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

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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 “” 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 subsp. .

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
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Image of FIGURE 1

Schematic representation of the domain organization of protein G. S, signal sequence; E, α-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 )

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
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Image of FIGURE 2

Organization of the streptokinase-M protein gene region in the subsp. H46A chromosome based on references and . Arrows represent the genes and their orientation: , ribonucleotide reductase; , multigene regulator of GCS; , M protein; , 2′,3′-cyclic nucleotide 2′-phosphodiesterase; , bifunctional (p)ppGppase and (p)ppGpp synthetase; , D-tyrosyl-tRNATyr deacylase; , streptokinase; , leucine-rich protein of unknown function; , ATP-binding cassette transporter; , α-glucosidase.

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
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Image of FIGURE 3

Sequence comparison of and σ factors ( ) 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 as contacting the TG extension of the −10 promoter hexamer are indicated by open boxes.

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
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Image of FIGURE 4

Bootstrapped (1,000 trials) neighbor-joining phylogenetic tree of the FasA-BlpRComE family of streptococcal response regulators graphed by the MEGA2 software ( ) based on ClustalX multiple alignment (http://www.ncbi.nlm.nih.gov). Species abbreviations and sources of the proteins are as follows: Sag1, , AF390107; San1, , AJ000864; Sau1, identical to AgrA from , AY082629; Sdy1, subsp. , AY075107; Seq1, Seq2, Seq3, subsp. , http://www.sanger.ac.uk/Projects/S_equi; Sgo1, , http://www.tigr.org/tdb/mdb/mdbinprogress.html; Sgo2, X98109; Sin1, , AF498313; Smi1, , AJ000871; Smi2, http://www.tigr.org/tdb/mdb/mdbinprogress.html; Smu1, , AE015016; Sor1, , AJ240794; Spn1, , AJ278302; Spn2, AJ240793; Spy1, , AE009971; Spy2, AE009991; Sso1, Sso2, , http://www.tigr.org/tdb/mdb/mdbinprogress.html; Ssu1, , AY125957; Sub1, , http://www.sanger.ac.uk/Projects/S_uberis; Szo1, Szo2, subsp. , 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 , 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.

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
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Image of FIGURE 5

() Structure of Rel1-385. (A) ppGpp Hydrolase-OFF/synthetase-ON conformation, in complex with Mn (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 Mn, 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 Rel1-385. 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 , with permission.)

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
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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.


Generic image for table

Classification of GCS and GGS

Adapted from references cited in the text.

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

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

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