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

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


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.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • COS Cells
  • Chlorocebus aethiops
  • Cytosol / metabolism
  • Cytosol / virology
  • Endoplasmic Reticulum / metabolism*
  • Endoplasmic Reticulum / virology
  • Gene Knockdown Techniques
  • HEK293 Cells
  • HSP47 Heat-Shock Proteins / genetics
  • HSP47 Heat-Shock Proteins / metabolism
  • Humans
  • Intracellular Membranes / metabolism*
  • Intracellular Membranes / virology
  • Intravital Microscopy
  • Kinesins / genetics
  • Kinesins / metabolism*
  • Microtubules / metabolism
  • Molecular Chaperones
  • RNA, Small Interfering / metabolism
  • Simian virus 40 / pathogenicity
  • Simian virus 40 / physiology*
  • Virion / metabolism
  • Virus Internalization*


  • DNAJB14 protein, human
  • HSP47 Heat-Shock Proteins
  • Molecular Chaperones
  • RNA, Small Interfering
  • Kinesins