The Haemophilus influenzae Hap serine protease promotes adherence and microcolony formation, potentiated by a soluble host protein

Molecular Cell

Volumn 2, Issue 6, 1998, Pages 841-850

  Hendrixson, David R ^a   St Geme III, Joseph W ^a  

^a ST LOUIS CHILDREN S HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HAP PROTEIN, HEMOPHILUS INFLUENZAE; LEUKOCYTE ELASTASE INHIBITOR; OUTER MEMBRANE PROTEIN; PROTEIN; SERINE PROTEINASE;

ARTICLE; BACTERIAL COUNT; BACTERIUM ADHERENCE; BINDING SITE; CELL CULTURE; CYTOLOGY; ENZYMOLOGY; GENETICS; GROWTH, DEVELOPMENT AND AGING; HAEMOPHILUS INFLUENZAE; HUMAN; HYDROLYSIS; METABOLISM; MICROBIOLOGY; MUTATION; PATHOGENICITY; PHYSIOLOGY; SCANNING ELECTRON MICROSCOPY;

BACTERIAL ADHESION; BACTERIAL OUTER MEMBRANE PROTEINS; BINDING SITES; COLONY COUNT, MICROBIAL; HAEMOPHILUS INFLUENZAE; HUMANS; HYDROLYSIS; MICROSCOPY, ELECTRON, SCANNING; MUTATION; PROTEINASE INHIBITORY PROTEINS, SECRETORY; PROTEINS; SERINE ENDOPEPTIDASES; TUMOR CELLS, CULTURED;

EID: 0032246189     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(00)80298-1     Document Type: Article

References (34)

