Format

Send to

Choose Destination
Nat Commun. 2017 May 24;8:15496. doi: 10.1038/ncomms15496.

Exploiting the kinesin-1 molecular motor to generate a virus membrane penetration site.

Author information

1
Department of Cell and Developmental Biology, University of Michigan Medical School, 109 Zina Pitcher Place, 3043 BSRB, Ann Arbor, Michigan 48109, USA.

Abstract

Viruses exploit cellular machineries to penetrate a host membrane and cause infection, a process that remains enigmatic for non-enveloped viruses. Here we probe how the non-enveloped polyomavirus SV40 penetrates the endoplasmic reticulum (ER) membrane to reach the cytosol, a crucial infection step. We find that the microtubule-based motor kinesin-1 is recruited to the ER membrane by binding to the transmembrane J-protein B14. Strikingly, this motor facilitates SV40 ER-to-cytosol transport by constructing a penetration site on the ER membrane called a 'focus'. Neither kinesin-2, kinesin-3 nor kinesin-5 promotes foci formation or infection. The specific use of kinesin-1 is due to its unique ability to select posttranslationally modified microtubules for cargo transport and thereby spatially restrict focus formation to the perinucleus. These findings support the idea of a 'tubulin code' for motor-dependent trafficking and establish a distinct kinesin-1 function in which a motor is exploited to create a viral membrane penetration site.

PMID:
28537258
PMCID:
PMC5458101
DOI:
10.1038/ncomms15496
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Nature Publishing Group Icon for PubMed Central
Loading ...
Support Center