Breast cancer-associated protein--a novel binding partner of Mason-Pfizer monkey virus protease

J Gen Virol. 2014 Jun;95(Pt 6):1383-1389. doi: 10.1099/vir.0.064345-0. Epub 2014 Mar 21.

Abstract

We identified breast cancer-associated protein (BCA3) as a novel binding partner of Mason-Pfizer monkey virus (MPMV) protease (PR). The interaction was confirmed by co-immunoprecipitation and immunocolocalization of MPMV PR and BCA3. Full-length but not C-terminally truncated BCA3 was incorporated into MPMV virions. We ruled out the potential role of the G-patch domain, a glycine-rich domain located at the C terminus of MPMV PR, in BCA3 interaction and virion incorporation. Expression of BCA3 did not affect MPMV particle release and proteolytic processing; however, it slightly increased MPMV infectivity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing / chemistry
  • Adaptor Proteins, Signal Transducing / genetics
  • Adaptor Proteins, Signal Transducing / metabolism*
  • Amino Acid Sequence
  • Animals
  • Endopeptidases / chemistry
  • Endopeptidases / genetics
  • Endopeptidases / metabolism*
  • Female
  • HEK293 Cells
  • Humans
  • Mason-Pfizer monkey virus / enzymology*
  • Mason-Pfizer monkey virus / genetics
  • Molecular Sequence Data
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • Protein Binding
  • Protein Interaction Domains and Motifs
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Sequence Homology, Amino Acid
  • Species Specificity

Substances

  • AKIP1 protein, human
  • Adaptor Proteins, Signal Transducing
  • Nuclear Proteins
  • Recombinant Proteins
  • Endopeptidases
  • Mason-Pfizer monkey virus protease