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Oligomerization of Mumps Virus Phosphoprotein
Adrian Pickar1, Andrew Elson1, Yang Yang1
1Department of Infectious Diseases, College of Veterinary Medicine, University of Georgia, Athens, Georgia, USA.
Unlabelled:
The mumps virus (MuV) genome encodes a phosphoprotein (P) that is important for viral RNA synthesis. P forms the viral RNA-dependent RNA polymerase with the large protein (L). P also interacts with the viral nucleoprotein (NP) and self-associates to form a homotetramer. The P protein consists of three domains, the N-terminal domain (P(N)), the oligomerization domain (P(O)), and the C-terminal domain (P(C)). While P(N) is known to relax the NP-bound RNA genome, the roles of P(O) and P(C) are not clear. In this study, we investigated the roles of P(O) and P(C) in viral RNA synthesis using mutational analysis and a minigenome system. We found that P(N) and P(C) functions can be trans-complemented. However, this complementation requires P(O), indicating that P(O) is essential for P function. Using this trans-complementation system, we found that P forms parallel dimers (P(N) to P(N) and P(C) to P(C)). Furthermore, we found that residues R231, K238, K253, and K260 in P(O) are critical for P's functions. We identified P(C) to be the domain that interacts with L. These results provide structure-function insights into the role of MuV P.
Importance:
MuV, a paramyxovirus, is an important human pathogen. The P protein of MuV is critical for viral RNA synthesis. In this work, we established a novel minigenome system that allows the domains of P to be complemented in trans. Using this system, we confirmed that MuV P forms parallel dimers. An understanding of viral RNA synthesis will allow the design of better vaccines and the development of antivirals.
Insights
Mumps virus phosphoprotein (P) domains P(O) and P(C) are essential for viral RNA synthesis. The P protein forms parallel dimers, with specific residues in P(O) being critical for function and P(C) interacting with the L protein.
Area of Science:
- Virology
- Molecular Biology
Background:
- Mumps virus (MuV) is a significant human pathogen.
- The viral phosphoprotein (P) is crucial for MuV RNA synthesis, forming part of the RNA-dependent RNA polymerase complex with the L protein.
- The P protein has three domains: N-terminal (P(N)), oligomerization (P(O)), and C-terminal (P(C)), with P(N) known to affect RNA binding, but the roles of P(O) and P(C) remain unclear.
Purpose of the Study:
- To elucidate the roles of the P(O) and P(C) domains in MuV RNA synthesis.
- To investigate the structural and functional relationships of the MuV P protein domains.
- To establish a trans-complementation system for studying P protein function.
Main Methods:
- Utilized mutational analysis to study the P protein domains.
- Employed a novel minigenome system to assess P protein function and domain complementation.
- Investigated protein-protein interactions, specifically P-L interactions and P self-association.
Main Results:
- Demonstrated that P(N) and P(C) functions can be complemented in trans, but this requires the P(O) domain, highlighting its essential role.
- Confirmed that MuV P protein forms parallel dimers (P(N)-P(N) and P(C)-P(C)).
- Identified critical residues (R231, K238, K253, K260) within the P(O) domain essential for P function and confirmed P(C) interacts with the L protein.
Conclusions:
- The P(O) domain is essential for MuV P protein function and its ability to form parallel dimers.
- The P(C) domain directly interacts with the L protein, contributing to the RNA polymerase complex.
- These findings provide crucial structure-function insights into MuV P protein's role in viral RNA synthesis, potentially aiding vaccine and antiviral development.
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