Roles of three amino acids of capsid proteins in mink enteritis parvovirus replication

Virus Res. 2016 Aug 15:222:24-28. doi: 10.1016/j.virusres.2016.05.019. Epub 2016 May 19.

Abstract

Virulent mink enteritis parvovirus (MEV) strain MEV-LHV replicated to higher titers in feline F81 cells than attenuated strain MEV-L. Phylogenetic and sequence analyses of the VP2 gene of MEV-LHV, MEV-L and other strains in GenBank revealed two evolutionary branches separating virulent and attenuated strains. Three residues, 101, 232 and 411, differed between virulent and attenuated strains but were conserved within the two branches. Site-directed mutagenesis of the VP2 gene of infectious plasmids of attenuated strain MEV-L respectively replacing residues 101 Ile and 411 Ala with Thr and Glu of virulent strains (MEV-L I101T and MEV-L A411E) increased replication efficiency but still to lower levels than MEV-LHV. However, viruses with mutation of residue 232 (MEV-L I232V and MEV-L I101T/I232V/A411E) decreased viral transcription and replication levels. The three VP2 residues 101, 232 and 411, located on or near the capsid surface, played different roles in the infection processes of MEV.

Keywords: Mink enteritis parvovirus; Replication; Site-directed mutagenesis; VP2 protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Substitution
  • Amino Acids / genetics*
  • Animals
  • Capsid Proteins / chemistry
  • Capsid Proteins / genetics*
  • Codon
  • Mink
  • Mutation
  • Parvoviridae Infections
  • Parvovirus / classification
  • Parvovirus / physiology*
  • Phylogeny
  • Virus Replication*

Substances

  • Amino Acids
  • Capsid Proteins
  • Codon