Nature Communications (Oct 2022)
Prion-like low complexity regions enable avid virus-host interactions during HIV-1 infection
- Guochao Wei,
- Naseer Iqbal,
- Valentine V. Courouble,
- Ashwanth C. Francis,
- Parmit K. Singh,
- Arpa Hudait,
- Arun S. Annamalai,
- Stephanie Bester,
- Szu-Wei Huang,
- Nikoloz Shkriabai,
- Lorenzo Briganti,
- Reed Haney,
- Vineet N. KewalRamani,
- Gregory A. Voth,
- Alan N. Engelman,
- Gregory B. Melikyan,
- Patrick R. Griffin,
- Francisco Asturias,
- Mamuka Kvaratskhelia
Affiliations
- Guochao Wei
- Division of Infectious Diseases, Anschutz Medical Campus, University of Colorado School of Medicine
- Naseer Iqbal
- Department of Biochemistry & Molecular Genetics, Anschutz Medical Campus, University of Colorado School of Medicine
- Valentine V. Courouble
- Department of Molecular Medicine, The Scripps Research Institute
- Ashwanth C. Francis
- Institute of Molecular Biophysics, Department of Biological Sciences, Florida State University
- Parmit K. Singh
- Department of Cancer Immunology & Virology, Dana-Farber Cancer Institute
- Arpa Hudait
- Department of Chemistry, Chicago Center for Theoretical Chemistry, Institute for Biophysical Dynamics, and James Franck Institute, The University of Chicago
- Arun S. Annamalai
- Division of Infectious Diseases, Anschutz Medical Campus, University of Colorado School of Medicine
- Stephanie Bester
- Division of Infectious Diseases, Anschutz Medical Campus, University of Colorado School of Medicine
- Szu-Wei Huang
- Division of Infectious Diseases, Anschutz Medical Campus, University of Colorado School of Medicine
- Nikoloz Shkriabai
- Division of Infectious Diseases, Anschutz Medical Campus, University of Colorado School of Medicine
- Lorenzo Briganti
- Division of Infectious Diseases, Anschutz Medical Campus, University of Colorado School of Medicine
- Reed Haney
- Division of Infectious Diseases, Anschutz Medical Campus, University of Colorado School of Medicine
- Vineet N. KewalRamani
- Center for Cancer Research, National Cancer Institute
- Gregory A. Voth
- Department of Chemistry, Chicago Center for Theoretical Chemistry, Institute for Biophysical Dynamics, and James Franck Institute, The University of Chicago
- Alan N. Engelman
- Department of Cancer Immunology & Virology, Dana-Farber Cancer Institute
- Gregory B. Melikyan
- Department of Pediatrics, Emory University
- Patrick R. Griffin
- Department of Molecular Medicine, The Scripps Research Institute
- Francisco Asturias
- Department of Biochemistry & Molecular Genetics, Anschutz Medical Campus, University of Colorado School of Medicine
- Mamuka Kvaratskhelia
- Division of Infectious Diseases, Anschutz Medical Campus, University of Colorado School of Medicine
- DOI
- https://doi.org/10.1038/s41467-022-33662-6
- Journal volume & issue
-
Vol. 13,
no. 1
pp. 1 – 19
Abstract
Host proteins CPSF6, NUP153, and SEC24C are vital for HIV-1 infection. They bind to the viral capsid protein and contribute to shuttling of virions through the cytoplasm (SEC24C), import into the nucleus (NUP153 and CPSF6) and subsequent trafficking to preferred integration sites (CPSF6). Here, Wei et al. combine structural, biochemical and virological assays to emphasize the importance of prion-like low complexity domains surrounding short phenylalanine-glycine regions in binding and increasing the avidity when interacting with viral capsid.
