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Surface-exposed amino- and carboxy-terminal residues are crucial for the initiation of assembly in Pepper vein banding virus: A flexuous rod-shaped virus
, H.S. Savithri
Published in Academic Press Inc.
2003
PMID: 14644614
Volume: 316
   
Issue: 2
Pages: 325 - 336
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. © 2003 Elsevier Inc. All rights reserved.
About the journal
JournalVirology
PublisherAcademic Press Inc.
ISSN00426822