1. Anderson, P., Johnston, R.B., Jr, and Smith, D.H. (1972). Human serum activities against Hemophilus influenzae type b. J. Clin. Invest. 51, 31-38.
2. Bieber, D., Ramer, S.W., Wu, C.-Y., Murray, W.J., Tobe, T., Fernandez, R., and Schoolnik, G.K. (1998). Type IV pili, transient bacterial aggregates, and virulence of enteropathogenic Escherichia coli. Science 280, 2114-2118.
3. Birrer, P., McElvaney, N.G., Rüdeberg, A., Sommer, C.W., Liechti-Gallati, S., Kraemer, R., Hubbard, R., and Crystal, R.G. (1994). Protease-antiprotease imbalance in the lungs of children with cystic fibrosis. Am. J. Respir. Crit. Care Med., 150, 207-213.
4. Carlone, G.M., Thomas, M.L., Rumschlag, H.S., and Sottnek, F.O. (1986). Rapid microprocedure for isolating detergent-insoluble outer membrane proteins from Haemophilus species. J. Clin. Microbiol. 24, 330-332.
5. Dower, W.J., Miller, J.F., and Ragsdale, C.W. (1988). High efficiency transformation of E. coli by high voltage electroporation. Nucleic Acids Res. 16, 6127-6145.
6. Gauthier, F., Fryksmark, U., Ohlsson, K., and Bieth, J.G. (1982). Kinetics of the inhibition of leukocyte elastase by the bronchial inhibitor. Biochim. Biophys. Acta 700, 178-183.
7. Heinzel, R., Appelhans, H., Gassen, G., Seemüller, U., Machleidt, W., Fritz, H., and Steffens, G. (1986). Molecular cloning and expression of cDNA for human antileukoprotease from cervix uterus. Eur. J. Biochem. 160, 61-67.
8. Hendrixson, D.R., de la Morena, M.L., Stathopoulos, C., and St. Geme, J.W., III (1997). Structural determinants of processing and secretion of the Haemophilus influenzae Hap protein. Mol. Microbiol. 26, 505-518.
9. Herriott, R.M., Meyer, E.M., and Vogt, M. (1970). Defined non-growth media for stage II development of competence in Haemophilus influenzae. J. Bacteriol. 101, 517-524.
10. Howard, A. J., Dunkin, K.T., and Millar, G.W. (1988). Nasopharyngeal carriage and antibiotic resistance of Haemophilus influenzae in healthy children. Epidemiol. Infect. 100, 192-203.
11. Jose, J., Jähnig, F., and Meyer, T.F. (1995). Common structural features of IgA1 protease-like outer membrane protein autotransporters. Mol. Microbiol., 18, 378-380.
12. β-mediated outer membrane transport. EMBO J. 11, 2327-2335.
13. Kleckner, N., Bender, J., and Gottesman, S. (1991). Uses of transposons with emphasis on Tn10. Meth. Enzymol. 204, 139-180.
14. Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage. Nature 227, 680-685.
15. Lee, C.H., Igarashi, Y., Hohman, R.J., Kaulbach, H., White, M.V., and Kaliner, M.A. (1993). Distribution of secretory leukoprotease inhibitor in the human nasal airway. Am. Rev. Respir. Dis. 147, 710-716.
16. Long, S.S., Henretig, F.M., Teter, M.J., and McGowan, K.L. (1983). Nasopharyngeal flora and acute otitis media. Infect. Immun. 41, 987-991.
17. Meyer, T.F., Mlawer, N., and So, M. (1982). Pilus expression in Neisseria gonorrhoeae involves chromosomal rearrangement. Cell 30, 45-52.
18. Murphy, T.F., and Sethi, S. (1992). Bacterial infection in chronic obstructive pulmonary disease. Am. Rev. Resp. Dis. 146, 1067-1083.
19. Murphy, T.F., Bernstein, J.M., Dryja, D.M., Campagnari, A.A., and Apicella, M.A. (1987). Outer membrane protein and lipoligosaccharide analysis of paired nasopharyngeal and middle ear isolates in otitis media due to non-typable Haemophilus influenzae: pathogenic and epidemiologic observations. J. Infect. Dis. 5, 723-731.
20. Pohlner, J., Halter, R., Beyreuther, K., and Meyer, T.F. (1987). Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease. Nature 325, 458-462.
21. Sallenave, J.-M., Shulmann, J., Crossley, J., Jordana, M., and Gauldie, J. (1994). Regulation of secretory leukocyte proteinase inhibitor (SLPI) and elastase-specific inhibitor (ESI/elafin) in human airway epithelial cells by cytokines and neutrophilic enzymes. Am. J. Respir. Cell Mol. Biol. 11, 733-741.
22. Sallenave, J.-M., Si-Ta har, M., Cox, G., Chignard, M., and Gauldie, J. (1997). Secretory leukocyte proteinase inhibitor is a major leukocyte elastase inhibitor in human neutrophils. J. Leukoc. Biol. 61, 695-702.
23. Sambrook, J., Fritsch, E.F., and Maniatis, T. (1989). Molecular Cloning: A Laboratory Manual (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press).
24. Seemüller, U., Arnhold, M., Fritz., H., Wiedenmann, K., Machleidt, W., Heinzel, R., Appelhans, H., Gassen, H-G., and Lottspeich, F. (1986). The acid-stable proteinase inhibitor of human mucous secretions (HUSI-I, antileukoprotease). FEBS Lett. 199, 43-48.
25. Setlow, J.K., Brown, D.C., Boling, M.E., Mattingly, A., and Gordon, M.P. (1968). Repair of deoxyribonucleic acid in Haemophilus influenzae. I. X-ray sensitivity of ultraviolet-sensitive mutants and their behavior as hosts to ultraviolet-irradiated bacteriophage and transforming deoxyribonuclelc acid. J. Bacteriol. 95, 546-558.
26. St. Geme, J.W., III, and Falkow, S. (1990). Haemophilus influenzae adheres to and enters cultured human epithelial cells. Infect. Immun. 58, 4036-4044.
27. St. Geme, J.W., III, Falkow, S., and Barenkamp, S.J. (1993). High-molecular-weight proteins of nontypable Haemophilus influenzae mediate attachment to human epithelial cells. Proc. Natl. Acad. Sci. USA 90, 2875-2879.
28. St. Geme, J.W., III, de la Morena, M.L., and Falkow, S. (1994). A Haemophilus influenzae IgA protease-like protein promotes intimate interaction with human epithelial cells. Mol. Microbiol., 14, 217-233.
29. Subauste, M.C., Jacoby, D.B., Richards, S.M., and Proud, D. (1995). Infection of a human respiratory epithelial cell line with rhinovirus: induction of cytokine release and modulation of susceptibility to infection by cytokine exposure. J. Clin. Invest. 96, 549-557.
30. Terajima, M., Yamaya, M., Sekizawa, K., Okinaga, S., Suzuki, T., Yamada, N., Nakayama, K., Ohrui, T., Oshima, T., Numazaki, Y., and Sasaki, H. (1997). Rhinovirus infection of primary cultures of human tracheal epithelium: role of ICAM-1 and IL-1β. Am. J. Physiol. 273, L749-L759.
31. Thompson, R.C., and Ohlsson, K. (1986). Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor, a potent inhibitor of leukocyte elastase. Proc. Natl. Acad. Sci. USA, 83, 6692-6696.
32. Tomb, J.-F., Barcak, G.J., Chandler, M.S., Redfield, R.J., and Smith, H.O. (1989). Transposon mutagenesis, characterization, and cloning of transformation genes of Haemophilus influenzae Rd. J. Bacteriol. 171, 3796-3802.
33. Turk, D.C. (1984). The pathogenicity of Haemophilus influenzae. J. Med. Microbiol. 18, 1-16.
34. Vogelmeier, C., Hubbard, R.C., Fells, G.A., Schnebli, H-P., Thompson, R.C., Fritz, H., and Crystal, R.G. (1991). Anti-neutrophil elastase defense of the normal human respiratory epithelial surface provided by the secretory leukoprotease inhibitor. J. Clin. Invest. 87, 482-488.