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1 Laboratory for Infectious Diseases, Department 144, Hvidovre Hospital, Kettegård Allé 30, 2650 Hvidovre, Denmark
and2 Department of Clinical Virology, University of Göteborg, 413 46, Sweden
The V3 loop of the human immunodeficiency virus (HIV) surface protein, gp120, constitutes a principal neutralizing determinant. HIV strains lacking a naturally conserved N-linked oligosaccharide (at position 306) within the V3 loop are highly sensitive to neutralization. We subjected molecular clones of HIVLAI lacking this 306N-glycan to in vitro immune selection with MAbs directed against the V3 loop. In all, ten clones were characterized, and all proved resistant to V3-directed neutralization. Sequencing of the V3 loop revealed that six of the clones had become resistant at least partly by reacquisition of the 306N-glycan. Only two of the clones possessed mutations within the binding site of the antibody itself, while the two remaining clones did not display changes within the V3 loop itself. Thus, HIV strains lacking the 306N-glycan primarily develop resistance to V3-directed neutralization through acquisition of the specific oligosaccharide. This demonstrates that protein glycosylation can be a primary modifier of virus antigenicity of possible importance for the interaction of HIV with the host immune response.
* Author for correspondence. Fax +45 3647 4979. e-mail infejesh@inet.uni-c.dk
Received 12 July 1995;
accepted 14 December 1995.
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