Abstract:
: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. 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 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. This synthetic peptide had unexpectedly potent antiviral activity and may be a potential tool for treatment of HIV-infected persons.
journal_name
Proc Natl Acad Sci U S Aauthors
Levi M,Sällberg M,Rudén U,Herlyn D,Maruyama H,Wigzell H,Marks J,Wahren Bdoi
10.1073/pnas.90.10.4374subject
Has Abstractpub_date
1993-05-15 00:00:00pages
4374-8issue
10eissn
0027-8424issn
1091-6490journal_volume
90pub_type
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