Vimentin inhibits α-tubulin acetylation via enhancing α-TAT1 degradation to suppress the replication of human parainfluenza virus type 3

We previously found that, among human parainfluenza virus type 3 (HPIV3) proteins, the interaction of nucleoprotein (N) and phosphoprotein (P) provides the minimal requirement for the formation of cytoplasmic inclusion bodies (IBs), which are sites of RNA synthesis, and that acetylated α-tubulin enh...

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Bibliographic Details
Published in:PLoS pathogens 2022-09, Vol.18 (9), p.e1010856
Main Authors: Liu, Pengfei, Zhang, Shengwei, Ma, Jingyi, Jin, Dongning, Qin, Yali, Chen, Mingzhou
Format: Article
Language:English
Subjects:
Acetylation
Acetyltransferase
Amino acids
Biology and Life Sciences
Degradation
Dengue fever
Factories
Foot & mouth disease
Genomes
Immunoprecipitation
Inclusion bodies
Infections
Mass spectrometry
Mass spectroscopy
Parainfluenza
Peptides
Physical Sciences
Plasmids
Proteins
Replication
Research and Analysis Methods
RNA polymerase
Scientific imaging
Severe acute respiratory syndrome coronavirus 2
Transcription
Tubulin
Vimentin
Viral infections
Viruses
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Summary:We previously found that, among human parainfluenza virus type 3 (HPIV3) proteins, the interaction of nucleoprotein (N) and phosphoprotein (P) provides the minimal requirement for the formation of cytoplasmic inclusion bodies (IBs), which are sites of RNA synthesis, and that acetylated α-tubulin enhances IB fusion and viral replication. In this study, using immunoprecipitation and mass spectrometry assays, we determined that vimentin (VIM) specifically interacted with the N–P complex of HPIV3, and that the head domain of VIM was responsible for this interaction, contributing to the inhibition of IB fusion and viral replication. Furthermore, we found that VIM promoted the degradation of α-tubulin acetyltransferase 1 (α-TAT1), through its head region, thereby inhibiting the acetylation of α-tubulin, IB fusion, and viral replication. In addition, we identified a 20-amino-acid peptide derived from the head region of VIM that participated in the interaction with the N–P complex and inhibited viral replication. Our findings suggest that VIM inhibits the formation of HPIV3 IBs by downregulating α-tubulin acetylation via enhancing the degradation of α-TAT1. Our work sheds light on a new mechanism by which VIM suppresses HPIV3 replication.
ISSN:1553-7374
1553-7366
1553-7374
DOI:10.1371/journal.ppat.1010856