Hsp27 Responds to and Facilitates Enterovirus A71 Replication by Enhancing Viral Internal Ribosome Entry Site-Mediated Translation

Journal of Virology
Xuelian DanMing-Liang He

Abstract

Enterovirus 71 (EV-A71) is a human pathogen that causes hand, foot, and mouth disease (HFMD) and fatal neurological diseases, and no effective treatment is available. Characterization of key host factors is important for understanding its pathogenesis and developing antiviral drugs. Here we report that Hsp27 is one of the most upregulated proteins in response to EV-A71 infection, as revealed by two-dimensional gel electrophoresis-based proteomics studies. Depletion of Hsp27 by small interfering RNA or CRISPR/Cas9-mediated knockout significantly inhibited viral replication, protein expression, and reproduction, while restoration of Hsp27 restored such virus activities. Furthermore, we show that Hsp27 plays a crucial role in regulating viral internal ribosome entry site (IRES) activities by two different mechanisms. Hsp27 markedly promoted 2Apro-mediated eukaryotic initiation factor 4G cleavage, an important process for selecting and initiating IRES-mediated translation. hnRNP A1 is a key IRES trans-acting factor (ITAF) for enhancing IRES-mediated translation. Surprisingly, knockout of Hsp27 differentially blocked hnRNP A1 but not FBP1 translocation from the nucleus to the cytoplasm and therefore abolished the hnRNP A1 interactio...Continue Reading

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Citations

Jan 9, 2020·Journal of Biomedical Science·Ming-Chih LaiRobert Y L Wang
May 26, 2020·Biochimica Et Biophysica Acta. Gene Regulatory Mechanisms·Aldo BarreraMarcelo López-Lastra
Aug 14, 2020·Developmental and Comparative Immunology·Liang JiangQingyou Xia

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Datasets Mentioned

BETA
AF302996

Methods Mentioned

BETA
electrophoresis
PCR
immunoprecipitation
immunoprecipitation assay
RIP
biopsy
transfection

Software Mentioned

PDQuest two -
ImageJ
Mascot Distiller
PDQuest
Metascape
SPSS
Mascot

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