Proteomics

Dataset Information

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Mass spectrometry runs and analysis of host proteins co-immunoprecipitated with RABV M protein


ABSTRACT: To explore the role of the matrix protein in RABV infection of host cells, we looked for host proteins that interact with the RABV M protein. We performed Flag-tag-based immunoprecipitation of lysates of HEK293T cells transfected with plasmids expressing either N- or C-terminally Flag-tagged M protein (M-NF or M-CF, respectively), and identified host proteins that interacted with the M proteins by using mass spectrometry (MS). Proteins were detected in lysates of cells transfected with the plasmid expressing Flag-tagged M proteins but not in those of cells transfected with the control plasmid. We identified a total of 2,672 host proteins that co-immunoprecipitated with the M protein; 492 proteins co-immunoprecipitated to both M-NF and M-CF, 1,761 proteins co-immunoprecipitated with M-NF only, and 419 proteins co-immunoprecipitated with M-CF only.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Xing Liu  

LAB HEAD: Zhigao Bu

PROVIDER: PXD021039 | Pride | 2021-09-09

REPOSITORIES: Pride

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Publications

The ATPase ATP6V1A facilitates rabies virus replication by promoting virion uncoating and interacting with the viral matrix protein.

Liu Xing X   Li Fang F   Zhang Jiwen J   Wang Lulu L   Wang Jinliang J   Wen Zhiyuan Z   Wang Zilong Z   Shuai Lei L   Wang Xijun X   Ge Jinying J   Zhao Dongming D   Bu Zhigao Z  

The Journal of biological chemistry 20201122


Rabies virus (RABV) matrix protein (M) plays crucial roles in viral transcription, replication, assembly, and budding; however, its function during the early stage of virus replication remains unknown. Here, we mapped the protein interactome between RABV M and human host factors using a proteomic approach, finding a link to the V-type proton ATPase catalytic subunit A (ATP6V1A), which is located in the endosomes where RABV first enters. By downregulating or upregulating ATP6V1A expression in HEK  ...[more]

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