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Crystal Structure of a Retroviral Polyprotein: Prototype Foamy Virus Protease-Reverse Transcriptase (PR-RT)

  1. Author:
    Harrison, Jerry Joe E K
    Tuske, Steve
    Das, Kalyan
    Ruiz, Francesc X
    Bauman, Joseph D
    Boyer,Paul
    DeStefano, Jeffrey J [ORCID]
    Hughes,Stephen
    Arnold, Eddy

  2. Author Address

    Center for Advanced Biotechnology and Medicine (CABM), Rutgers University, Piscataway, NJ 08854, USA., Department of Medicinal Chemistry, Ernest Mario School of Pharmacy, Rutgers University, Piscataway, NJ 08854, USA., Department of Chemistry, University of Ghana, Legon P.O. Box LG 56, Ghana., Department of Microbiology, Immunology and Transplantation, Rega Institute, KU Leuven, 3000 Leuven, Belgium., HIV Dynamics and Replication Program, National Cancer Institute, Frederick, MD 21702, USA., Department of Cell Biology and Molecular Genetics, University of Maryland College Park, College Park, MD 20742, USA., Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ 08854, USA.,
    1. Year: 2021
    2. Date: Aug
    3. Epub Date: 2021 07 29
  2. Journal: Viruses
    1. 13
    2. 8
  4. Type of Article: Article
  5. Article Number: 1495
  6. ISSN: 1999-4915
  1. Abstract:

    In most cases, proteolytic processing of the retroviral Pol portion of the Gag-Pol polyprotein precursor produces protease (PR), reverse transcriptase (RT), and integrase (IN). However, foamy viruses (FVs) express Pol separately from Gag and, when Pol is processed, only the IN domain is released. Here, we report a 2.9 197; resolution crystal structure of the mature PR-RT from prototype FV (PFV) that can carry out both proteolytic processing and reverse transcription but is in a configuration not competent for proteolytic or polymerase activity. PFV PR-RT is monomeric and the architecture of PFV PR is similar to one of the subunits of HIV-1 PR, which is a dimer. There is a C-terminal extension of PFV PR (101-145) that consists of two helices which are adjacent to the base of the RT palm subdomain, and anchors PR to RT. The polymerase domain of PFV RT consists of fingers, palm, thumb, and connection subdomains whose spatial arrangements are similar to the p51 subunit of HIV-1 RT. The RNase H and polymerase domains of PFV RT are connected by flexible linkers. Significant spatial and conformational (sub)domain rearrangements are therefore required for nucleic acid binding. The structure of PFV PR-RT provides insights into the conformational maturation of retroviral Pol polyproteins.

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External Sources

  1. View Full Text
  2. DOI: 10.3390/v13081495
  3. PMID: 34452360
  4. PMCID: PMC8402755
  5. View record in Web of Science®
  6. WOS: 000690080800001
  7. PII : v13081495

Library Notes

  1. Fiscal Year: FY2020-2021
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