HIV-1 binds dynein directly to hijack microtubule transport machinery.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 40532013.
- Also identified by DOI 10.1126/sciadv.adn6796 and PMC identifier 12175901.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
HIV-1 uses the microtubule cytoskeleton to reach the host cell nucleus during replication, yet the molecular basis for microtubule-dependent HIV-1 motility is poorly understood. Using in vitro reconstitution biochemistry and single-molecule imaging, we found that HIV-1 binds to the retrograde microtubule-associated motor, dynein, directly and not via a cargo adaptor, as has been previously suggested. The HIV-1 capsid lattice binds to accessory chains on dynein's tail domain. Further, we demonstrate that multiple dynein motors tethered to rigid cargoes, such as HIV-1 capsids, display reduced motility, distinct from the behavior of multiple motors on membranous cargoes. Our results provide an updated model of HIV-1 trafficking wherein HIV-1 binds to dynein directly to "hijack" the dynein transport machinery for microtubule motility.
Medical subject headings
- Microtubules
- HIV-1
- Dyneins