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Research at St Andrews

Heat shock protein 40 (Hsp40) plays a key role in the virus life cycle

Research output: Contribution to journalReview articlepeer-review

Author(s)

Caroline Knox, Garry A. Luke, Gregory L. Blatch, Eva-Rachele Pesce

School/Research organisations

Abstract

The heat shock proteins (Hsps) are a diverse subset of molecular chaperones that generally promote the proper folding of proteins after translation and also prevent their aggregation during cellular stress. Paradoxically, cellular chaperones might perform important antiviral functions for host cells, yet, at the same time, might be beneficial for virus replication. Among them, Hsp40 is a specialized co-chaperone that has recently received much attention for its crucial role in both constitutive cellular functions and virus pathogenicity. The aim of this review is to raise awareness of its importance in the life cycles of a wide range of viruses. (C) 2011 Elsevier BM. All rights reserved.

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Details

Original languageEnglish
Pages (from-to)15-24
Number of pages10
JournalVirus Research
Volume160
Issue number1-2
DOIs
Publication statusPublished - Sep 2011

    Research areas

  • J-proteins, Hsp40, Chaperone, Heat shock, HEPATITIS-B-VIRUS, SMALL-T-ANTIGEN, SIMIAN-VIRUS-40 LARGE-T, SV40 LARGE T, MOLLUSCUM CONTAGIOSUM VIRUS, PAPILLOMAVIRUS TYPE-16 E7, LAMBDA-DNA-REPLICATION, ESCHERICHIA-COLI DNAJ, STRESSED ENDOPLASMIC-RETICULUM, VIRAL PREINTEGRATION COMPLEX

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