Surface-exposed amino- and carboxy-terminal residues are crucial for the initiation of assembly in Pepper vein banding virus: a flexuous rod-shaped virus.
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.
Anindya
R
R
Department of Biochemistry, Indian Institute of Science, Bangalore-560 012, India.
Savithri
H S
HS
D002212:Capsicum / Q000821:virology*; D036022:Capsid Proteins / Q000737:chemistry / Q000502:physiology*; D006863:Hydrogen-Ion Concentration; D008954:Models, Biological; D009994:Osmolar Concentration; D017800:Potyvirus / Q000502:physiology*; D014357:Trypsin / Q000494:pharmacology; D014771:Virion / Q000502:physiology; D019065:Virus Assembly
D036022:Capsid Proteins; D014357:Trypsin