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PMID: 6816951 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Structure of the lipid-containing bacteriophage PRD1: disruption of wild-type and nonsense mutant phage particles with guanidine hydrochloride.

Journal of virology ·Vol. 44 ·No. 3 ·1982-12-00 ·Pages 1031-8

Bamford D, Mindich L

Abstract

The lipid-containing bacteriophage PRD1 was disrupted, and the subviral particles were studied. Guanidine treatment released two phage proteins (P3 and P5). These proteins form the polyhedral capsid. The remaining phage proteins were associated with the phage membrane vesicle. The vesicle was capable of forming a tubular structure. The isolated phage membrane vesicles aggregated readily. We found that aggregation and tube formation were associated with specific phage proteins (P11 and P18, respectively) by using protease treatment and an analysis of nonsense mutant phage particles. In addition, the possibility that free vesicles might be precursors to empty virions was studied.

MeSH Terms
Bacteriophages/genetics Cell Membrane/ultrastructure Guanidine Guanidines/pharmacology Lipids/analysis Microscopy, Electron Mutation Pseudomonas aeruginosa/genetics Salmonella Phages/genetics Salmonella typhimurium/genetics Viral Proteins/genetics
Chemicals
Guanidines Lipids Viral Proteins Guanidine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Bamford D
Mindich L
References (15)
15 references, click to expand
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
Published
1982-12-00
Pages
1031-8
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC256363
Subset
IM
Grants
NIAID NIH HHS · AI-09861 · United States
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