Affiliation:
1. Department of Biosciences
2. Institute of Biotechnology
3. Protein Chemistry Laboratory, Institute of Biotechnology, University of Helsinki, Helsinki, Finland
Abstract
ABSTRACT
The marine double-stranded DNA (dsDNA) bacteriophage PM2, studied since 1968, is the type organism of the family
Corticoviridae
, infecting two gram-negative
Pseudoalteromonas
species. The virion contains a membrane underneath an icosahedral protein capsid composed of two structural proteins. The purified major capsid protein, P2, appears as a trimer, and the receptor binding protein, P1, appears as a monomer. The C-terminal part of P1 is distal and is responsible for receptor binding activity. The rest of the structural proteins are associated with the internal phospholipid membrane enclosing the viral genome. This internal particle is designated the lipid core. The overall structural organization of phage PM2 resembles that of dsDNA bacteriophage PRD1, the type organism of the family
Tectiviridae
.
Publisher
American Society for Microbiology
Subject
Virology,Insect Science,Immunology,Microbiology
Cited by
43 articles.
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