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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.

Funding
This study was supported by the:
  • University of Leeds (Award International Strategy Fund)
    • Principle Award Recipient: AdrianWhitehouse
  • Academy of Medical Sciences (Award Newton Advanced Fellowship)
    • Principle Award Recipient: AdrienneLesley Edkins
  • Rhodes University (Award RGG grant)
    • Principle Award Recipient: AdrienneLesley Edkins
  • National Research Foundation (Award SARChI 98566)
    • Principle Award Recipient: AdrienneLesley Edkins
  • Medical Research Foundation (Award MR/V030701/1)
    • Principle Award Recipient: AdrienneLesley Edkins
  • 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.
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2024-11-28
2024-12-02
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