Journal
CELL HOST & MICROBE
Volume 2, Issue 3, Pages 181-192Publisher
CELL PRESS
DOI: 10.1016/j.chom.2007.07.003
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Funding
- NIAID NIH HHS [R01AI5228] Funding Source: Medline
- NIDDK NIH HHS [R01 DK061931-06, R01 DK061931] Funding Source: Medline
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The major group B coxsackievirus (CVB) receptor is a component of the epithelial tightjunction (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.
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