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Chapter 11 : Early Events in the Pathogenesis of Disease

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Abstract:

Historically, type b has been a leading cause of bacterial meningitis and other systemic diseases in infants and young children. Disease caused by is believed to begin with colonization of the upper respiratory mucosa. This chapter reviews the current understanding of hemagglutinating pili and the nontypeable high-molecular-weight adhesive proteins. It examines a set of diverse biogroup aegyptius strains, including the Brazilian purpuric fever case clone. Initial analysis including electron microscopy and assessment of hemagglutinating ability demonstrated that 50% of these strains were piliated. Analysis of the nucleotide sequence of the pilin genes reveals that they are highly homologous to one another. In general, the assembly and surface localization of pili requires multiple genes which are clustered together on the bacterial chromosome. More recently, van Ham et al. reported that the promoter regions of the divergently transcribed structural pilin and genes overlap; the area of overlap contains a variable number of TA repeats. On the basis of their derived amino acid sequences, both high-molecular-weight (HMW)-1 and HMW- 2 show sequence similarity to filamentous hemagglutinin, a critical adherence factor of . Immunoblot studies demonstrate that the HMW-1 and HMW-2 proteins are also antigenically related to filamentous hemagglutinin. To evaluate HMW-1 and HMW-2 cellular specificity, adherence by DH5α expressing either HMW-1 or HMW-2 was examined by using a variety of cultured epithelial cell lines.

Citation: St. Geme J. 1994. Early Events in the Pathogenesis of Disease, p 157-172. In Miller V, Kaper J, Portnoy D, Isberg R (ed), Molecular Genetics of Bacterial Pathogenesis. ASM Press, Washington, DC. doi: 10.1128/9781555818340.ch11

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Figure 1

Pathogenic sequence for disease caused by

Citation: St. Geme J. 1994. Early Events in the Pathogenesis of Disease, p 157-172. In Miller V, Kaper J, Portnoy D, Isberg R (ed), Molecular Genetics of Bacterial Pathogenesis. ASM Press, Washington, DC. doi: 10.1128/9781555818340.ch11
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Figure 2

Transmission electron micrographs demonstrating hemagglutinating pili after negative staining with uranyl acetate. (A) Long, flexible, peritrichous hemagglutinating pili on the surface of type b Eagan. Magnification, × 27,000. (B) Purified hemagglutinating pili from strain Eagan. Magnification, × 65,000.

Citation: St. Geme J. 1994. Early Events in the Pathogenesis of Disease, p 157-172. In Miller V, Kaper J, Portnoy D, Isberg R (ed), Molecular Genetics of Bacterial Pathogenesis. ASM Press, Washington, DC. doi: 10.1128/9781555818340.ch11
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Figure 3

Transmission electron micrograph of nontypeable 12 after incubation of bacteria with a polyclonal antiserum reactive with HMW-1 and HMW-2 and then incubation with protein Α-conjugated 10-nm-diameter gold particles and negative staining with uranyl acetate. Note the intense labeling, consistent with surface exposure of HMW-1 and HMW-2. Magnification, × 36,000.

Citation: St. Geme J. 1994. Early Events in the Pathogenesis of Disease, p 157-172. In Miller V, Kaper J, Portnoy D, Isberg R (ed), Molecular Genetics of Bacterial Pathogenesis. ASM Press, Washington, DC. doi: 10.1128/9781555818340.ch11
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Figure 4

Light micrographs of nontypeable 12 derivatives incubated with Chang conjunctival epithelial cells and stained with Giemsa. (A) Parental strain 12; (B) HMW-2 mutant (HMW-1 , HMW-2): (C) HMW-1 mutant (HMW-1, HMW-2); (D) HMW-1 and HMW-2 double mutant (HMW-1, HMW-2). Magnification, × 550. Reprinted with permission ( ).

Citation: St. Geme J. 1994. Early Events in the Pathogenesis of Disease, p 157-172. In Miller V, Kaper J, Portnoy D, Isberg R (ed), Molecular Genetics of Bacterial Pathogenesis. ASM Press, Washington, DC. doi: 10.1128/9781555818340.ch11
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Figure 5

Light micrographs of DH5a expressing HMW-1 or HMW-2 incubated with Chang conjunctival epithelial cells and stained with Giemsa stain. (A) DH5α containing vector alone; (B) DH5α containing locus; (C) DH5α containing locus. Magnification, × 550. Reprinted with permission ( ).

