Skip NavigationSkip to Content
Return Return to Search Results

The capsid lattice engages a bipartite NUP153 motif to mediate nuclear entry of HIV-1 cores

  1. Author:
    Shen, Qi [ORCID]
    Kumari, Sushila [ORCID]
    Xu, Chaoyi
    Jang, Sooin
    Shi, Jiong
    Burdick,Ryan
    Levintov, Lev
    Xiong, Qiancheng [ORCID]
    Wu, Chunxiang [ORCID]
    Devarkar, Swapnil C
    Tian, Taoran
    Tripler, Therese N
    Hu, Yingxia
    Yuan, Shuai
    Temple, Joshua [ORCID]
    Feng, Qingzhou
    Lusk, C Patrick [ORCID]
    Aiken, Christopher [ORCID]
    Engelman, Alan N [ORCID]
    Perilla, Juan R [ORCID]
    Pathak,Vinay [ORCID]
    Lin, Chenxiang [ORCID]
    Xiong, Yong [ORCID]

  2. Author Address

    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511., Department of Cell Biology, Yale School of Medicine, New Haven, CT 06520., Nanobiology Institute, Yale University, West Haven, CT 06516., HIV Dynamics and Replication Program, Center for Cancer Research, National Cancer Institute at Frederick, Frederick, MD 21702., Department of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716., Department of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Boston, MA 02215., Department of Medicine, Harvard Medical School, Boston, MA 02115., Department of Pathology, Microbiology and Immunology, Vanderbilt University Medical Center, Nashville, TN 37232., Department of Biomedical Engineering, Yale University, New Haven, CT 06511.,
    1. Year: 2023
    2. Date: Mar 28
    3. Epub Date: 2023 03 21
  2. Journal: Proceedings of the National Academy of Sciences of the United States of America
    1. 120
    2. 13
    3. Pages: e2202815120
  4. Type of Article: Article
  5. Article Number: e2202815120
  1. Abstract:

    Increasing evidence has suggested that the HIV-1 capsid enters the nucleus in a largely assembled, intact form. However, not much is known about how the cone-shaped capsid interacts with the nucleoporins (NUPs) in the nuclear pore for crossing the nuclear pore complex. Here, we elucidate how NUP153 binds HIV-1 capsid by engaging the assembled capsid protein (CA) lattice. A bipartite motif containing both canonical and noncanonical interaction modules was identified at the C-terminal tail region of NUP153. The canonical cargo-targeting phenylalanine-glycine (FG) motif engaged the CA hexamer. By contrast, a previously unidentified triple-arginine (RRR) motif in NUP153 targeted HIV-1 capsid at the CA tri-hexamer interface in the capsid. HIV-1 infection studies indicated that both FG- and RRR-motifs were important for the nuclear import of HIV-1 cores. Moreover, the presence of NUP153 stabilized tubular CA assemblies in 160;vitro. Our results provide molecular-level mechanistic evidence that NUP153 contributes to the entry of the intact capsid into the nucleus.

    See More

  1. Keywords:

External Sources

  1. View Full Text
  2. DOI: 10.1073/pnas.2202815120
  3. PMID: 36943880

Library Notes

  1. Fiscal Year: FY2022-2023
NCI at Frederick

You are leaving a government website.

This external link provides additional information that is consistent with the intended purpose of this site. The government cannot attest to the accuracy of a non-federal site.

Linking to a non-federal site does not constitute an endorsement by this institution or any of its employees of the sponsors or the information and products presented on the site. You will be subject to the destination site's privacy policy when you follow the link.

ContinueCancel