Abstract
Whole, 125I-labeled gonococci (GC) were incubated with rabbit sera against whole GC. After washing, the [125I]GC were lysed in detergent, and radioiodinated antigen-antibody complexes were immunoprecipitated by protein A-Sepharose. Several GC outer membrane proteins, including proteins I, II, and III, could be identified in immunoprecipitates obtained with these antisera. In many immunoprecipitates, a 44K protein was present. Reactivity of antisera toward protein II could be demonstrated, and some rabbit sera contained very prominent apparent antibody activity toward this protein. Proteins I and III were found in similar ratios in immunoprecipitates, suggesting that they form heteropolymers in GC outer membranes. Qualitative and quantitative difference in antibody reactivity and specificity could be demonstrated with serially obtained sera from rabbits immunized with whole GC. The use of viable or Formalin-fixed heat-killed staphylococci yielded "non-immunological" precipitation of 125I-labeled GC constituents; this occurred with staphylococci regardless of whether they contained protein A.
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- Blake M. S., Gotschlich E. C., Swanson J. Effects of proteolytic enzymes on the outer membrane proteins of Neisseria gonorrhoeae. Infect Immun. 1981 Jul;33(1):212–222. doi: 10.1128/iai.33.1.212-222.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- DULBECCO R., VOGT M. Plaque formation and isolation of pure lines with poliomyelitis viruses. J Exp Med. 1954 Feb;99(2):167–182. doi: 10.1084/jem.99.2.167. [DOI] [PMC free article] [PubMed] [Google Scholar]
- DiRienzo J. M., Nakamura K., Inouye M. The outer membrane proteins of Gram-negative bacteria: biosynthesis, assembly, and functions. Annu Rev Biochem. 1978;47:481–532. doi: 10.1146/annurev.bi.47.070178.002405. [DOI] [PubMed] [Google Scholar]
- Draper D. L., James J. F., Brooks G. F., Sweet R. L. Comparison of virulence markers of peritoneal and fallopian tube isolates with endocervical Neisseria gonorrhoeae isolates from women with acute salpingitis. Infect Immun. 1980 Mar;27(3):882–888. doi: 10.1128/iai.27.3.882-888.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Heckels J. E., Everson J. S. The isolation of a new outer membrane protein from the parent strain of Neisseria gonorrhoeae P9. J Gen Microbiol. 1978 May;106(1):179–182. doi: 10.1099/00221287-106-1-179. [DOI] [PubMed] [Google Scholar]
- Heckels J. E. The surface of Neisseria gonorrhoeae: isolation of the major components of the outer membrane. J Gen Microbiol. 1977 Apr;99(2):333–341. doi: 10.1099/00221287-99-2-333. [DOI] [PubMed] [Google Scholar]
- James J. F., Swanson J. Studies on gonococcus infection. XIII. Occurrence of color/opacity colonial variants in clinical cultures. Infect Immun. 1978 Jan;19(1):332–340. doi: 10.1128/iai.19.1.332-340.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Johnston K. H., Holmes K. K., Gotschlich E. C. The serological classification of Neisseria gonorrhoeae. I. Isolation of the outer membrane complex responsible for serotypic specificity. J Exp Med. 1976 Apr 1;143(4):741–758. doi: 10.1084/jem.143.4.741. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kessler S. W. Rapid isolation of antigens from cells with a staphylococcal protein A-antibody adsorbent: parameters of the interaction of antibody-antigen complexes with protein A. J Immunol. 1975 Dec;115(6):1617–1624. [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]
- Lambden P. R., Heckels J. E., James L. T., Watt P. J. Variations in surface protein composition associated with virulence properties in opacity types of Neisseria gonorrhoeae. J Gen Microbiol. 1979 Oct;114(2):305–312. doi: 10.1099/00221287-114-2-305. [DOI] [PubMed] [Google Scholar]
- Markwell M. A., Fox C. F. Surface-specific iodination of membrane proteins of viruses and eucaryotic cells using 1,3,4,6-tetrachloro-3alpha,6alpha-diphenylglycoluril. Biochemistry. 1978 Oct 31;17(22):4807–4817. doi: 10.1021/bi00615a031. [DOI] [PubMed] [Google Scholar]
- McDade R. L., Jr, Johnston K. H. Characterization of serologically dominant outer membrane proteins of Neisseria gonorrhoeae. J Bacteriol. 1980 Mar;141(3):1183–1191. doi: 10.1128/jb.141.3.1183-1191.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nakamura K., Mizushima S. Effects of heating in dodecyl sulfate solution on the conformation and electrophoretic mobility of isolated major outer membrane proteins from Escherichia coli K-12. J Biochem. 1976 Dec;80(6):1411–1422. doi: 10.1093/oxfordjournals.jbchem.a131414. [DOI] [PubMed] [Google Scholar]
- Newhall W. J., Sawyer W. D., Haak R. A. Cross-linking analysis of the outer membrane proteins of Neisseria gonorrhoeae. Infect Immun. 1980 Jun;28(3):785–791. doi: 10.1128/iai.28.3.785-791.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nogueira N., Chaplan S., Tydings J. D., Unkeless J., Cohn Z. Trypanosoma cruzi. Surface antigens of blood and culture forms. J Exp Med. 1981 Mar 1;153(3):629–639. doi: 10.1084/jem.153.3.629. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Overbeeke N., Van Scharrenburg G., Lugtenberg B. Antigenic relationships between pore proteins of Escherichia coli K12. Eur J Biochem. 1980 Sep;110(1):247–254. doi: 10.1111/j.1432-1033.1980.tb04862.x. [DOI] [PubMed] [Google Scholar]
- Straley S. C., Brubaker R. R. Cytoplasmic and membrane proteins of yersiniae cultivated under conditions simulating mammalian intracellular environment. Proc Natl Acad Sci U S A. 1981 Feb;78(2):1224–1228. doi: 10.1073/pnas.78.2.1224. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Swanson J. 125I-labeled peptide mapping of some heat-modifiable proteins of the gonococcal outer membrane. Infect Immun. 1980 Apr;28(1):54–64. doi: 10.1128/iai.28.1.54-64.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Swanson J. Studies on gonococcus infection. XII. Colony color and opacity varienats of gonococci. Infect Immun. 1978 Jan;19(1):320–331. doi: 10.1128/iai.19.1.320-331.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Swanson J. Studies on gonococcus infection. XIV. Cell wall protein differences among color/opacity colony variants of Neisseria gonorrhoeae. Infect Immun. 1978 Jul;21(1):292–302. doi: 10.1128/iai.21.1.292-302.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Swanson J. Studies on gonococcus infection. XVIII. 125I-labeled peptide mapping of the major protein of the gonococcal cell wall outer membrane. Infect Immun. 1979 Mar;23(3):799–810. doi: 10.1128/iai.23.3.799-810.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Virji M., Everson J. S. Comparative virulence of opacity variants of Neisseria gonorrhoeae strain P9. Infect Immun. 1981 Mar;31(3):965–970. doi: 10.1128/iai.31.3.965-970.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]