Citation: St. Geme J. 1994. Early Events in the Pathogenesis of Disease, p 157-172. In Miller V, Kaper J, Portnoy D, Isberg R (ed), Molecular Genetics of Bacterial Pathogenesis. ASM Press, Washington, DC. doi: 10.1128/9781555818340.ch11
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References

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1. Adams, W. G.,, K. A. Deaver,, S. L. Cochi,, B. D. Plikaytis,, E. R. Zeli,, C. V. Broome,, and J. D. Wenger. 1993. Decline of childhood Haemophilus influenzae type b (Hib) disease in the Hib vaccine era. JAMA 269:221226.
2.American Academy of Pediatrics Committeeon Infectious Diseases. 1991. Haemophilus influenzae type b conjugate vaccines: recommendations for immunization of infants and children 2 months of age and older: update. Pediatrics 88:169172.
3. Bakaletz, L. O.,, B. M. Tallan,, T. Hoepf,, T. F. DeMaria,, H. G. Birck,, and D. J. Lim. 1988. Frequency of fimbriation of nontypable Haemophilus influenzae and its ability to adhere to chinchilla and human respiratory epithelium. Infect. Immun. 56:331335.
4. Barenkamp, S. J.,, and J. W. St. Geme III. Genes encoding high-molecular-weight adhesion proteins of nontypeable Haemophilus influenzae are part of gene clusters. Infect. Immun., in press.
5. Barenkamp, S. J.,, and F. F. Bodor. 1990. Development of serum bactericidal activity following nontypable Haemophilus influenzae acute otitis media. Pediatr. Infect. Dis. J. 9:333339.
6. Barenkamp, S. J.,, and E. Leininger. 1992. Cloning, expression, and DNA sequence analysis of genes encoding nontypeable Haemophilus influenzae high-molecular-weight surface-exposed proteins related to filamentous hemagglutinin of Bordetella pertussis. Infect. Immun. 60:13021313.
7.BrazilianPurpuricFeverStudyGroup. 1987. Brazilian purpuric fever: epidemic purpura fulminans associated with antecedent purulent conjunctivitis. Lancet ii:757761.
8.Brazilian Purpuric Fever Study Group. 1987. Haemophilus aegyptius bacteremia in Brazilian purpuric fever. Lancet ii:761763.
9. Brinton, C. C.,, M. J. Carter,, D. B. Derber,, S. Kar,, J. A. Kramarik,, A. C.-C. To,, S. C.-M. To,, and S. W. Wood. 1989. Design and development of pilus vaccines for Haemophilus influenzae diseases. Pediatr. Infect. Dis. J. 8:S54S61.
10. Broadhurst, L. E.,, R. L. Erickson,, and P. W. Kelley. 1993. Decreases in invasive Haemophilus influenzae diseases in US Army children, 1984 through 1991. JAMA 269:227231.
11.Centers for Disease Control and Prevention. 1993. Recommendations for use of Haemophilus b conjugate vaccines and a combined diphtheria, tetanus, pertussis, and Haemophilus b vaccine. Morbid. Mortal. Weekly Rep. 42:115.
12. Cochi, S. L.,, and C. V. Broome. 1986. Vaccine prevention of Haemophilus influenzae type b disease: past, present and future. Pediatr. Infect. Dis. 5:1219.
13. Coleman, T.,, S. Grass,, and R. Munson, Jr. 1991. Molecular cloning, expression, and sequence of the pilin gene from nontypeable Haemophilus influenzae M37. Infect. Immun. 59:17161722.
14. Connor, E. M.,, and M. R. Loeb. 1983. A hemadsorption method for detection of colonies of Haemophilus influenzae type b expressing fimbriae. J. Infect. Dis. 148:855860.
15. Faden, F.,, L. Brodsky,, J. Bernstein,, J. Stanievich,, D. Krystofik,, C. Snuff,, J. J. Hong,, and P. L. Ogra. 1989. Otitis media in children. I. The systemic immune response to nontypable Haemophilus influenzae. J. Infect. Dis. 160:9991004.
16. Falk, P.,, K. A. Roth,, T. Boren,, T. U. Westblom,, J. I. Gordon,, and S. Normark. 1993. An in vitro adherence assay reveals that Helicobacter pylori exhibits cell lineage-specific tropism in the human gastric epithelium. Proc. Natl. Acad. Sci. USA 90:20352039.
