Abstract
The outer membrane protein profile of Actinobacillus (Haemophilus) pleuropneumoniae grown under iron-restricted and iron-replete conditions was studied by polyacrylamide gel electrophoresis and immunoblotting. A virulent serotype 1 isolate synthesized a novel protein with an apparent molecular weight of 105,000 (105K) and increased the synthesis of a 76K protein under iron-restricted conditions. Both proteins were synthesized within 15 min of establishment of iron-restricted conditions. Proteins of equivalent molecular weights could also be induced by iron restriction in serotype 2, 3, 4, 5, and 7 isolates of A. pleuropneumoniae. Convalescent-phase sera from serotype 1-infected pigs contained antibodies which recognized both the 105K and 76K proteins from all six serotypes examined, indicating that these proteins were expressed in vivo and were immunologically conserved. Cells expressing the 105K and 76K proteins also displayed an enhanced ability to bind Congo red and hemin, suggesting that one or both of these proteins functioned to acquire complexed iron during in vivo growth.
Full text
PDF






Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Altman E., Brisson J. R., Perry M. B. Structural studies of the capsular polysaccharide from Haemophilus pleuropneumoniae serotype 1. Biochem Cell Biol. 1986 Aug;64(8):707–716. doi: 10.1139/o86-097. [DOI] [PubMed] [Google Scholar]
- Black J. R., Dyer D. W., Thompson M. K., Sparling P. F. Human immune response to iron-repressible outer membrane proteins of Neisseria meningitidis. Infect Immun. 1986 Dec;54(3):710–713. doi: 10.1128/iai.54.3.710-713.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bolin C. A., Jensen A. E. Passive immunization with antibodies against iron-regulated outer membrane proteins protects turkeys from Escherichia coli septicemia. Infect Immun. 1987 May;55(5):1239–1242. doi: 10.1128/iai.55.5.1239-1242.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Daskaleros P. A., Payne S. M. Congo red binding phenotype is associated with hemin binding and increased infectivity of Shigella flexneri in the HeLa cell model. Infect Immun. 1987 Jun;55(6):1393–1398. doi: 10.1128/iai.55.6.1393-1398.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Deneer H. G., Potter A. A. Iron-repressible outer-membrane proteins of Pasteurella haemolytica. J Gen Microbiol. 1989 Feb;135(Pt 2):435–443. doi: 10.1099/00221287-135-2-435. [DOI] [PubMed] [Google Scholar]
- Fenwick B. W., Osburn B. I., Olander H. J. Isolation and biological characterization of two lipopolysaccharides and a capsular-enriched polysaccharide preparation from Haemophilus pleuropneumoniae. Am J Vet Res. 1986 Jul;47(7):1433–1441. [PubMed] [Google Scholar]
- Fohn M. J., Mietzner T. A., Hubbard T. W., Morse S. A., Hook E. W., 3rd Human immunoglobulin G antibody response to the major gonococcal iron-regulated protein. Infect Immun. 1987 Dec;55(12):3065–3069. doi: 10.1128/iai.55.12.3065-3069.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Higgins R., Larivière S., Mittal K. R., Martineau G. P., Rousseau P., Cameron J. Evaluation of a Killed Vaccine Against Porcine Pleuropneumonia Due to Haemophilus pleuropneumoniae. Can Vet J. 1985 Feb;26(2):86–89. [PMC free article] [PubMed] [Google Scholar]
- Kay W. W., Phipps B. M., Ishiguro E. E., Trust T. J. Porphyrin binding by the surface array virulence protein of Aeromonas salmonicida. J Bacteriol. 1985 Dec;164(3):1332–1336. doi: 10.1128/jb.164.3.1332-1336.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- Lawlor K. M., Daskaleros P. A., Robinson R. E., Payne S. M. Virulence of iron transport mutants of Shigella flexneri and utilization of host iron compounds. Infect Immun. 1987 Mar;55(3):594–599. doi: 10.1128/iai.55.3.594-599.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Markwell M. A., Haas S. M., Bieber L. L., Tolbert N. E. A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal Biochem. 1978 Jun 15;87(1):206–210. doi: 10.1016/0003-2697(78)90586-9. [DOI] [PubMed] [Google Scholar]
- Martin P. G., Lachance P., Niven D. F. Production of RNA-dependent haemolysin by Haemophilus pleuropneumoniae. Can J Microbiol. 1985 May;31(5):456–462. doi: 10.1139/m85-085. [DOI] [PubMed] [Google Scholar]
