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. 1983 Feb;80(4):1092–1095. doi: 10.1073/pnas.80.4.1092

Vibrio cholerae hemagglutinin/lectin/protease hydrolyzes fibronectin and ovomucin: F. M. Burnet revisited

Richard A Finkelstein *, Mary Boesman-Finkelstein †, Peter Holt *
PMCID: PMC393534  PMID: 6341990

Abstract

Cholera vibrios produce a single polymeric protein that (i) causes hemagglutination; (ii) appears to participate in their attachment to gut epithelium; (iii) may mediate their detachment from gut epithelium; and (iv) is a protease that hydrolyzes fibronectin and mucin, cleaves lactoferrin, and nicks the A subunit of the choleragen-related heat-labile enterotoxin of Escherichia coli.

Keywords: lactoferrin, mucinase, enterotoxin, adherence, immunity

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Agin P. P., Gartner T. K. A novel method for purification of plasma fibronectin. Biochim Biophys Acta. 1982 Jun 16;716(3):443–445. doi: 10.1016/0304-4165(82)90039-3. [DOI] [PubMed] [Google Scholar]
  2. Boesman-Finkelstein M., Finkelstein R. A. Protection in rabbits induced by the Texas Star-SR attenuated A-B+ mutant candidate live oral cholera vaccine. Infect Immun. 1982 Apr;36(1):221–226. doi: 10.1128/iai.36.1.221-226.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Boesman-Finkelstein M., Finkelstein R. A. Sequential purification of lactoferrin, lysozyme and secretory immunoglobulin A from human milk. FEBS Lett. 1982 Jul 19;144(1):1–5. doi: 10.1016/0014-5793(82)80556-5. [DOI] [PubMed] [Google Scholar]
  4. Bullen J. J. The significance of iron in infection. Rev Infect Dis. 1981 Nov-Dec;3(6):1127–1138. doi: 10.1093/clinids/3.6.1127. [DOI] [PubMed] [Google Scholar]
  5. CHUGH M. L., JENSEN K. E., KENDRICK P. L. Antigenic relationships and toxicity of mucinolytic preparations from Vibrio comma and related vibrios. J Bacteriol. 1956 Jun;71(6):722–727. doi: 10.1128/jb.71.6.722-727.1956. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. FINKELSTEIN R. A., NORRIS H. T., DUTTA N. K. PATHOGENESIS EXPERIMENTAL CHOLERA IN INFANT RABBITS. I. OBSERVATIONS ON THE INTRAINTESTINAL INFECTION AND EXPERIMENTAL CHOLERA PRODUCED WITH CELL-FREE PRODUCTS. J Infect Dis. 1964 Jun;114:203–216. doi: 10.1093/infdis/114.3.203. [DOI] [PubMed] [Google Scholar]
  7. FRETER R. The serologic character of cholera Vibrio mucinase. J Infect Dis. 1955 Nov-Dec;97(3):238–245. doi: 10.1093/infdis/97.3.238. [DOI] [PubMed] [Google Scholar]
  8. Finkelstein R. A., Fujita K., LoSpalluto J. J. Procholeragenoid: an aggregated intermediate in the formation of choleragenoid. J Immunol. 1971 Oct;107(4):1043–1051. [PubMed] [Google Scholar]
  9. Finkelstein R. A., Hanne L. F. Purification and characterization of the soluble hemagglutinin (cholera lectin)( produced by Vibrio cholerae. Infect Immun. 1982 Jun;36(3):1199–1208. doi: 10.1128/iai.36.3.1199-1208.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Finkelstein R. A., Sobocinski P. Z., Atthasampunna P., Charunmethee P. Pathogenesis of experimental cholera: identification of choleragen (procholeragen A) by disc immunoelectrophoresis and its differentiation from cholera mucinase. J Immunol. 1966 Jul;97(1):25–33. [PubMed] [Google Scholar]
  11. GANGAROSA E. F., BEISEL W. R., BENYAJATI C., SPRINZ H., PIYARATN P. The nature of the gastrointestinal lesion in asiatic cholera and its relation to pathogenesis: a biopsy study. Am J Trop Med Hyg. 1960 Mar;9:125–135. doi: 10.4269/ajtmh.1960.9.125. [DOI] [PubMed] [Google Scholar]
  12. Geary S. J., Marchlewicz B. A., Finkelstein R. A. Comparison of heat-labile enterotoxins from porcine and human strains of Escherichia coli. Infect Immun. 1982 Apr;36(1):215–220. doi: 10.1128/iai.36.1.215-220.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Gill D. M., Rappaport R. S. Origin of the enzymatically active A1 fragment of cholera toxin. J Infect Dis. 1979 Jun;139(6):674–680. doi: 10.1093/infdis/139.6.674. [DOI] [PubMed] [Google Scholar]
  14. Hanne L. F., Finkelstein R. A. Characterization and distribution of the hemagglutinins produced by Vibrio cholerae. Infect Immun. 1982 Apr;36(1):209–214. doi: 10.1128/iai.36.1.209-214.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Honda T., Finkelstein R. A. Selection and characteristics of a Vibrio cholerae mutant lacking the A (ADP-ribosylating) portion of the cholera enterotoxin. Proc Natl Acad Sci U S A. 1979 Apr;76(4):2052–2056. doi: 10.1073/pnas.76.4.2052. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. JENSEN K. E. Immunologic characterization of a mucinolytic enzyme of Vibrio cholerae. J Infect Dis. 1953 Jul-Aug;93(1):107–110. doi: 10.1093/infdis/93.1.107. [DOI] [PubMed] [Google Scholar]
  17. Kornfeld S. J., Plaut A. G. Secretory immunity and the bacterial IgA proteases. Rev Infect Dis. 1981 May-Jun;3(3):521–534. doi: 10.1093/clinids/3.3.521. [DOI] [PubMed] [Google Scholar]
  18. LOWENTHAL J. P. Stability of a fluid cholera mucinase preparation when combined with a commercially prepared cholera vaccine. Proc Soc Exp Biol Med. 1956 Oct;93(1):103–106. doi: 10.3181/00379727-93-22676. [DOI] [PubMed] [Google Scholar]
  19. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  20. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  21. Levine M. M., Black R. E., Clements M. L., Cisneros L., Nalin D. R., Young C. R. Duration of infection-derived immunity to cholera. J Infect Dis. 1981 Jun;143(6):818–820. doi: 10.1093/infdis/143.6.818. [DOI] [PubMed] [Google Scholar]
  22. Marchalonis J. J. An enzymic method for the trace iodination of immunoglobulins and other proteins. Biochem J. 1969 Jun;113(2):299–305. doi: 10.1042/bj1130299. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Mosher D. F. Fibronectin. Prog Hemost Thromb. 1980;5:111–151. [PubMed] [Google Scholar]
  24. Nelson E. T., Clements J. D., Finkelstein R. A. Vibrio cholerae adherence and colonization in experimental cholera: electron microscopic studies. Infect Immun. 1976 Aug;14(2):527–547. doi: 10.1128/iai.14.2.527-547.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Phillips R. A. Twenty years of cholera research. JAMA. 1967 Nov 13;202(7):610–614. [PubMed] [Google Scholar]
  26. Quaroni A., Isselbacher K. J., Ruoslahti E. Fibronectin synthesis by epithelial crypt cells of rat small intestine. Proc Natl Acad Sci U S A. 1978 Nov;75(11):5548–5552. doi: 10.1073/pnas.75.11.5548. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Schneider D. R., Parker C. D. Isolation and characterization of protease-deficient mutants of vibrio cholerae. J Infect Dis. 1978 Aug;138(2):143–151. doi: 10.1093/infdis/138.2.143. [DOI] [PubMed] [Google Scholar]
  28. Schneider D. R., Parker C. D. Purification and characterization of the mucinase of Vibrio cholerae. J Infect Dis. 1982 Apr;145(4):474–482. doi: 10.1093/infdis/145.4.474. [DOI] [PubMed] [Google Scholar]
  29. Sokol P. A., Ohman D. E., Iglewski B. H. A more sensitive plate assay for detection of protease production by Pseudomanas aeruginosa. J Clin Microbiol. 1979 Apr;9(4):538–540. doi: 10.1128/jcm.9.4.538-540.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Woods D. E., Straus D. C., Johanson W. G., Jr, Bass J. A. Role of fibronectin in the prevention of adherence of Pseudomonas aeruginosa to buccal cells. J Infect Dis. 1981 Jun;143(6):784–790. doi: 10.1093/infdis/143.6.784. [DOI] [PubMed] [Google Scholar]
  31. Yamada K. M., Olden K. Fibronectins--adhesive glycoproteins of cell surface and blood. Nature. 1978 Sep 21;275(5677):179–184. doi: 10.1038/275179a0. [DOI] [PubMed] [Google Scholar]

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