Bovine viral diarrhea virus core is an intrinsically disordered protein that binds RNA. Academic Article uri icon

Overview

abstract

  • Pestiviruses, including bovine viral diarrhea virus (BVDV), are important animal pathogens and close relatives of hepatitis C virus. Pestivirus particles are composed of an RNA genome, a host-derived lipid envelope, and four virion-encoded structural proteins, core (C), E(rns), E1, and E2. Core is a small, highly basic polypeptide that is processed by three enzymatic cleavages before its incorporation into virions. Little is known about its biological properties or its role in virion assembly and structure. We have purified BVDV core protein and characterized it biochemically. We have determined that the processed form of core lacks significant secondary structure and is instead intrinsically disordered. Consistent with its highly basic sequence, we observed that core binds to RNA, although with low affinity and little discernible specificity. We found that BVDV core protein was able to functionally replace the nonspecific RNA binding and condensing region of an unrelated viral capsid protein. Together these results suggest that the in vitro properties of core may reflect its mechanism of action in RNA packaging and virion morphogenesis.

publication date

  • November 21, 2007

Research

keywords

  • Diarrhea Viruses, Bovine Viral
  • RNA, Viral
  • RNA-Binding Proteins
  • Viral Core Proteins
  • Virus Assembly

Identity

PubMed Central ID

  • PMC2224441

Scopus Document Identifier

  • 38349088979

Digital Object Identifier (DOI)

  • 10.1128/JVI.01815-07

PubMed ID

  • 18032507

Additional Document Info

volume

  • 82

issue

  • 3