Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1973 Mar;113(3):1400–1403. doi: 10.1128/jb.113.3.1400-1403.1973

Immunologically Cross-Reacting Proteins in Cell Walls of Many Bacteria

Harry G Rittenhouse a,1, J Barry Rodda a, Bruce A McFadden a,2
PMCID: PMC251710  PMID: 4120606

Abstract

Antibodies to a protein present in the cell envelope of Hydrogenomonas facilis agglutinate many gram-negative bacteria and a few gram-positive bacteria. Immunodiffusion studies of extracts from the various organisms tested indicate the presence of components sharing antigenic determinants with the cell envelope protein in all bacteria which can be agglutinated and a few that cannot. Cross-reacting components were not detected in extracts of Mycoplasma laidlawii, Anacystis nidulans, and several eukaryotic organisms.

Full text

PDF
1400

Selected References

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

  1. Braun V., Bosch V. Sequence of the murein-lipoprotein and the attachment site of the lipid. Eur J Biochem. 1972 Jun 23;28(1):51–69. doi: 10.1111/j.1432-1033.1972.tb01883.x. [DOI] [PubMed] [Google Scholar]
  2. Braun V., Rehn K. Chemical characterization, spatial distribution and function of a lipoprotein (murein-lipoprotein) of the E. coli cell wall. The specific effect of trypsin on the membrane structure. Eur J Biochem. 1969 Oct;10(3):426–438. doi: 10.1111/j.1432-1033.1969.tb00707.x. [DOI] [PubMed] [Google Scholar]
  3. Fukui Y., Nachbar M. S., Salton M. R. Immunochemistry and peptide mapping of Micrococcus lysodeikticus membrane proteins. Biochim Biophys Acta. 1971 Jul 6;241(1):30–41. doi: 10.1016/0005-2736(71)90300-2. [DOI] [PubMed] [Google Scholar]
  4. Fukui Y., Nachbar M. S., Salton M. R. Immunological properties of Micrococcus lysodeikticus membranes. J Bacteriol. 1971 Jan;105(1):86–92. doi: 10.1128/jb.105.1.86-92.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Homma J. Y., Suzuki N. The protein moiety of the endotoxin of Pseudomonas aeruginosa. Ann N Y Acad Sci. 1966 Jun 30;133(2):508–526. doi: 10.1111/j.1749-6632.1966.tb52386.x. [DOI] [PubMed] [Google Scholar]
  6. Kahane I., Razin S. Immunological analysis of Mycoplasma membranes. J Bacteriol. 1969 Oct;100(1):187–194. doi: 10.1128/jb.100.1.187-194.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Kuehn G. D., McFadden B. A., Johanson R. A., Hill J. M., Shumway L. K. The facile isolation of a structural phospholipoprotein from hydrogenomon as facilis and Neurospora crassa. Proc Natl Acad Sci U S A. 1969 Feb;62(2):407–414. doi: 10.1073/pnas.62.2.407. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. MCCARTY M., MORSE S. I. CELL WALL ANTIGENS OF GRAM-POSITIVE BACTERIA. Adv Immunol. 1964;27:249–286. doi: 10.1016/s0065-2776(08)60709-9. [DOI] [PubMed] [Google Scholar]
  9. Minden P., McClatchy J. K., Cooper R., Bardana E. J., Jr, Farr R. S. Shared antigens between Mycobacterium bovis (BCG) and other bacterial species. Science. 1972 Apr 7;176(4030):57–58. doi: 10.1126/science.176.4030.57. [DOI] [PubMed] [Google Scholar]
  10. PERKINS H. R. Chemical structure and biosynthesis of bacterial cell walls. Bacteriol Rev. 1963 Mar;27:18–55. doi: 10.1128/br.27.1.18-55.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Ralston E., Palleroni N. J., Doudoroff M. Deoxyribonucleic acid homologies of some so-called "Hydrogenomonas" species. J Bacteriol. 1972 Jan;109(1):465–466. doi: 10.1128/jb.109.1.465-466.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Rittenhouse H. G., Heptinstall J., McFadden B. A. A hydrophobic protein from the cell envelope of Hydrogenomonas facilis. Biochemistry. 1971 Oct 26;10(22):4045–4049. doi: 10.1021/bi00798a006. [DOI] [PubMed] [Google Scholar]
  13. SHOCKMAN G. D., KOLB J. J., TOENNIES G. Relations between bacterial cell wall synthesis, growth phase, and autolysis. J Biol Chem. 1958 Feb;230(2):961–977. [PubMed] [Google Scholar]
  14. Salton M. R., Schmitt M. D., Trefts P. E. Fractionation of isolated bacterial membranes. Biochem Biophys Res Commun. 1967 Dec 15;29(5):728–733. doi: 10.1016/0006-291x(67)90278-1. [DOI] [PubMed] [Google Scholar]
  15. Schnaitman C. A. Comparison of the envelope protein compositions of several gram-negative bacteria. J Bacteriol. 1970 Dec;104(3):1404–1405. doi: 10.1128/jb.104.3.1404-1405.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Sjöquist J., Movitz J., Johansson I. B., Hjelm H. Localization of protein A in the bacteria. Eur J Biochem. 1972 Oct 17;30(1):190–194. doi: 10.1111/j.1432-1033.1972.tb02086.x. [DOI] [PubMed] [Google Scholar]
  17. WELSHIMER H. J. Staphylococcal antibody production in response to injections with Listeria monocytogenes. J Bacteriol. 1960 Mar;79:456–457. doi: 10.1128/jb.79.3.456-457.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Weise G., Drews G., Jann B., Jann K. Identification and analysis of a lipopolysaccharide in cell walls of the blue-green alga Anacystis nidulans. Arch Mikrobiol. 1970;71(1):89–98. doi: 10.1007/BF00412238. [DOI] [PubMed] [Google Scholar]
  19. Whiteside T. L., Salton M. R. Antibody to adenosine triphosphatase from membranes of Micrococcus lysodeikticus. Biochemistry. 1970 Jul 21;9(15):3034–3040. doi: 10.1021/bi00817a015. [DOI] [PubMed] [Google Scholar]

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

RESOURCES