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Virology. 2013 Sep;444(1-2):355-62. doi: 10.1016/j.virol.2013.07.001. Epub 2013 Jul 27.

ϕ29 Scaffolding and connector structure-function relationship studied by trans-complementation.

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1
Department of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294, USA.

Abstract

A dodecamer of connector protein forms a conduit at a unique five-fold vertex in the capsid of many dsDNA-containing viruses providing the means for DNA entry and egress. The molecular mechanism guiding the incorporation of one connector per procapsid remains obscure; however, a recent bacteriophage ϕ29 model suggests that incorporation is coupled to nucleation between the connector and scaffolding proteins and particular amino acids may promote interactions between the two proteins. To test this model in vivo, a trans-complementation system using cloned scaffolding genes was implemented and tested for the ability to complement a ϕ29 amber-scaffolding strain. Wild type scaffolding gene induction resulted in efficient virion production, whereas synthesis of mutant scaffolding proteins displayed various phenotypes. Biochemical analyses of the resultant particles substantiate the previously identified amino acid residues in connector incorporation. Furthermore, kinetic studies of virion production using the in vivo trans-complementation system support the nucleation model.

KEYWORDS:

Bacteriophage ϕ29; Procapsid; Scaffold; Virus assembly

PMID:
23896641
DOI:
10.1016/j.virol.2013.07.001
[Indexed for MEDLINE]
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