17. Farley, M. M.,, D. S. Stephens,, S. L. Kaplan,, and E. O. Mason, Jr. 1990. Pilus- and non-pilus-mediated interactions of Haemophilus influenzae type b with human erythrocytes and human nasopharyngeal mucosa. J. Infect. Dis. 161:274280.
18. Forney, L. J.,, J. R. Gilsdorf,, and D. C. L. Wong. 1992. Effect of pili-specific antibodies on the adherence of Haemophilus influenzae type b to buccal epithelial cells. J. Infect. Dis. 165:464470.
19. Forney, L. J.,, C. F. Marrs,, S. L. Bektesh,, and J. R. Gilsdorf. 1991. Comparison and analysis of the nucleotide sequences of pilin genes from Haemophilus influenzae type b strains Eagan and M43. Infect. Immun. 59:19911996.
20. Gilsdorf, J. R.,, H. Y. Chang,, K. W. McCrea,, and L. O. Bakaletz. 1992. Comparison of hemagglutinating pili of Haemophilus influenzae type b with similar structures of nontypeable H. influenzae. Infect. Immun. 60:374379.
21. Gilsdorf, J. R.,, C. F. Marrs,, K. W. McCrea,, and L. J. Forney. 1990. Cloning, expression, and sequence analysis of the Haemophilus influenzae type b strain M43p+ pilin gene. Infect. Immun. 58:10651072.
22. Gilsdorf, J. R.,, K. McCrea,, and L. Forney. 1990. Conserved and nonconserved epitopes among Haemophilus influenzae type b pili. Infect. Immun. 58:22522257.
23. Guerina, N. G.,, S. Langermann,, H. W. Clegg,, H. W. Kessler,, D. A. Goldmann,, and J. R. Gilsdorf. 1982. Adherence of piliated Haemophilus influenzae type b to human oropharyngeal cells. J. Infect. Dis. 146:564.
24. Holmgren, A.,, and C.-I. Branden. 1989. Crystal structure of chaperone protein PapD reveals an immunoglobulin fold. Nature (London) 342:248251.
25. Huber, P. S.,, and I. N. Egwu. 1985. Capsular variation in experimental strains of Haemophilus influenzae. Med. Microbiol. Immunol.. 173:345353.
26. Hultgren, S. J.,, S. Abraham,, M. Caparon,, P. Falk,, J. W. St. Geme III, and S. Normark. 1993. Pilus and nonpilus bacterial adhesins: assembly and function in cell recognition. Cell 73:887901.
27. Hultgren, S. J.,, F. Jacob-Dubuisson,, C. H. Jones,, and C.-I. Branden. 1993. PapD and superfamily of periplasmic immunoglobulin-like pilus chaperones. Adv. Protein Chem. 44:99123.
28. Hultgren, S. J.,, and S. Normark. 1991. Biogenesis of the bacterial pilus. Curr. Opin. Genet. Dev. 1:313318.
29. Jones, C. H.,, F. Jacob-Dubuisson,, K. Dodson,, M. Kuehn,, L. Slonim,, R. Striker,, and S. J. Hultgren. 1992. Adhesin presentation in bacteria requires molecular chaperones and ushers. Infect. Immun. 60:44454451.
30. Kimura, A.,, K. T. Mountzouros,, D. A. Reiman,, S. Falkow,, and J. L. Cowell. 1990. Bordetella pertussis filamentous hemagglutinin: evaluation as a protective antigen and colonization factor in a mouse respiratory infection model. Infect. Immun. 58:716.
31. Langermann, S.,, and A. Wright. 1990. Molecular analysis of the Haemophilus influenzae type b pilin gene. Mol. Microbiol. 4:221230.
32. Mason, E. O.,, S. L. Kaplan,, B. L. Wiedermann,, E. Pinna Norrod,, and W. A. Stenback. 1985. Frequency and properties of naturally occurring adherent piliated strains of Haemophilus influenzae type b. Infect. Immun. 49:98103.
33. Murphy, T. V.,, K. E. White,, P. Pastor,, L. Gabriel,, F. Medley,, D. M. Granoff,, and M. T. Osterholm. 1993. Declining incidence of Haemophilus influenzae type b disease since introduction of vaccination. JAMA 269:246248.
34. Musser, J. M.,, S. J. Barenkamp,, D. M. Granoff,, and R. K. Selander. 1986. Genetic relationships of serologically nontypable and serotype b strains of Haemophilus influenzae. Infect. Immun. 52: 183191.
