Anindya, R 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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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|
|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:||19 Sep 2010 04:25|
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