Surface-exposed amino- and carboxy-terminal residues are crucial for the initiation of assembly in Pepper vein banding virus: a flexuous rod-shaped virus

Anindya, Roy and Savithri, HS (2003) Surface-exposed amino- and carboxy-terminal residues are crucial for the initiation of assembly in Pepper vein banding virus: a flexuous rod-shaped virus. In: Virology, 316 (2). pp. 325-336.

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Abstract

The mechanism of assembly of flexuous viruses, such as potyviruses, is poorly understood. Using a recombinant system, we provide evidence that disassembly and reassembly of Pepper vein banding virus (PVBV), a member of the genus potyvirus, proceeds via a ring-like intermediate, and show that electrostatic interactions may be pivotal in stabilizing the particles. Although the surface-exposed N- and C-terminal residues can be removed from the virus-like particles (VLPs) by limited trypsinization without affecting their stability, such truncated CP subunits are unable to form VLPs. To further evaluate importance of these residues, N- and C-terminal deletion mutants were generated and their assembly behavior was investigated. N-terminal 53 and C-terminal 23 amino acids were found to be crucial for the intersubunit interactions involved in the initiation of virus assembly. These segments are surface exposed in the ring-like intermediate and dispensable for further interactions that result in the formation of the VLPs.

Item Type:	Journal Article
Publication:	Virology
Publisher:	Elsevier
Additional Information:	The Copyright belongs to Elsevier.
Keywords:	PVBV;Assembly;Recombinant coat protein;VLPs;Deletion mutants;Potyvirus
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	19 Apr 2006
Last Modified:	21 Feb 2019 09:08
URI:	http://eprints.iisc.ac.in/id/eprint/6340

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