641.

131. Sheinerman, F. B.,, and C. L. Brooks. 1998. Calculations on folding of segment B1 of streptococcal protein G. J. Molec. Biol. 278: 439– 456.

132. Sheoran, A. S.,, B. T. Sponseller,, M. A. Holmes,, and J. F. Timoney. 1997. Serum and mucosal antibody isotype responses to M-like protein (SeM) of Streptococcus equi in convalescent and vaccinated horses. Vet. Immunol. Immunopathol. 59: 239– 251.

133. Simpson, W. J.,, J. C. Robbins,, and P. P. Cleary. 1987. Evidence for group A-related M protein genes in human but not animal-associated group G streptococcal pathogens. Microb. Pathog. 3: 339– 350.

134. Simpson, W. J.,, J. M. Musser,, and P. P. Cleary. 1992. Evidence consistent with horizontal transfer of the gene ( emm12) encoding serotype M12 protein between group A and group G pathogenic streptococci. Infect. Immun. 60: 1890– 1893.

135. Sing, A.,, K. Trebesius,, and J. Heesemann. 2001. Diagnosis of Streptococcus dysgalactiae subsp. equisimilis (group C streptococci) associated with deep soft tissue infections using fluorescent in situ hybridization. Eur. J. Clin. Microbiol. Infect Dis. 20: 146– 149.

136. Skjold, S. A.,, H. Malke,, and L. W. Wannamaker,. 1979. Transduction of plasmid-mediated erythromycin resistance between group-A and -G streptococci, p. 274– 275. In M. T. Parker (ed.), Pathogenic Streptococci, Reedbooks Ltd., Chertsey, Surrey, England.

137. Song, X. M.,, J. Perez-Casal,, and A. A. Potter. 2004. The Mig protein of Streptococcus dysgalactiae inhibits bacterial internalization into bovine mammary gland epithelial cells. FEMS Microbiol. Lett. 231: 33– 38.

138. Speziale, P.,, D. Joh,, L. Visai,, S. Bozzini,, K. House-Pompeo,, M. Lindberg,, and M. Höök. 1996. A monoclonal antibody enhances ligand binding of fibronectin MSCRAMM (adhesin) from Streptococcus dysgalactiae. J. Biol. Chem. 271: 1371– 1378.

139. Sriprakash, K. S.,, and J. Hartas. 1996. Lateral genetic transfers between group A and G streptococci for M-like genes are ongoing. Microb. Pathog. 20: 275– 285.

140. Steiner, K.,, and H. Malke. 1995. Transcription termination of the streptokinase gene of Streptococcus equisimilis H46A: bidirectionality and efficiency in homologous and heterologous hosts. Molec. Gen. Genet. 246: 374– 380.

141. Steiner, K.,, and H. Malke. 1997. Primary structure requirements for in vivo activity and bidirectional function of the transcription terminator shared by the oppositely oriented skc/rel-orf1 genes of Streptococcus equisimilis. Molec. Gen. Genet. 255: 611– 618.

142. Steiner, K.,, and H. Malke. 2000. Life in protein-rich environments: the relA-independent response of Streptococcus pyogenes to amino acid starvation. Mol. Microbiol. 38: 1004– 1016.

143. Steiner, K.,, and H. Malke. 2001. relA-independent amino acid starvation response network of Streptococcus pyogenes. J. Bacteriol. 183: 7354– 7364.

144. Steiner, K.,, and H. Malke. 2002. Dual control of streptokinase and streptolysin S production by the covRS and fasCAX two-component regulators in Streptococcus dysgalactiae subsp. equisimilis. Infect. Immun. 70: 3627– 3636.

145. Sultana, F.,, Y. Kawamura,, X. G. Hou,, S. E. Shu,, and T. Ezaki. 1998. Determination of 23S rRNA sequences from members of the genus Streptococcus and characterization of genetically distinct organisms previously identified as members of the Streptococcus anginosus group. FEMS Microbiol. Lett. 158: 223– 230.

145a.. Sumby, P.,, K. D. Barbian,, D. J. Gardner,, A. R. Whitney,, D. M. Welty,, R. D. Long,, J. R. Bailey,, M. J. Parnell,, N. P. Hoe,, and G. G. Adams,, F. R. DeLeo,, and J. M. Musser. 2005. Extracellular deoxyribonuclease made by group A Streptococcus assists pathogenesis by enhancing evasion of the innate immune response. Proc. Natl. Acad. Sci. USA 102: 1679– 1684.

145b.. Sun, H.,, U. Ringdahl,, J. W. Homeister,, W. P. Fay,, N. C. Engleberg,, A. Y. Yang,, L. S. Rozek,, X. Wang,, U. Sjöbring,, and D. Ginsburg. 2004. Plasminogen is a critical host pathogenicity factor for group A streptococcal infection. Science 305: 1283– 1286.

146. Talay, S. R.,, M. P. Grammel,, and G. S. Chhatwal. 1996. Structure of a group C streptococcal protein that binds to fibrinogen, albumin and immunoglobulin G via overlapping modules. Biochem. J. 315: 577– 582.

147. Timoney, J. F. 2004. The pathogenic equine streptococci. Vet. Res. 35: 397– 409.

148. Timoney, J. F.,, J. Walker,, M. Zhou,, and J. Ding. 1995. Cloning and sequence analysis of a protective M-like protein gene from Streptococcus equi subsp. zooepidemicus. Infect. Immun. 63: 1440– 1445.

