Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1980 Jul;143(1):182–187. doi: 10.1128/jb.143.1.182-187.1980

Cross-linking analysis of Neisseria gonorrhoeae outer membrane proteins.

D K Leith, S A Morse
PMCID: PMC294206  PMID: 6772627

Abstract

The arrangement of proteins in the outer membrane of Neisseria gonorrhoeae was investigated through the use of cleavable chemical cross-linking reagents and two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Cross-linking of isolated outer membranes yielded dimers and trimers of the major outer membrane protein. In addition, data were obtained suggesting that a stable interaction exists between the major protein I and protein II, the second most prevalent protein in the gonococcal outer membrane.

Full text

PDF
185

Images in this article

Selected References

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

  1. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  2. Buchanan T. M., Pearce W. A., Schoolnik G. K., Arko R. J. Protection against infection with Neisseria gonorrhoeae by immunization with outer membrane protein complex and purified pili. J Infect Dis. 1977 Aug;136 (Suppl):S132–S137. doi: 10.1093/infdis/136.supplement.s132. [DOI] [PubMed] [Google Scholar]
  3. Endermann R., Henning U. Nearest neighbors of major proteins in the outer membrane of Escherichia coli K12. FEBS Lett. 1979 Jan 15;97(2):339–342. doi: 10.1016/0014-5793(79)80117-9. [DOI] [PubMed] [Google Scholar]
  4. Fish W. W., Reynolds J. A., Tanford C. Gel chromatography of proteins in denaturing solvents. Comparison between sodium dodecyl sulfate and guanidine hydrochloride as denaturants. J Biol Chem. 1970 Oct 10;245(19):5166–5168. [PubMed] [Google Scholar]
  5. Frasch C. E., Gotschlich E. C. An outer membrane protein of Neisseria meningitidis group B responsible for serotype specificity. J Exp Med. 1974 Jul 1;140(1):87–104. doi: 10.1084/jem.140.1.87. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. 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]
  7. Hildebrandt J. F., Mayer L. W., Wang S. P., Buchanan T. M. Neisseria gonorrhoeae acquire a new principal outer-membrane protein when transformed to resistance to serum bactericidal activity. Infect Immun. 1978 Apr;20(1):267–272. doi: 10.1128/iai.20.1.267-272.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Johnston K. H., Gotschlich E. C. Isolation and characterization of the outer membrane of Neisseria gonorrhoeae. J Bacteriol. 1974 Jul;119(1):250–257. doi: 10.1128/jb.119.1.250-257.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. 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]
  10. KELLOGG D. S., Jr, PEACOCK W. L., Jr, DEACON W. E., BROWN L., PIRKLE D. I. NEISSERIA GONORRHOEAE. I. VIRULENCE GENETICALLY LINKED TO CLONAL VARIATION. J Bacteriol. 1963 Jun;85:1274–1279. doi: 10.1128/jb.85.6.1274-1279.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. 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]
  12. Novotny P., Short J. A., Walker P. D. An electron-microscope study of naturally occurring and cultured cells of Neisseria Gonorrhoeae. J Med Microbiol. 1975 Aug;8(3):413–427. doi: 10.1099/00222615-8-3-413. [DOI] [PubMed] [Google Scholar]
  13. Odugbemi T. O., Hafiz S. The effects of iron chelators on the colonial morphology of Neisseria gonorrhoeae. J Gen Microbiol. 1978 Jan;104(1):165–167. doi: 10.1099/00221287-104-1-165. [DOI] [PubMed] [Google Scholar]
  14. Palva E. T., Randall L. L. Arrangement of protein I in Escherichia coli outer membrane: cross-linking study. J Bacteriol. 1978 Jan;133(1):279–286. doi: 10.1128/jb.133.1.279-286.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Palva E. T., Randall L. L. Cross-linking analysis of the two forms of protein I, a major outer membrane protein of Escherichia coli. J Bacteriol. 1979 Apr;138(1):254–256. doi: 10.1128/jb.138.1.254-256.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Palva E. T., Randall L. L. Nearest-neighbor analysis of Escherichia coli outer membrane proteins using cleavable cross-links. J Bacteriol. 1976 Sep;127(3):1558–1560. doi: 10.1128/jb.127.3.1558-1560.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Reithmeier R. A., Bragg P. D. Cross-linking of the proteins in the outer membrane of Escherichia coli. Biochim Biophys Acta. 1977 Apr 18;466(2):245–256. doi: 10.1016/0005-2736(77)90222-x. [DOI] [PubMed] [Google Scholar]
  18. Rosenbusch J. P. Characterization of the major envelope protein from Escherichia coli. Regular arrangement on the peptidoglycan and unusual dodecyl sulfate binding. J Biol Chem. 1974 Dec 25;249(24):8019–8029. [PubMed] [Google Scholar]
  19. Steck T. L. Cross-linking the major proteins of the isolated erythrocyte membrane. J Mol Biol. 1972 May 14;66(2):295–305. doi: 10.1016/0022-2836(72)90481-0. [DOI] [PubMed] [Google Scholar]
  20. Steven A. C., Heggeler B., Müller R., Kistler J., Rosenbusch J. P. Ultrastructure of a periodic protein layer in the outer membrane of Escherichia coli. J Cell Biol. 1977 Feb;72(2):292–301. doi: 10.1083/jcb.72.2.292. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Swanson J., Kraus S. J., Gotschlich E. C. Studies on gonococcus infection. I. Pili and zones of adhesion: their relation to gonococcal growth patterns. J Exp Med. 1971 Oct 1;134(4):886–906. doi: 10.1084/jem.134.4.886. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Swanson J. Studies on gonococcus infection. II. Freeze-fracture, freeze-etch studies on gonocci. J Exp Med. 1972 Nov 1;136(5):1258–1271. doi: 10.1084/jem.136.5.1258. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Walstad D. L., Guymon L. F., Sparling P. F. Altered outer membrane protein in different colonial types of Neisseria gonorrhoeae. J Bacteriol. 1977 Mar;129(3):1623–1627. doi: 10.1128/jb.129.3.1623-1627.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Wang K., Richards F. M. An approach to nearest neighbor analysis of membrane proteins. Application to the human erythrocyte membrane of a method employing cleavable cross-linkages. J Biol Chem. 1974 Dec 25;249(24):8005–8018. [PubMed] [Google Scholar]
  25. Wolf-Watz H., Elmros T., Normark S., Bloom G. D. Cell envelope of Neisseria gonorrhoeae: outer membrane and peptidoglycan composition of penicillin-sensitive and-resistant strains. Infect Immun. 1975 Jun;11(6):1332–1341. doi: 10.1128/iai.11.6.1332-1341.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES