Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1979 Jan;137(1):545–555. doi: 10.1128/jb.137.1.545-555.1979

Bacteriophage T4D receptors and the Escherichia coli cell wall structure: role of spherical particles and protein b of the cell wall in bacteriophage infection.

J Zorzopulos, L M Kozloff, V Chapman, S DeLong
PMCID: PMC218482  PMID: 368029

Abstract

The nature of the interaction of bacteriophage T4D and the outer cell wall of its host, Escherichia coli B, has been investigated. Bacteria with altered or modified cell walls have been obtained by two different growth procedures: (i) growth in high osmolarity medium or (ii) growth in broth in the presence of divalent heavy metal ions. When these altered host cells were washed and subsequently added to regular growth medium, they interacted with added phage particles, but successful infection did not occur. Most of the phage particles released from these treated cells were observed to have full heads and an altered tail structure. The altered phage tails had contracted sheaths and unusual pieces of the bacterial cell wall attached to the distal portion of the exposed phage tail tube. Phage released from bacteria grown in the high osmolarity medium had attached cell wall pieces of two major types, these pieces being either 40 or 21 nm in diameter. The smaller-type cell wall pieces (21 nm) were formed by three spheres each measuring 7 nm in diameter. Phage particles released from cells previously exposed to the divalent metal ions had only one 7-nm cell wall sphere attached to the distal end of the tail tube. It was found that these 7-nm spheres (i) are normal components of the cell wall and are morphologically similar to endotoxin, (ii) are held in place on the cell wall by a component of the cell wall called protein b, and (iii) are most likely the site of penetration of the phage tail tube through which the phage DNA enters the host cell.

Full text

PDF
555

Images in this article

548Image
on p.548
549Image
on p.549
550Image
on p.550
552Image
on p.552
553Image
on p.553
554Image
on p.554

