Kirigin, E., Okpara, M.O., Matandirotya, L. et al. (7 more authors) (2024) Hsp70-Hsp90 organising protein (HOP/STIP1) is required for KSHV lytic replication. Journal of General Virology, 105 (11). 002053. ISSN 0022-1317
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2024 The Authors. This is an open-access article distributed under the terms of the Creative Commons Attribution License. This article was made open access via a Publish and Read agreement between the Microbiology Society and the corresponding author’s institution. |
Keywords: | chaperone; HOP/STIP1; KSHV; viral lytic replication |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Molecular Biology (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 17 Dec 2024 11:18 |
Last Modified: | 17 Dec 2024 11:18 |
Published Version: | https://www.microbiologyresearch.org/content/journ... |
Status: | Published |
Publisher: | Microbiology Society |
Identification Number: | 10.1099/jgv.0.002053 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:220897 |
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