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

Year: 2024
Type: article
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.
DOI: 10.1099/jgv.0.002053
Authors: Elisa Kirigin, Michael Obinna Okpara, Lorraine Matandirotya, Jamie-Lee Ruck, Frederick Weaver, Zoe Jackson, Abir Chakraborty, Clinton Gareth Lancaster Veale, Adrian Whitehouse, Adrienne Lesley Edkins
Language: English
Open Access status: hybrid
Funders: 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 ID: W4404813638
FWCI: 0.232
Cites: 73
Cited by: 2
Related to: 10