HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

Cover caption:

Front cover illustration: What confers virus-neutralizing capacity to an antibody? Neutralizing antibodies bind to epitopes on native antigens exposed on the virion surface. Viruses counter with numerous mechanisms of resistance, including amino acid variation, carbohydrate masking and oligomeric occlusion. These are illustrated in a trimeric model of the HIV-1 outer envelope glycoprotein, gp120, the target of most HIV-1-neutralizing antibodies. The view is of the oligomer facing outwards from the virus surface. A Calpha worm of a truncated gp120 is shown in red; green depicts differences in core amino acid residues between gp120 of a T-cell line-adapted (TCLA) strain of HIV-1, which is highly sensitive to neutralization, and a primary isolate (PI), which is generally resistant. Glycosylation, with some differences between isolates, is also indicated. A striking concentration of core residues that differ between the isolates and of carbohydrate attachment is seen on the exposed oligomer surface. The tightness or openness of the subunit association in the trimer determines the degree of oligomeric shielding of epitopes: this has a major influence on neutralization sensitivity. See the article by P. J. Klasse and Q. J. Sattentau on pages 2091-2108 of this issue. The image is reproduced courtesy of Peter Kwong and with kind permission from Elsevier Science (Kwong et al., Structure 8, 1329-1339, 2000).

[Table of Contents]