Selected References

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

  1. Alphen W. V., Lugtenberg B. Influence of osmolarity of the growth medium on the outer membrane protein pattern of Escherichia coli. J Bacteriol. 1977 Aug;131(2):623–630. doi: 10.1128/jb.131.2.623-630.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bayer M. E. Adsorption of bacteriophages to adhesions between wall and membrane of Escherichia coli. J Virol. 1968 Apr;2(4):346–356. doi: 10.1128/jvi.2.4.346-356.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bayer M. E. Areas of adhesion between wall and membrane of Escherichia coli. J Gen Microbiol. 1968 Oct;53(3):395–404. doi: 10.1099/00221287-53-3-395. [DOI] [PubMed] [Google Scholar]
  4. Braun V. Covalent lipoprotein from the outer membrane of Escherichia coli. Biochim Biophys Acta. 1975 Oct 31;415(3):335–377. doi: 10.1016/0304-4157(75)90013-1. [DOI] [PubMed] [Google Scholar]
  5. Crowther R. A., Lenk E. V., Kikuchi Y., King J. Molecular reorganization in the hexagon to star transition of the baseplate of bacteriophage T4. J Mol Biol. 1977 Nov 5;116(3):489–523. doi: 10.1016/0022-2836(77)90081-x. [DOI] [PubMed] [Google Scholar]
  6. Datta D. B., Arden B., Henning U. Major proteins of the Escherichia coli outer cell envelope membrane as bacteriophage receptors. J Bacteriol. 1977 Sep;131(3):821–829. doi: 10.1128/jb.131.3.821-829.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Dawes J. Characterisation of the bacteriophage T4 receptor site. Nature. 1975 Jul 10;256(5513):127–128. doi: 10.1038/256127a0. [DOI] [PubMed] [Google Scholar]
  8. Glauert A. M., Thornley M. J. The topography of the bacterial cell wall. Annu Rev Microbiol. 1969;23:159–198. doi: 10.1146/annurev.mi.23.100169.001111. [DOI] [PubMed] [Google Scholar]
  9. Henning U., Höhn B., Sonntag I. Cell envelope and shape of Escherichia coli K12. The ghost membrane. Eur J Biochem. 1973 Nov 1;39(1):27–36. doi: 10.1111/j.1432-1033.1973.tb03099.x. [DOI] [PubMed] [Google Scholar]
  10. Hoekstra D., van der Laan J. W., de Leij L., Witholt B. Release of outer membrane fragments from normally growing Escherichia coli. Biochim Biophys Acta. 1976 Dec 14;455(3):889–899. doi: 10.1016/0005-2736(76)90058-4. [DOI] [PubMed] [Google Scholar]
  11. Knox K. W., Cullen J., Work E. An extracellular lipopolysaccharide-phospholipid-protein complex produced by Escherichia coli grown under lysine-limiting conditions. Biochem J. 1967 Apr;103(1):192–201. doi: 10.1042/bj1030192. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Lindberg A. A. Bacteriophage receptors. Annu Rev Microbiol. 1973;27:205–241. doi: 10.1146/annurev.mi.27.100173.001225. [DOI] [PubMed] [Google Scholar]
  13. Lugtenberg B., Bronstein H., van Selm N., Peters R. Peptidoglycan-associated outer membrane proteins in gammegatine bacteria. Biochim Biophys Acta. 1977 Mar 17;465(3):571–578. doi: 10.1016/0005-2736(77)90274-7. [DOI] [PubMed] [Google Scholar]
  14. Lugtenberg B., Meijers J., Peters R., van der Hoek P., van Alphen L. Electrophoretic resolution of the "major outer membrane protein" of Escherichia coli K12 into four bands. FEBS Lett. 1975 Oct 15;58(1):254–258. doi: 10.1016/0014-5793(75)80272-9. [DOI] [PubMed] [Google Scholar]
  15. Lugtenberg B., Peters R., Bernheimer H., Berendsen W. Influence of cultural conditions and mutations on the composition of the outer membrane proteins of Escherichia coli. Mol Gen Genet. 1976 Sep 23;147(3):251–262. doi: 10.1007/BF00582876. [DOI] [PubMed] [Google Scholar]
  16. Lutkenhaus J. F. Role of a major outer membrane protein in Escherichia coli. J Bacteriol. 1977 Aug;131(2):631–637. doi: 10.1128/jb.131.2.631-637.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Manning P. A., Reeves P. Further characterization of the recipient ability of Escherichia coli K-12 bacteriophage-resistant mutants. J Bacteriol. 1977 Apr;130(1):540–541. doi: 10.1128/jb.130.1.540-541.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Mitra R. S., Gray R. H., Chin B., Bernstein I. A. Molecular mechanisms of accommodation in Escherichia coli to toxic levels of Cd2+. J Bacteriol. 1975 Mar;121(3):1180–1188. doi: 10.1128/jb.121.3.1180-1188.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Osborn M. J., Gander J. E., Parisi E., Carson J. Mechanism of assembly of the outer membrane of Salmonella typhimurium. Isolation and characterization of cytoplasmic and outer membrane. J Biol Chem. 1972 Jun 25;247(12):3962–3972. [PubMed] [Google Scholar]
  20. Prehm P., Jann B., Jann K., Schmidt G., Stirm S. On a bacteriophage T3 and T4 receptor region within the cell wall lipopolysaccharide of Escherichia coli B. J Mol Biol. 1976 Feb 25;101(2):277–281. doi: 10.1016/0022-2836(76)90377-6. [DOI] [PubMed] [Google Scholar]
  21. Rogers S. W., Gilleland H. E., Jr, Eagon R. G. Characterization of a protein-lipopolysaccharide complex released from cell walls of Pseudomonas aeruginosa by ethylenediaminetetraacetic acid. Can J Microbiol. 1969 Jul;15(7):743–748. doi: 10.1139/m69-130. [DOI] [PubMed] [Google Scholar]
  22. 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]
  23. Rothfield L., Pearlman-Kothencz M. Synthesis and assembly of bacterial membrane components. A lipopolysaccharide-phospholipid-protein complex excreted by living bacteria. J Mol Biol. 1969 Sep 28;44(3):477–492. doi: 10.1016/0022-2836(69)90374-x. [DOI] [PubMed] [Google Scholar]
  24. Schmitges C. J., Henning U. The major proteins of the Escherichia coli outer cell-envelope membrane. Heterogeneity of protein I. Eur J Biochem. 1976 Mar 16;63(1):47–52. doi: 10.1111/j.1432-1033.1976.tb10205.x. [DOI] [PubMed] [Google Scholar]
  25. Schnaitman C. A. Outer membrane proteins of Escherichia coli. 3. Evidence that the major protein of Escherichia coli O111 outer membrane consists of four distinct polypeptide species. J Bacteriol. 1974 May;118(2):442–453. doi: 10.1128/jb.118.2.442-453.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Schweizer M., Henning U. Action of a major outer cell envelope membrane protein in conjugation of Escherichia coli K-12. J Bacteriol. 1977 Mar;129(3):1651–1652. doi: 10.1128/jb.129.3.1651-1652.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Simon L. D., Anderson T. F. The infection of Escherichia coli by T2 and T4 bacteriophages as seen in the electron microscope. I. Attachment and penetration. Virology. 1967 Jun;32(2):279–297. doi: 10.1016/0042-6822(67)90277-2. [DOI] [PubMed] [Google Scholar]
  28. Simon L. D., Swan J. G., Flatgaard J. E. Functional defects in T4 bacteriophages lacking the gene 11 and gene 12 products. Virology. 1970 May;41(1):77–90. doi: 10.1016/0042-6822(70)90056-5. [DOI] [PubMed] [Google Scholar]
  29. WEIDEL W., PELZER H. BAGSHAPED MACROMOLECULES--A NEW OUTLOOK ON BACTERIAL CELL WALLS. Adv Enzymol Relat Areas Mol Biol. 1964;26:193–232. doi: 10.1002/9780470122716.ch5. [DOI] [PubMed] [Google Scholar]
  30. Wilson J. H., Luftig R. B., Wood W. B. Interaction of bacteriophage T4 tail fiber components with a lipopolysaccharide fraction from Escherichia coli. J Mol Biol. 1970 Jul 28;51(2):423–434. doi: 10.1016/0022-2836(70)90152-x. [DOI] [PubMed] [Google Scholar]

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

RESOURCES