- McIntosh M. A., Chenault S. S., Earhart C. F. Genetic and physiological studies on the relationship between colicin B resistance and ferrienterochelin uptake in Escherichia coli K-12. J Bacteriol. 1979 Jan;137(1):653–657. doi: 10.1128/jb.137.1.653-657.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- McIntosh M. A., Earhart C. F. Coordinate regulation by iron of the synthesis of phenolate compounds and three outer membrane proteins in Escherichia coli. J Bacteriol. 1977 Jul;131(1):331–339. doi: 10.1128/jb.131.1.331-339.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mickelsen P. A., Blackman E., Sparling P. F. Ability of Neisseria gonorrhoeae, Neisseria meningitidis, and commensal Neisseria species to obtain iron from lactoferrin. Infect Immun. 1982 Mar;35(3):915–920. doi: 10.1128/iai.35.3.915-920.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mickelsen P. A., Sparling P. F. Ability of Neisseria gonorrhoeae, Neisseria meningitidis, and commensal Neisseria species to obtain iron from transferrin and iron compounds. Infect Immun. 1981 Aug;33(2):555–564. doi: 10.1128/iai.33.2.555-564.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Neilands J. B. Microbial envelope proteins related to iron. Annu Rev Microbiol. 1982;36:285–309. doi: 10.1146/annurev.mi.36.100182.001441. [DOI] [PubMed] [Google Scholar]
- Nielsen R. Haemophilus pleuropneumoniae serotypes--cross protection experiments. Nord Vet Med. 1984 Jul-Aug;36(7-8):221–234. [PubMed] [Google Scholar]
- Nielsen R. Serological characterization of Actinobacillus pleuropneumoniae strains and proposal of a new serotype: serotype 12. Acta Vet Scand. 1986;27(3):453–455. doi: 10.1186/BF03548158. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Prpic J. K., Robins-Browne R. M., Davey R. B. Differentiation between virulent and avirulent Yersinia enterocolitica isolates by using Congo red agar. J Clin Microbiol. 1983 Sep;18(3):486–490. doi: 10.1128/jcm.18.3.486-490.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rapp V. J., Munson R. S., Jr, Ross R. F. Outer membrane protein profiles of Haemophilus pleuropneumoniae. Infect Immun. 1986 May;52(2):414–420. doi: 10.1128/iai.52.2.414-420.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rapp V. J., Ross R. F. Antibody response of swine to outer membrane components of Haemophilus pleuropneumoniae during infection. Infect Immun. 1986 Dec;54(3):751–760. doi: 10.1128/iai.54.3.751-760.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rogers H. J. Iron-Binding Catechols and Virulence in Escherichia coli. Infect Immun. 1973 Mar;7(3):445–456. doi: 10.1128/iai.7.3.445-456.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rycroft A. N., Taylor D. J. Preparation and characterisation of envelope proteins from Haemophilus pleuropneumoniae. Vet Microbiol. 1987 Dec;15(4):303–314. doi: 10.1016/0378-1135(87)90018-6. [DOI] [PubMed] [Google Scholar]
- Sebunya T. N., Saunders J. R. Haemophilus pleuropneumoniae infection in swine: a review. J Am Vet Med Assoc. 1983 Jun 15;182(12):1331–1337. [PubMed] [Google Scholar]
- Sebunya T. N., Saunders J. R., Osborne A. D. A model aerosol exposure system for induction of porcine Haemophilus pleuropneumonia. Can J Comp Med. 1983 Jan;47(1):48–53. [PMC free article] [PubMed] [Google Scholar]
- Shand G. H., Anwar H., Kadurugamuwa J., Brown M. R., Silverman S. H., Melling J. In vivo evidence that bacteria in urinary tract infection grow under iron-restricted conditions. Infect Immun. 1985 Apr;48(1):35–39. doi: 10.1128/iai.48.1.35-39.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Surgalla M. J., Beesley E. D. Congo red-agar plating medium for detecting pigmentation in Pasteurella pestis. Appl Microbiol. 1969 Nov;18(5):834–837. doi: 10.1128/am.18.5.834-837.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
- West S. E., Sparling P. F. Response of Neisseria gonorrhoeae to iron limitation: alterations in expression of membrane proteins without apparent siderophore production. Infect Immun. 1985 Feb;47(2):388–394. doi: 10.1128/iai.47.2.388-394.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]




