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Updated: Jan 28, 2026

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

A Conserved Basic Patch and Central Kink in the Nipah Virus Phosphoprotein Multimerization Domain Are Essential for

Jessica F Bruhn¹, Anne L Hotard², Christina F Spiropoulou²

¹Department of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA.

Structure (London, England : 1993)

|February 26, 2019

Summary

This summary is machine-generated.

Nipah virus phosphoprotein P

Keywords:

Nipah virus RNA-dependent RNA polymerase X-ray crystallography coiled coil differential scanning calorimetry henipavirus minigenome oligomerization phosphoprotein

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Area of Science:

Virology
Molecular Biology
Structural Biology

Background:

Nipah virus (NiV) is a lethal zoonotic virus causing encephalitis outbreaks in Southeast Asia with high mortality.
NiV's RNA-dependent RNA polymerase (L protein) requires the phosphoprotein (P) for efficient function.
The P protein's central multimerization domain, a tetrameric coiled coil, is crucial for tethering L to the viral nucleocapsid.

Purpose of the Study:

To investigate the structural features of the NiV P protein's central coiled coil domain essential for polymerase function.
To elucidate the role of specific structural elements in NiV replication and pathogenesis.

Main Methods:

Utilized a newly constructed NiV bicistronic minigenome assay to assess polymerase activity.
Employed site-directed mutagenesis to analyze the importance of conserved structural features within the P protein's coiled coil domain.

Main Results:

Identified a conserved basic patch and a central kink within the P protein's coiled coil as critical for polymerase function.
Determined that the arginine at position 555 (R555) is absolutely essential for NiV polymerase activity.
Demonstrated that these structural features are conserved in related morbilliviruses like measles and mumps viruses.

Conclusions:

The identified basic patch and central kink in the NiV P protein's coiled coil are vital for RNA-dependent RNA polymerase function.
The essential role of R555 highlights a key structural requirement for NiV replication.
Conserved structural mechanisms in the P protein suggest a potentially conserved pathway for polymerase function across related viral pathogens.