Document 0844
 DOCN  M9540844
 TI    Identification of an N-linked glycan in the V1-loop of HIV-1 gp120
       influencing neutralization by anti-V3 antibodies and soluble CD4.
 DT    9504
 AU    Gram GJ; Hemming A; Bolmstedt A; Jansson B; Olofsson S; Akerblom L;
       Nielsen JO; Hansen JE; Laboratory for Infectious Diseases, Hvidovre
       Hospital, Denmark.
 SO    Arch Virol. 1994;139(3-4):253-61. Unique Identifier : AIDSLINE
       MED/95134083
 AB    Glycosylation is necessary for HIV-1 gp120 to attain a functional
       conformation, and individual N-linked glycans of gp120 are important,
       but not essential, for replication of HIV-1 in cell culture. We have
       constructed a mutant HIV-1 infectious clone lacking a signal for
       N-linked glycosylation in the V1-loop of HIV-1 gp120. Lack of an
       N-linked glycan was verified by a mobility enhancement of mutant gp120
       in SDS-gel electrophoresis. The mutated virus showed no differences in
       either gp120 content per infectious unit or infectivity, indicating that
       the N-linked glycan was neither essential nor affecting viral
       infectivity in cell culture. We found that the mutated virus lacking an
       N-linked glycan in the V1-loop of gp120 was more resistant to
       neutralization by monoclonal antibodies to the V3-loop and
       neutralization by soluble recombinant CD4 (sCD4). Both viruses were
       equally well neutralized by ConA and a conformation dependent human
       antibody IAM-2G12. This suggests that the N-linked glycan in the V1-loop
       modulates the three-dimensional conformation of gp120, without changing
       the overall functional integrity of the molecule.
 DE    Amino Acid Sequence  Antibodies, Monoclonal/IMMUNOLOGY  Antigens,
       CD4/*IMMUNOLOGY  Base Sequence  Cell Line  Cell Survival  Concanavalin
       A/IMMUNOLOGY  Glycosylation  Human  HIV Antibodies/IMMUNOLOGY  HIV
       Antigens/BIOSYNTHESIS  HIV Envelope Protein
       gp120/*CHEMISTRY/GENETICS/*IMMUNOLOGY
       HIV-1/*CHEMISTRY/IMMUNOLOGY/PHYSIOLOGY  Molecular Sequence Data
       Mutagenesis  Neutralization Tests  Peptide
       Fragments/*CHEMISTRY/GENETICS/*IMMUNOLOGY  Polysaccharides/CHEMISTRY
       Protein Conformation  Recombinant Proteins/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).