149. Timoney, J. F.,, S. C. Artiushin,, and J. S. Boschwitz. 1997. Comparison of the sequences and functions of Streptococcus equi M-like proteins SeM and SzPSe. Infect. Immun. 65: 3600– 3605.

150. Tlapak-Simmons, V. L.,, B. A. Baggenstoss,, T. Clyne,, and P. H. Weigel. 1999. Purification and lipid dependence of the recombinant hyaluronan synthases from Streptococcus pyogenes and Streptococcus equisimilis. J. Biol. Chem. 274: 4239– 4245.

151. Tlapak-Simmons, V. L.,, B. A. Baggenstoss,, K. Kumari,, C. Heldermon,, and P. H. Weigel. 1999. Kinetic characterization of the recombinant hyaluronan synthases from Streptococcus pyogenes and Streptococcus equisimilis. J. Biol. Chem. 274: 4246– 4253.

152. Tlapak-Simmons, V. L.,, C. A. Baron,, and P. H. Weigel. 2004. Characterization of the purified hyaluronan synthase from Streptococcus equisimilis. Biochemistry 43: 9234– 9242.

153. Ullberg, M.,, I. Karlsson,, B. Wiman,, and G. Kronvall. 1992. Two types of receptors for human plasminogen on group G streptococci. Acta Pathol. Microbiol. Immunol. Scand. 100: 21– 28.

154. Valentin-Weigand, P.,, M. Y. Traore,, H. Blobel,, and G. S. Chhatwal. 1990. Role of α 2-macroglobulin in phagocytosis of group A and C streptococci. FEMS Microbiol. Lett. 70: 321– 324.

155. Vandamme, P.,, B. Pot,, E. Falsen,, K. Kersters,, and L. A. Devriese. 1996. Taxonomic study of Lancefield streptococcal groups C, G, and L ( Streptococcus dysgalactiae) and proposal of S. dysgalactiae subsp. equisimilis subsp. nov. Int. J. System. Bacteriol. 46: 774– 781.

156. Vasi, J.,, L. Frykberg,, L. E. Carlsson,, M. Lindberg,, and B. Guss. 2000. M-like proteins of Streptococcus dysgalactiae. Infect. Immun. 68: 294– 302.

157. Vieira, V. V.,, L. M. Teixeira,, V. Zahner,, H. Momen,, R. R. Facklam,, A. G. Steigerwalt,, D. J. Brenner,, and A. C. Castro. 1998. Genetic relationships among the different phenotypes of Streptococcus dysgalactiae strains. Int. J. Syst. Bacteriol. 48: 1231– 1243.

158. Visai, L.,, E. De Rossi,, V. Valtulina,, F. Casolini,, S. Rindi,, P. Guglierame,, G. Pietrocola,, V. Bellotti,, G. Riccardi,, and P. Speziale. 2003. Identification and characterization of a new ligand-binding site in FnbB, a fibronectin-binding adhesin from Streptococcus dysgalactiae. Biochim. Biophys. Acta 1646: 173– 183.

159. Walter, F.,, M. Siegel,, and H. Malke. 1989. Nucleotide sequence of the streptokinase gene from a group G Streptococcus. Nucleic Acids Res. 17: 1262.

160. Wang, X.,, X. Lin,, J. A. Loy,, J. Tang,, and X. C. Zhang. 1998. Crystal structure of the catalytic domain of human plasmin complexed with streptokinase. Science 281: 1662– 1665.

161. Wannamaker, L. W.,, S. Almquist,, and S. Skjold. 1973. Intergroup phage reactions and transduction between group C and group A streptococci. J. Exp. Med. 137: 1338– 1353.

162. Ward, P. N.,, T. R. Field,, W. G. F. Ditcham,, E. Maguin,, and J. A. Leigh. 2001. Identification and disruption of two discrete loci encoding hyaluronic acid capsule bio-synthesis genes hasA, hasB, and hasC in Streptococcus uberis. Infect. Immun. 69: 392– 399.

163. Wolinowska, R.,, P. Ceglowski,, J. Kok,, and G. Venema. 1991. Isolation, sequence and expression in Escherichia coli, Bacillus subtilis and Lactococcus lactis of the Dnase (streptodornase)-encoding gene from Streptococcus equisimilis H46A. Gene 106: 115– 119.

164. Woo, P. C. Y.,, A. M. Y. Fung,, S. K. P. Lau,, S. S. Y. Wong,, and K.-Y. Yuen. 2001. Group G beta-hemolytic streptococcal bacteremia characterized by 16S ribosomal RNA sequencing. J. Clin. Microbiol. 39: 3147– 3155.

165. Zaoutis, T.,, M. Attia,, R. Gross,, and J. Klein. 2004. The role of group C and group G streptococci in acute pharyngitis in children. Clin. Microbiol. Infect. 10: 37– 40.

166. Zhai, P.,, N. Wakeham,, J. A. Loy,, and X. C. Zhang. 2003. Functional roles of streptokinase C-terminal flexible peptide in active site formation and substrate recognition in plasminogen activation. Biochemistry 42: 114– 120.

Tables

Genetics and Pathogenicity Factors of Group C and G Streptococci

/content/10.1128/9781555816513.chap16.tab16-1

TABLE 1

Classification of GCS and GGS a

a Adapted from references cited in the text.

b Uncommonly, this subspecies may also comprise serogroup A and L strains and may also be found in animals.

10.1128/9781555816513/tab16-1_thmb.gif

10.1128/9781555816513/tab16-1.gif

TABLE 1

Classification of GCS and GGS a

a Adapted from references cited in the text.

b Uncommonly, this subspecies may also comprise serogroup A and L strains and may also be found in animals.