NanoViricides Inc. (NNVC)

[Ubertino]

Still working on this!

Complex!

EBOV entry
The EBOV envelope GP directly mediates binding of the virion to the host cell. A number of cellular factors, including DC-SIGN/L-SIGN [68,69], LSECtin [70,71], hMGL [72], ß-integrins [73] and Tyro3 family receptors [74], have been implicated as attachment factors, however, none of these proteins individually are necessary and sufficient for viral entry. Hence, a critical cell-surface receptor responsible for EBOV attachment has yet to be identified, despite significant effort. It appears that EBOV enters through a receptor-mediated endocytotic mechanism, but it is still unclear whether clathrin-, caveolae- or cholesterol-dependent processes are used. Recombinant systems using pseudotyped retro-virus particles with ZEBOV GP and live virus studies using chemical inhibitors of clathrin- and caveolae-mediated endocytosis point to the use of caveolae and clathrin in EBOV entry [75,76]. However, cells lacking in caveolae can still be infected with EBOV [77].
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Future perspective
The EBOV GP is one of the most studied proteins of EBOV owing to its critical role in viral entry and potential as a target for therapeutics. Although the crystal structure of ZEBOV GP has shed light on its many roles, many questions remain unanswered.

What is the identity of the EBOV host receptor? A receptor necessary and sufficient for EBOV entry still eludes researchers. We hypothesize that cathepsin cleavage of ZEBOV GP?muc?tm probably leaves behind a convex surface for binding to such a critical entry factor. The fold, location and physiochemical properties of this site should now provide new leads for the search for EBOV receptor(s).

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2829775/