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National Science Foundation
Experimental Program to
Stimulate Competitive Research

Summer Undergraduate Diversity Research Program


Vanessa Thompson
Faculty Advisor
Dr. Jack Nunberg, Director
Montana Biotechnology Center

Mutagenic Analysis of the HIV Envelope
Glycoprotein Complex gp 120 - gp 41:
Determination of the Effects of a Single Alanine

Abstract

The envelope glycoprotein complex of the Human Immunodeficiency Virus (HIV) consists of two noncovalently bound subunits, gp120 and gp41, and is necessary for virion binding and fusion with a target host cell. While much is known about this complex, additional information about its structure and function will aid in the understanding of the HIV infection mechanism. The goal of this project was to determine the effects of a threonine-to-alanine substitution in gp41 on the stability of the gp41-gp120 association. The threonine 606 residue was selected as the site for investigation because it is highly conserved among most HIV-1 isolates. In addition, the region containing T606 has been strongly implicated in the association between gp120 and gp41. To accomplish the project goal, a mutation was engineered into the envelope glycoprotein genetic sequence changing amino acid 606 from its native threonine to an alanine. This mutated DNA was then introduced into monkey COS cells and resulting envelope glycoprotein expression was evaluated to determine the mutated glycoprotein's biosynthesis, stability and fusogenic potential. Presentation topics will include background information on HIV, experimental design, methodology and results from these studies.

 

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