HIV-1 binds dynein directly to hijack microtubule transport machinery.

Autor:	Badieyan S; Life Sciences Institute, University of Michigan, Ann Arbor, MI, USA., Lichon D; Department of Microbiology and Immunology, Stritch School of Medicine, Loyola University Chicago, IL, USA., Andreas MP; Department of Biological Chemistry, Michigan Medicine, University of Michigan, Ann Arbor, MI, USA., Gillies JP; Department of Molecular, Cellular, and Developmental Biology, College of Literature, Sciences, and the Arts, University of Michigan, Ann Arbor, MI USA., Peng W; EMBL Australia Node in Single Molecule Science and ARC Centre of Excellence in Advanced Molecular Imaging, School of Medical Sciences, UNSW Sydney, Sydney, New South Wales, Australia., Shi J; Department of Pathology, Microbiology, and Immunology, Vanderbilt Institute for Infection, Immunology, and Inflammation, Vanderbilt University Medical Center, Nashville, Tennessee, USA., DeSantis ME; Department of Molecular, Cellular, and Developmental Biology, College of Literature, Sciences, and the Arts, University of Michigan, Ann Arbor, MI USA., Aiken CR; Department of Pathology, Microbiology, and Immunology, Vanderbilt Institute for Infection, Immunology, and Inflammation, Vanderbilt University Medical Center, Nashville, Tennessee, USA., Böcking T; EMBL Australia Node in Single Molecule Science and ARC Centre of Excellence in Advanced Molecular Imaging, School of Medical Sciences, UNSW Sydney, Sydney, New South Wales, Australia., Giessen TW; Department of Biological Chemistry, Michigan Medicine, University of Michigan, Ann Arbor, MI, USA., Campbell EM; Department of Microbiology and Immunology, Stritch School of Medicine, Loyola University Chicago, IL, USA., Cianfrocco MA; Life Sciences Institute, University of Michigan, Ann Arbor, MI, USA.; Department of Biological Chemistry, Michigan Medicine, University of Michigan, Ann Arbor, MI, USA.
Jazyk:	angličtina
Zdroj:	BioRxiv : the preprint server for biology [bioRxiv] 2023 Dec 02. Date of Electronic Publication: 2023 Dec 02.
DOI:	10.1101/2023.08.29.555335
Abstrakt:	Viruses exploit host cytoskeletal elements and motor proteins for trafficking through the dense cytoplasm. Yet the molecular mechanism that describes how viruses connect to the motor machinery is unknown. Here, we demonstrate the first example of viral microtubule trafficking from purified components: HIV-1 hijacking microtubule transport machinery. We discover that HIV-1 directly binds to the retrograde microtubule-associated motor, dynein, and not via a cargo adaptor, as previously suggested. Moreover, we show that HIV-1 motility is supported by multiple, diverse dynein cargo adaptors as HIV-1 binds to dynein light and intermediate chains on dynein's tail. Further, we demonstrate that multiple dynein motors tethered to rigid cargoes, like HIV-1 capsids, display reduced motility, distinct from the behavior of multiple motors on membranous cargoes. Our results introduce a new model of viral trafficking wherein a pathogen opportunistically 'hijacks' the microtubule transport machinery for motility, enabling multiple transport pathways through the host cytoplasm. Competing Interests: Declaration of interests Authors declare that they have no competing interests.
Databáze:	MEDLINE
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