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Coxsackievirus entry across epithelial tight junctions requires
occluding and the small GTPases Rab34 and Rab5
Coyne CB, Shen L, Turner JR and JM Bergelson. (2007) Cell Host Microbe
2: 181-182.
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.
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