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

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.

• Authors: Michaela Rumlová, Ivana Křížová, Romana Hadravová, Michal Doležal, Karolína Strohalmová, Alena Keprová, Iva Pichová, Tomáš Ruml
• Journal: The Journal of general virology (J Gen Virol) Vol. 95 Issue Pt 6 Pg. 1383-1389 (Jun 2014) ISSN: 1465-2099 [Electronic] England
• PMID: 24659101 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: © 2014 The Authors.

Chemical References

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

Topics

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