Document 1928
 DOCN  M94A1928
 TI    A naturally occurring single amino acid substitution within the V3
       region of HIV-1 ENV protein affects the viral cellular host range and
       antigenic structure.
 DT    9412
 AU    Shioda T; Oka S; Ida S; Nokihara K; Toriyoshi H; Mori S; Takebe Y;
       Kimura S; Shimada K; Nagai Y; Institute of Medical Science, Univ. of
       Tokyo, Japan.
 SO    Int Conf AIDS. 1994 Aug 7-12;10(1):42 (abstract no. 143A). Unique
       Identifier : AIDSLINE ICA10/94370647
 AB    OBJECTIVE: To examine sequence changes in the V3 domain of gp120 during
       the course of HIV-1 infection and to learn their significance for the
       viral cellular host range and antigenic drift. METHODS: Sera
       sequentially obtained from an infected individual were subjected to
       reverse-transcription of the V3 region followed by PCR and cloning by
       the TA cloning kit. Multiple clones thus obtained at each time point
       were sequenced. Recombinant viruses carrying different V3 sequences were
       generated and tested for their in vitro cellular tropism. Synthetic
       peptides mimicking the V3 sequence were used for ELISA as antigens.
       RESULTS: All the clones obtained at the clinical phase I had aspartic
       acid (D) at position 323 in the V3, but this residue was replaced with
       lysine (K) in about one-third of the clones at the phase IV. This single
       amino acid change led to broadening cell tropism in vitro and resulted
       in different recognition by several of anti HIV human sera. CONCLUSIONS:
       V3 domain may evolve in vivo to increase net charge to broaden in vitro
       cell tropism and to drift antigenically in the disease course. This
       notion appear to be worthy of assessing with more clinical cases.
 DE    *Amino Acid Sequence  Antigenic Variation  Cloning, Molecular  Human
       HIV Antigens/*ULTRASTRUCTURE  HIV Envelope Protein gp120/*GENETICS
       HIV-1/*GENETICS  Polymerase Chain Reaction  Viral Envelope
       Proteins/*ULTRASTRUCTURE  MEETING ABSTRACT

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       protected by Copyright Law (Title 17, U.S.Code).