Document 1972 DOCN M94A1972 TI A miniantibody to HIV neutralizes HIV strains. DT 9412 AU Levi M; Hinkula J; Ruden U; Osterhaus A; Wigzell H; Wahren B; Dept. Clin. Virol., Karolinska Institute, Stockholm, Sweden. SO Int Conf AIDS. 1994 Aug 7-12;10(1):41 (abstract no. 139A). Unique Identifier : AIDSLINE ICA10/94370603 AB OBJECTIVE: To reveal important regions of HIV neutralizing antibodies. METHODS: A complementarity-determining region (CDR) of the mouse monoclonal antibody (mAb) F58 was constructed with specificity to a neutralization-inducing region of human immunodeficiency virus type 1 (HIV-1). The mAb has its major reactivity to the amino acid sequence I-GPGRA in the V3 viral envelope region. All CDRs including several framework amino acids were synthesized from the sequence deduced by cloning and sequencing mAB F58 heavy- and light-chain variable domains. RESULTS: Peptides derived from the third heavy-chain domain (CDR-H3) alone or in combination with the other CDR sequences competed with F58 mAb for the V3 region. The CDR-H3 peptide was chemically modified by cyclization, substitution or deletion and then inhibited HIV-1 replication as well as syncytium formation by infected cells. Both the homologous IIIB viral strain to which the F58 mAb was induced and the heterologous SF2 strain were inhibited. Passive immunization of HIV-challenged immunodefective mice and eleven HIV infected patients indicated an in vivo HIV inhibitory effect of the parental monoclonal antibody. CONCLUSION: This synthetic peptide had unexpectedly potent antiviral activity and may be a potential tool for treatment of HIV infected persons. DE Amino Acid Sequence Animal Antibodies, Monoclonal/GENETICS/*IMMUNOLOGY Antiviral Agents/THERAPEUTIC USE Genes, Immunoglobulin Human HIV Antibodies/*BIOSYNTHESIS/GENETICS/IMMUNOLOGY HIV-1/*IMMUNOLOGY Immunoglobulin Variable Region/*BIOSYNTHESIS Mice MEETING ABSTRACT SOURCE: National Library of Medicine. NOTICE: This material may be protected by Copyright Law (Title 17, U.S.Code).