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Development of monoclonal catalytic antibodies for HIV immunotherapy

Award Information
Agency: Department of Health and Human Services
Branch: National Institutes of Health
Contract: 1R41AI087527-01
Agency Tracking Number: R41AI087527
Amount: $173,142.00
Phase: Phase I
Program: STTR
Solicitation Topic Code: NIAID
Solicitation Number: PHS2010-2
Timeline
Solicitation Year: 2010
Award Year: 2010
Award Start Date (Proposal Award Date): N/A
Award End Date (Contract End Date): N/A
Small Business Information
MISSOURI CITY, TX 77459-
United States
DUNS: 830180282
HUBZone Owned: No
Woman Owned: No
Socially and Economically Disadvantaged: No
Principal Investigator
 STEPHANIE PLANQUE
 (713) 270-5391
 STEPHANIE.A.PLANQUE@UTH.TMC.EDU
Business Contact
 BENJAMIN ADLER
Phone: (713) 500-3999
Email: e_osp@uth.tmc.edu
Research Institution
 University Of Texas Hlth Sci Ctr Houston
 
Box 20036
HOUSTON, TX 77225-
United States

 () -
 Nonprofit College or University
Abstract

DESCRIPTION (provided by applicant): We have raised murine monoclonal antibodies (MAbs) to a conserved region of the CD4 binding site of gp120 (CD4bs) that neutralize genetically diverse HIV strains. The MAbs have a novel mechanism of action. They hydrolyze multiple molecules of gp120, thereby imparting MAb increased biological efficacy. About 10% of HIV infected subjects develop resistance to currently available drug regimens and have no other treatment options. Our MAbs are intended to fulfill this unmet medical need. In the present Phase I proposal, we will conduct molecular engineering and initial functional studies necessary to preparing therapy-grade MAbs. We will: (a) clone two chimeric MAbs (cMAbs) with reduced immunogenicity by fusing the murine catalytic variable domains to human IgG constant domains; (b) establish that the cMAbs express catalytic and epitope specificity properties comparable to the parent MAbs; (c) determine the potency with which the cMAbs neutralize genetically diverse HIV strains as the initial efficacy indicator; and (d) confirm the absence of cMAb cross-reaction with host human proteins, a requirement for a MAb designed for clinical use in humans. If the cMAbs meet the Phase I milestones, we will seek Phase II support for animal model efficacy tests, toxicity analysis and pharmacokinetic studies to enable human testing. PUBLIC HEALTH RELEVANCE: No adequate therapies are available for HIV infected patients who develop resistance to antiretroviral drugs. We will examine the feasibility of developing antibodies that degrade the coat protein of HIV for treatment of such patients.

* Information listed above is at the time of submission. *

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