Evidence map›Paper›PMID 39607759›Full record

ArticleThe Journal of general virology2024

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

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

Abstract read
In one paragraph

Article in The Journal of general virology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Hsp90: Bringing it all together.Cell stress & chaperones · 2025
    Review
  4. Review
  5. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Elisa KiriginBiomedical Biotechnology Research Unit (BioBRU), Department of Biochemistry and Microbiology, Rhodes University, Makhanda, 6139, South Africa.
Michael Obinna OkparaBiomedical Biotechnology Research Unit (BioBRU), Department of Biochemistry and Microbiology, Rhodes University, Makhanda, 6139, South Africa.
Lorraine MatandirotyaBiomedical Biotechnology Research Unit (BioBRU), Department of Biochemistry and Microbiology, Rhodes University, Makhanda, 6139, South Africa.
Jamie-Lee RuckBiomedical Biotechnology Research Unit (BioBRU), Department of Biochemistry and Microbiology, Rhodes University, Makhanda, 6139, South Africa.
Frederick WeaverSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.
Zoe JacksonSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.
Abir ChakrabortyBiomedical Biotechnology Research Unit (BioBRU), Department of Biochemistry and Microbiology, Rhodes University, Makhanda, 6139, South Africa.
Clinton Gareth Lancaster VealeDepartment of Chemistry, University of Cape Town, Rondebosch, Cape Town, 7700, South Africa.
Adrian WhitehouseBiomedical Biotechnology Research Unit (BioBRU), Department of Biochemistry and Microbiology, Rhodes University, Makhanda, 6139, South Africa.
Adrienne Lesley EdkinsBiomedical Biotechnology Research Unit (BioBRU), Department of Biochemistry and Microbiology, Rhodes University, Makhanda, 6139, South Africa.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Heat-Shock ProteinsHerpesvirus 8, HumanVirus ReplicationCell LineHost-Pathogen InteractionsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansImmediate-Early ProteinsSarcoma, KaposiViral ProteinsHeat-Shock ProteinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsImmediate-Early ProteinsSTIP1 protein, humanViral ProteinschaperoneHOP/STIP1KSHVviral lytic replication

Identifiers

PMID39607759
PMCPMC12453414

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.