Document 0536
 DOCN  M9460536
 TI    An N-glycan within the human immunodeficiency virus type 1 gp120 V3 loop
       affects virus neutralization.
 DT    9404
 AU    Back NK; Smit L; De Jong JJ; Keulen W; Schutten M; Goudsmit J; Tersmette
       M; Department of Virology, University of Amsterdam, Academic Medical;
       Center, The Netherlands.
 SO    Virology. 1994 Mar;199(2):431-8. Unique Identifier : AIDSLINE
       MED/94167877
 AB    Carbohydrate side chains of envelope glycoproteins of HIV-1 and other
       viruses have been postulated to interfere with binding of neutralizing
       antibodies. So far, however, little evidence for interference of
       specific N-glycans with virus neutralization has been provided. We used
       four infectious HIV-1 molecular clones chimeric for their gp 120 V3
       domains to study the influence on HIV-1 neutralization of an N-glycan
       localized within the V3 loop. Two clones lacking the 301N-glycan were at
       least 8-fold more sensitive to neutralization by two V3-specific
       monoclonal antibodies (MAbs) and 2- to 10-fold more sensitive to
       neutralization by a CD4-binding-site-specific human MAb than two HIV-1
       clones glycosylated at this site. The affinity of the V3 MAbs for
       soluble gp120 of the four clones was similar. However, a decreased
       binding of these MAbs to the gp120 of the two 301N-glycosylated clones
       was observed when the majority of gp120 was virion-associated during the
       initial binding step. These findings indicate that the 301N-glycan may
       interfere with the binding of neutralizing antibodies by limiting the
       accessibility of neutralization sites or by inducing conformational
       changes in the HIV-1 gp120 molecule.
 DE    Amino Acid Sequence  Antibodies, Monoclonal  Antigens, CD4/*IMMUNOLOGY
       Chimeric Proteins/IMMUNOLOGY  Cloning, Molecular  Glycosylation  Hela
       Cells  Human  HIV Envelope Protein gp120/*IMMUNOLOGY  HIV-1/*IMMUNOLOGY
       Molecular Sequence Data  Neutralization Tests
       Polysaccharides/*IMMUNOLOGY  Support, Non-U.S. Gov't  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).