Abstract
Serological methods and electron microscopy were used to study the structural proteins of the small Bacillus subtilis bacteriophage φ29. This virus has a large number of fibers attached at both ends of its prolate head. A complex neck assembly is comprised of 12 symmetrically arranged appendages as the outer component. Head fibers, neck appendages, and the head surface bind anti-φ29 antibodies. Immune sera absorbed with defective lysates of suppressor-sensitive (sus) mutants have been used to determine the genetic control of neck appendages production. Studies on the serum-blocking power of lysates defective in different tail components showed that appendages contain the main serum-blocking protein. This finding suggests an essential role of the neck appendages in phage adsorption or DNA injection.
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Selected References
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- Anderson D. L., Hickman D. D., Reilly B. E. Structure of Bacillus subtilis bacteriophage phi 29 and the length of phi 29 deoxyribonucleic acid. J Bacteriol. 1966 May;91(5):2081–2089. doi: 10.1128/jb.91.5.2081-2089.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
- DE MARS R. I. The production of phage-related materials when bacteriophage development in interrupted by proflavine. Virology. 1955 May;1(1):83–99. doi: 10.1016/0042-6822(55)90007-6. [DOI] [PubMed] [Google Scholar]
- Doermann A. H. Lysis and Lysis Inhibition with Escherichia coli Bacteriophage. J Bacteriol. 1948 Feb;55(2):257–276. doi: 10.1128/jb.55.2.257-276.1948. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Edgar R. S., Lielausis I. Serological studies with mutants of phage T4D defective in genes determining tail fiber structure. Genetics. 1965 Dec;52(6):1187–1200. doi: 10.1093/genetics/52.6.1187. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Höglund S., Levin O. Electron microscopic studies of some proteins from normal human serum. J Mol Biol. 1965 Jul;12(3):866–871. doi: 10.1016/s0022-2836(65)80333-3. [DOI] [PubMed] [Google Scholar]
- LUFT J. H. Improvements in epoxy resin embedding methods. J Biophys Biochem Cytol. 1961 Feb;9:409–414. doi: 10.1083/jcb.9.2.409. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Méndez E., Ramírez G., Salas M., Viñuela E. Structural proteins of bacteriophage phi 29. Virology. 1971 Sep;45(3):567–576. doi: 10.1016/0042-6822(71)90172-3. [DOI] [PubMed] [Google Scholar]
- REILLY B. E., SPIZIZEN J. BACTERIOPHAGE DEOXYRIBONUCLEATE INFECTION OF COMPETENT BACILLUS SUBTILIS. J Bacteriol. 1965 Mar;89:782–790. doi: 10.1128/jb.89.3.782-790.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Reilly B. E., Zeece V. M., Anderson D. L. Genetic study of suppressor-sensitive mutants of the Bacillus subtilis bacteriophage phi 29. J Virol. 1973 May;11(5):756–760. doi: 10.1128/jvi.11.5.756-760.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Salas M., Vásquez C., Méndez E., Viñuela E. Head fibers of bacteriophage phi 29. Virology. 1972 Oct;50(1):180–188. doi: 10.1016/0042-6822(72)90358-3. [DOI] [PubMed] [Google Scholar]
- Valentine R. C., Green N. M. Electron microscopy of an antibody-hapten complex. J Mol Biol. 1967 Aug 14;27(3):615–617. doi: 10.1016/0022-2836(67)90063-0. [DOI] [PubMed] [Google Scholar]
- Welker N. E., Campbell L. L. Unrelatedness of Bacillus amyloliquefaciens and Bacillus subtilis. J Bacteriol. 1967 Oct;94(4):1124–1130. doi: 10.1128/jb.94.4.1124-1130.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Yanagida M., Ahmad-Zadeh C. Determination of gene product positions in bacteriophage T4 by specific antibody association. J Mol Biol. 1970 Jul 28;51(2):411–421. doi: 10.1016/0022-2836(70)90151-8. [DOI] [PubMed] [Google Scholar]
- Yguerabide J., Epstein H. F., Stryer L. Segmental flexibility in an antibody molecule. J Mol Biol. 1970 Aug;51(3):573–590. doi: 10.1016/0022-2836(70)90009-4. [DOI] [PubMed] [Google Scholar]