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

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

doi:10.1016/j.virusres.2011.06.013

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

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

Research output: Contribution to journal › Review article › peer-review

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.

Original language	English
Pages (from-to)	15-24
Number of pages	10
Journal	Virus Research
Volume	160
Issue number	1-2
DOIs	https://doi.org/10.1016/j.virusres.2011.06.013
Publication status	Published - Sept 2011

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

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

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.",

keywords = "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",

author = "Caroline Knox and Luke, \{Garry A.\} and Blatch, \{Gregory L.\} and Eva-Rachele Pesce",

year = "2011",

month = sep,

doi = "10.1016/j.virusres.2011.06.013",

language = "English",

volume = "160",

pages = "15--24",

journal = "Virus Research",

issn = "0168-1702",

publisher = "Elsevier",

number = "1-2",

}

TY - JOUR

T1 - Heat shock protein 40 (Hsp40) plays a key role in the virus life cycle

AU - Knox, Caroline

AU - Luke, Garry A.

AU - Blatch, Gregory L.

AU - Pesce, Eva-Rachele

PY - 2011/9

Y1 - 2011/9

N2 - 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.

AB - 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.

KW - J-proteins

KW - Hsp40

KW - Chaperone

KW - Heat shock

KW - HEPATITIS-B-VIRUS

KW - SMALL-T-ANTIGEN

KW - SIMIAN-VIRUS-40 LARGE-T

KW - SV40 LARGE T

KW - MOLLUSCUM CONTAGIOSUM VIRUS

KW - PAPILLOMAVIRUS TYPE-16 E7

KW - LAMBDA-DNA-REPLICATION

KW - ESCHERICHIA-COLI DNAJ

KW - STRESSED ENDOPLASMIC-RETICULUM

KW - VIRAL PREINTEGRATION COMPLEX

U2 - 10.1016/j.virusres.2011.06.013

DO - 10.1016/j.virusres.2011.06.013

M3 - Review article

SN - 0168-1702

VL - 160

SP - 15

EP - 24

JO - Virus Research

JF - Virus Research

IS - 1-2

ER -

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

Abstract

UN SDGs

Keywords

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