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New Details About Epitope Targeted By Potent Monoclonal Antibody.(Brief Article)

Vaccine Weekly

| November 21, 2001 | COPYRIGHT 2001 NewsRX. This material is published under license from the publisher through the Gale Group, Farmington Hills, Michigan.  All inquiries regarding rights should be directed to the Gale Group. (Hide copyright information)Copyright

2001 NOV 21 - (NewsRx.com & NewsRx.net) -- by Michael Greer, senior medical writer - Researchers in the United States and Europe say that they have shed new light on a potential HIV vaccine target.

In a multi-institutional study, Carol E. Parker, University of North Carolina - Chapel Hill, and colleagues sought to "identify the functional epitope on human immunodeficiency virus envelope glycoprotein gp41 for the broadly neutralizing anti-gp41 human monoclonal antibody 2F5."

With the aid of mass spectrometry, Parker and coworkers were able to provide new details about the structure of this important epitope.

The researchers first bound a soluble form of gp140 protein to immobilized 2F5, then used proteolytic enzymes to cut away exposed residues. The remaining residues were identified with matrix-assisted laser desorption ionization (MALDI) mass spectrometry, they said.

Using this data, Parker's team were able to determine that the epitope neutralized by 2F5 is 16 amino acid residues long, with the sequence NEQELLELDKWASLWN. It can be found near the gp41 C terminus, according to their report.

Previous research had suggested that 2F5's target epitope was only composed of six amino acid residues (Fine definition of the epitope on the gp41 glycoprotein of human immunodeficiency virus type 1 for the neutralizing ...

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