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Wednesday, September 25, 2013 11:09:15 AM
I guess in this instance I need to go elsewhere for an answer....and I will!
OK to publish this from Anil
EUGENE SEYMOUR, MD, MPH
Chief Executive Officer
NANOVIRICIDES, INC
Nanotechnology-based targeted anti-viral therapeutics
http://www.nanoviricides.com
eugene@nanoviricides.com
310-486-5677
Begin forwarded message:
From: Anil R Diwan NNVC <adiwan@nanoviricides.com>
Subject: Re: N&H changes
Date: September 24, 2013 10:03:11 PM PDT
To: EUGENE SEYMOUR <drgeno@mac.com>
Sure, it is an important finding. But it is quite logical. We have already accounted for such possibilities in designing nanoviricides.
Influenza virus carries two major surface proteins: H and N. BOTH ARE CAPABLE OF BINDING TO THE SIALIC ACID RECEPTOR. They have always been and they will always be. That is simply by definition of the virus itself.
H alone on the virus surface would allow binding followed by internalization. When virus progeny are created, they try to bud out of the cell, and the H on them gets stuck onto the sialic acid receptors outside, which causes the virus to remain stuck and not be able to be released for infecting another cell. N evolved beyond just binding to perform an enzymatic action. It cuts off the terminal sialic acid sugar, like scissors, thereby allowing the virus to walk away from the cell.
Yes, you can evolve, H into a protein that has reduced or very little binding to sialic acid. In this case, the virus binds to cells poorly, has poor infecting ability, and therefore would not cause much of disease (assuming other pathogenic transformations have not occurred). But in cell cultures, you can force the virus to grow.
In some of these viruses, at the same time, N may have evolved but retained its sialic acid binding and scissors activities. Then the case is as above.
However, in some cases, N can evolve such that its scissors activity is decreased. [and H has lost ability to bind the silaic acid]. Then naturally, N will take on the role of binding to cell surface and causing virus internalization. When the progeny virus is trying to escape, the new N has limited scissors activity, so some virus will be able to walk away, but much of it will remain stuck to cell surface. Again, such a virus would be very poor in its pathogenicity in intact host. However, in cell cultures in the lab, you can force these viruses to grow.
In all these cases, the virus still needs to bind to the same sialic acid receptor that we mimic on FluCide(tm). So FluCide will still be effective against the virus. Only, in the case of such a virus, it would be primarily N that binds to FluCide than H, just as in the case of host cells as these scientists have shown.
We have tried to "mimic" sialic acid rather than using sialic acid itself in creating FluCide. We believe that the sialic acid mimicking ligand attached on FluCide is much less susceptible to the scissors action of N (possibly not at all in the case of some types of N) compared to sialic acid. Thus the ligand does not get cut off by N from FluCide, or if it does, such activity is very weak, even with the native N, and same should be valid with the N that has improved its binding ability and decreased its scissors activity.
The rule that logically descends is that, if a virus does not bind to FluCide efficiently, then it would not bind to the cells efficiently either and in general should be very weak in its pathogenesis. It does not matter which protein(s) the virus is using for binding to its cell surface target.
You are right, the nanoviricides don't care, as long as the cell surface receptor for the virus remains the same.
-anil
Sincerely,
Anil R. Diwan, Ph.D.
President & Chairman
NanoViricides, Inc.
135 Wood Street, Ste. 205
West Haven, CT 06516.
Tel: 203-937-6137
Fax: 203-859-5059.
http://www.nanoviricides.com
A publicly traded Company: NNVC
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