Coxsackievirus entry across epithelial tight junctions requires occludin and the small GTPases Rab34 and Rab5.

Journal Article (Journal Article)

The major group B coxsackievirus (CVB) receptor is a component of the epithelial tight junction (TJ), a protein complex that regulates the selective passage of ions and molecules across the epithelium. CVB enters polarized epithelial cells from the TJ, causing a transient disruption of TJ integrity. Here we show that CVB does not induce major reorganization of the TJ, but stimulates the specific internalization of occludin-a TJ integral membrane component-within macropinosomes. Although occludin does not interact directly with virus, depletion of occludin prevents CVB entry into the cytoplasm and inhibits infection. Both occludin internalization and CVB entry require caveolin but not dynamin; both are blocked by inhibitors of macropinocytosis and require the activity of Rab34, Ras, and Rab5, GTPases known to regulate macropinocytosis. Thus, CVB entry depends on occludin and occurs by a process that combines aspects of caveolar endocytosis with features characteristic of macropinocytosis.

Full Text

Duke Authors

Cited Authors

  • Coyne, CB; Shen, L; Turner, JR; Bergelson, JM

Published Date

  • September 13, 2007

Published In

Volume / Issue

  • 2 / 3

Start / End Page

  • 181 - 192

PubMed ID

  • 18005733

Pubmed Central ID

  • PMC2719558

Electronic International Standard Serial Number (EISSN)

  • 1934-6069

Digital Object Identifier (DOI)

  • 10.1016/j.chom.2007.07.003


  • eng

Conference Location

  • United States