Editing Abzyme (section)

==Potential HIV treatment==

In a June 2008 issue of the journal Autoimmunity Review,<ref>{{Cite journal | pmid = 18558365| year = 2008| last1 = Planque| first1 = S| title = Catalytic antibodies to HIV: Physiological role and potential clinical utility| journal = Autoimmunity Reviews| volume = 7| issue = 6| pages = 473–9| last2 = Nishiyama| first2 = Y| last3 = Taguchi| first3 = H| last4 = Salas| first4 = M| last5 = Hanson| first5 = C| last6 = Paul| first6 = S| doi = 10.1016/j.autrev.2008.04.002| pmc = 2527403}}</ref><ref name="physorg">{{cite web |url=http://www.physorg.com/news135360794.html |title=UT pathologists believe they have pinpointed Achilles heel of HIV |work=physorg.com |access-date=2008-07-16}}</ref> researchers S. Planque, Sudhir Paul, Ph.D., and Yasuhiro Nishiyama, Ph.D. of the University Of Texas Medical School at Houston announced that they have engineered an abzyme that degrades the superantigenic region of the [[gp120]] [[CD4]] binding site. This is the one part of the [[HIV]] [[virus]] outer coating that does not change, because it is the attachment point to [[T lymphocytes]], the key cell in [[cell-mediated immunity]]. Once infected by HIV, patients produce antibodies to the more changeable parts of the viral coat. The antibodies are ineffective because of the virus' ability to change their coats rapidly. Because this protein gp120 is necessary for HIV to attach, it does not change across different strains and is a point of vulnerability across the entire range of the HIV variant population.

The abzyme does more than bind to the site: it catalytically destroys the site, rendering the virus inert, and then can attack other HIV viruses. A single abzyme molecule can destroy thousands of HIV viruses.