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Updated: May 1, 2026

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
Published on: April 29, 2022
Breast cancer-associated protein--a novel binding partner of Mason-Pfizer monkey virus protease
Michaela Rumlová1,2, Ivana Křížová2, Romana Hadravová2
1Department of Biotechnology, Institute of Chemical Technology, Technická 5, 166 28 Prague, Czech Republic.
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.
Insights
Breast cancer-associated protein (BCA3) binds to Mason-Pfizer monkey virus (MPMV) protease. Full-length BCA3 incorporates into virions, slightly enhancing MPMV infectivity.
Area of Science:
- Virology
- Molecular Biology
- Oncology
Background:
- Mason-Pfizer monkey virus (MPMV) is a retrovirus with a protease (PR) essential for its replication cycle.
- Understanding viral protein interactions is crucial for developing antiviral strategies.
Purpose of the Study:
- To identify novel binding partners of MPMV protease.
- To investigate the role of these interactions in viral replication and infectivity.
Main Methods:
- Co-immunoprecipitation assays to confirm protein-protein interactions.
- Immunocolocalization to determine the cellular localization of interacting proteins.
- Analysis of viral particle incorporation and infectivity.
Main Results:
- Breast cancer-associated protein (BCA3) was identified as a novel binding partner of MPMV protease.
- The interaction between MPMV protease and BCA3 was confirmed experimentally.
- Full-length BCA3, but not a C-terminally truncated version, was incorporated into MPMV virions.
- The G-patch domain of MPMV protease was not involved in BCA3 interaction or virion incorporation.
- BCA3 expression did not affect viral particle release or processing but slightly increased MPMV infectivity.
Conclusions:
- BCA3 is a novel binding partner of MPMV protease.
- BCA3 incorporation into virions is dependent on its full-length structure.
- BCA3 may play a role in enhancing MPMV infectivity.
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