35. Pfiefler, R. 1893. Die Aetiologie der Influenzae. Z. Hyg. Infect. 13:357386.
36. Pichichero, M. E.,, P. Anderson,, M. Loeb,, and D. H. Smith. 1982. Do pili play a role in pathogenicity of Haemophilus influenzae type b? Lancet ii:960962.
37. Pittman, M. 1931. Variation and type specificity in the bacterial species Haemophilus influenzae. J. Exp. Med. 53:471493.
38. Porras, O.,, D. A. Caugant,, B. Gray,, T. Lagergard,, B. R. Levin,, and C. Svanborg-Eden. 1986. Difference in structure between type b and nontypable Haemophilus influenzae populations. Infect. Immun. 53:7989.
39. Read, R. C.,, R. Wilson,, A. Rutman,, V. Lund,, H. C. Todd,, A. P. R. Brain,, P. K. Jeffery,, and P. J. Cole. 1991. Interaction of nontypable Haemophilus influenzae with human respiratory mucosa in vitro. J. Infect. Dis. 163:549558.
40. Reiman, D. A.,, M. Domenighini,, E. Tuomanen,, R. Rappuoli,, and S. Falkow. 1989. Filamentous hemagglutinin of Bordetella pertussis: nucleotide sequence and crucial role in adherence. Proc. Natl. Acad. Sci. USA 86:26372641.
41. Sell, S. H.,, and D. T. Karzon. 1973. Haemophilus influenzae. Vanderbilt University Press, Nashville, Tenn..
42. Shurin, P. A.,, S. I. Pelton,, I. B. Tager,, and D. L. Kasper. 1980. Bactericidal antibody and susceptibility to otitis media caused by nontypable strains of Haemophilus influenzae. J. Pediatr. 97: 364369.
43. Slonim, L. N.,, J. S. Pinkner,, C.-I. Branden,, and S. J. Hultgren. 1992. Interactive surface in the PapD chaperone cleft is conserved in pilus chaperone superfamily and essential in subunit recognition and assembly. EMBO J. 11:47474756.
44. Smith, A. L.,, L. Slonim,, L. Forney,, M. Chanyangam,, S. Lohrke,, S. Moseley,, S. Hultgren,, and J. Haas. Unpublished data.
45. Spinola, S. M.,, J. Peacock,, F. W. Denny,, D. L. Smith,, and J. G. Cannon. 1986. Epidemiology of colonization by nontypable Haemophilus influenzae in children: a longitudinal study. J. Infect. Dis. 154:100109.
46. Sterk, L. M. T.,, L. van Alphen,, L. Geelen-van den Broek,, H. J. Houthoff,, and J. Dankert. 1991. Differential binding of Haemophilus influenzae to human tissues by fimbriae. J. Med. Microbiol. 35:129138.
47. St. Geme, J. W., III. 1993. Nontypeable Haemophilus influenzae disease: epidemiology, pathogenesis, and prospects for prevention. Infect. Agents Dis. 2:116.
48.. St. Geme, J. W., III. Submitted for publication.
49. St. Geme, J. W., III. Unpublished data.
50. St. Geme, J. W.,, III, and S. Falkow. 1990. Haemophilus influenzae adheres to and enters cultured human epithelial cells. Infect. Immun. 58:40364044.
51. St. Geme, J. W.,, III, and S. Falkow. 1993. Isolation, expression, and nucleotide sequencing of the pilin structural gene of the Brazilian purpuric fever clone of Haemophilus influenzae biogroup aegyptius. Infect. Immun. 61:22332237.
52. St. Geme, J. W.,, III, S. Falkow,, and S. J. Barenkamp. 1993. High-molecular-weight proteins of nontypable Haemophilus influenzae mediate attachment to human epithelial cells. Proc. Natl. Acad. Sci. USA 90:28752879.
53. St. Geme, J. W., III,, J. R. Gilsdorf,, and S. Falkow. 1991. Surface structures and adherence properties of diverse strains of Haemophilus influenzae biogroup aegyptius. Infect. Immun. 59:33663371.
54. Stull, T. L.,, P. M. Mendelman,, J. E. Haas,, M. A. Schoenborn,, K. D. Mack,, and A. L. Smith. 1984. Characterization of Haemophilus influenzae type b pili. Infect. Immun. 46:787796.
