Archive for February 27th, 2016

Structural and molecular basis for Ebola virus neutralization by protective human antibodies

27 February, 2016

Ebola virus causes hemorrhagic fever with a high mortality rate and for which there is no approved therapy. Two human monoclonal antibodies, mAb100 and mAb114, in combination, protect nonhuman primates against all signs of Ebola virus disease, including viremia. Here, we demonstrate that mAb100 recognizes the base of the Ebola virus glycoprotein (GP) trimer, occludes access to the cathepsin-cleavage loop, and prevents the proteolytic cleavage of GP that is required for virus entry. We show that mAb114 interacts with the glycan cap and inner chalice of GP, remains associated following proteolytic removal of the glycan cap, and inhibits binding of cleaved GP to its receptor. These results define the basis of neutralization for two protective antibodies and may facilitate development of therapies and vaccines.

Sourced through Scoop.it from: science.sciencemag.org

Why is it that structural / molecular immunologic studies always "may facilitate development of therapies and vaccines"?  Really??  How about looking at what the actual vaccines did in terms of eliciting sterilising immunity, or controlling viral load?

So nice work, but it characterises the mode of action of just two monoclonal antibodies from the spectrum of many thousand that would be involved in reaction to infection, and of the hundreds that are involved in vaccine responses, and the many in any single individual that would be involved in actual neutralisation of infectivity / ADCC / infected cell killing, etc.

What I’m getting at is that whole protein responses, in the context of live vaccine vector inoculations, are almost certainly more complex than anything that involves just these two antibodies, and elegant immunological / structural studies are a minor part of understanding the whole problem.

See on Scoop.itVirology News