Hsp70-Hsp90 organising protein (HOP/STIP1) is required for KSHV lytic replication

Kaposi's sarcoma-associated herpesvirus (KSHV) is a DNA virus that causes Kaposi's sarcoma, a cancer of endothelial origin. KSHV uses the activity of host molecular chaperones like Hsp70 and Hsp90 for the folding of host and viral proteins required for productive infection. Hsp70 and Hsp90 chaperones form proteostasis networks with several regulatory proteins known as co-chaperones. Of these, Hsp90-Hsp70-organizing protein (HOP) is an early-stage co-chaperone that regulates the transfer of folding substrate proteins between the Hsp70 and Hsp90 chaperone systems. While the roles for Hsp90 and Hsp70 in KSHV biology have been described, HOP has not previously been studied in this context despite its prominent interaction with both chaperones. Here, we demonstrate a novel function for HOP as a new host factor required for effective lytic replication of KSHV in primary effusion cell lines.

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Publication Details

Journal
Journal of General Virology
Published
2024-11-28
DOI
https://doi.org/10.1099/jgv.0.002053
Citations
2
Primary Topic
Vector-borne infectious diseases
Type
article
Field-Weighted Citation Impact
1.03

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article

Hsp70-Hsp90 organising protein (HOP/STIP1) is required for KSHV lytic replication

Michael Okpara, Adrienne L. Edkins, Abir Chakraborty, Adrian Whitehouse et al.
2 citations
Journal of General Virology
Vector-borne infectious diseases
1.03
article

Hsp70-Hsp90 organising protein (HOP/STIP1) is required for KSHV lytic replication

Michael Okpara, Adrienne L. Edkins, Abir Chakraborty, Adrian Whitehouse, Zoè Jackson, Clinton G. L. Veale, Elisa Kirigin, Frederick Weaver, Lorraine Matandirotya, Jamie-Lee Ruck
article en
2 citations

Abstract

Kaposi's sarcoma-associated herpesvirus (KSHV) is a DNA virus that causes Kaposi's sarcoma, a cancer of endothelial origin. KSHV uses the activity of host molecular chaperones like Hsp70 and Hsp90 for the folding of host and viral proteins required for productive infection. Hsp70 and Hsp90 chaperones form proteostasis networks with several regulatory proteins known as co-chaperones. Of these, Hsp90-Hsp70-organizing protein (HOP) is an early-stage co-chaperone that regulates the transfer of folding substrate proteins between the Hsp70 and Hsp90 chaperone systems. While the roles for Hsp90 and Hsp70 in KSHV biology have been described, HOP has not previously been studied in this context despite its prominent interaction with both chaperones. Here, we demonstrate a novel function for HOP as a new host factor required for effective lytic replication of KSHV in primary effusion cell lines.

Journal of General VirologyVol. 105(11)
University of Leeds (GB), University of Cape Town (ZA), Rhodes University (ZA)
Academy of Medical Sciences, University of Leeds, National Research Foundation, Rhodes University, Foreign, Commonwealth and Development Office, Medical Research Council, European and Developing Countries Clinical Trials Partnership
Openalex Percentile: Top 23%
Vector-borne infectious diseases
1.03
DOIOpen Access PDFOpenAlex
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