55. Tarentino, A. L.,, C. M. Gomez,, and T. H. Plummer, Jr. 1985. Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase F. Biochemistry 24:46654671.
56. Tuomanen, E.,, H. Towbin,, G. Rosenfelder,, D. Braun,, G. Hanson,, G. Larson,, and R. Hill. 1988. Receptor analogs and monoclonal antibodies which inhibit adherence of Bordetella pertussis to human ciliated respiratory epithelial cells. J. Exp. Med. 168:267277.
57. Turk, D. C. 1984. The pathogenicity of Haemophilus influenzae. J. Med. Microbiol. 18:116.
58. van Alphen, L.,, L. Geelen van den Broek,, L. Blaas,, M. van Ham,, and J. Dankert. 1991. Blocking of fimbria-mediated adherence of Haemophilus influenzae by sialyl gangliosides. Infect. Immun. 59:44734477.
59. van Alphen, L.,, J. Poole,, L. Geelen,, and H. C. Zanen. 1987. The erythrocyte and epithelial cell receptors for Haemophilus influenzae are expressed independently. Infect. Immun. 55:23552358.
60. van Alphen, L.,, J. Poole,, and M. Overbeeke. 1986. The Anton blood group antigen is the erythrocyte receptor for Haemophilus influenzae. FEMS Microbiol. Lett. 37:6971.
61. van Alphen, L.,, N. vandenBerghe,, and L. Geelen van den Broek. 1988. Interaction of Haemophilus influenzae with human erythrocytes and oropharyngeal epithelial cells is mediated by a common fimbrial epitope. Infect. Immun. 56:18001806.
62. van Ham, S. M.,, F. R. Mooi,, M. G. Sindhunata,, W. R. Maris,, and L. van Alphen. 1989. Cloning and expression in Escherichia coli of Haemophilus influenzae fimbrial genes establishes adherence to oropharyngeal epithelial cells. EMBO J. 8:35353540.
63. van Ham, S. M.,, L. van Alphen,, F. R. Mooi,, and J. P. M. van Putten. 1993. Phase variation of H. influenzae fimbriae: transcriptional control of two divergent genes through a variable combined promoter region. Cell 73:11871196.
64. Watson, W. J.,, J. R. Gilsdorf,, M. A. Tucci,, K. W. McCrea,, L. J. Forney,, and C. F. Marrs. 1994. Identification of a gene essential for piliation in Haemophilus influenzae type b with homology to the pilus assembly platform genes of gram-negative bacteria. Infect. Immun. 62:468475.
65. Weber, A.,, K. Harris,, S. Lohrke,, L. Forney,, and A. L. Smith. 1991. Inability to express fimbriae results in impaired ability of Haemophilus influenzae b to colonize the nasopharynx. Infect. Immun. 59:47244728.
66. Whitney, A. M.,, and M. M. Farley. 1993. Cloning and sequence analysis of the structural pilin gene of Brazilian purpuric fever-associated Haemophilus influenzae biogroup aegyptius. Infect. Immun. 61:15591562.
67. Woodward, M. P.,, W. W. Young, Jr.,, and R. A. Bloodgood. 1985. Detection of monoclonal antibodies specific for carbohydrate epitopes using periodate oxidation. J. Immunol. Methods 78:143153.

Tables

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Table 1

Adherence to cultured cells by DH5α expressing the high-molecular-weight proteins HMW-1 or HMW-2

Adherence values were determined In a 30-min assay by dividing the number of adherent bacteria by the number of inoculated bacteria. For the purposes of comparison, these values were normalized to adherence by DHSα lacking expression of HMW-1 or HMW-2, which was arbitrarily defined as 1.0. Numbers represent the means ± standard errors of the means of measurements made in triplicate from representative experiments. Reprinted with permission ( ).

Citation: St. Geme J. 1994. Early Events in the Pathogenesis of Disease, p 157-172. In Miller V, Kaper J, Portnoy D, Isberg R (ed), Molecular Genetics of Bacterial Pathogenesis. ASM Press, Washington, DC. doi: 10.1128/9781555818340.ch11

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