       Document 0007
 DOCN  M9620007
 TI    The synthetic [Tyr5,12,Lys7]-polyphemusin II peptide (T22) binds to the
       CD4 cell surface molecule.
 DT    9602
 AU    Weeks BS; Nomizu M; Otaka A; Weston CA; Okusu A; Tamamura H; Yamamoto N;
       Fujii N; Department of Medicine, University of Pennsylvania,
       Philadelphia; 19104, USA.
 SO    Biochem Biophys Res Commun. 1995 Oct 13;215(2):626-31. Unique Identifier
       : AIDSLINE MED/96011824
 AB    The [Tyr5,12,Lys7]-polyphemusin II peptide (T22) inhibits HIV-1
       replication in lymphocytes. The mechanism of T22 inhibition of HIV-1
       replication may involve T22 competition with HIV-1 for attachment sites
       on the plasma membrane of targeted cells. Here we find that the T22
       peptide binds to the CD4 molecule in affinity columns. We also find that
       antiserum to CD4 inhibits cell attachment to T22. Further CD4+
       transfected cells attach to T22 while their parental cells which do not
       express CD4 do not attach to T22. These data demonstrate that T22 binds
       to the CD4 molecule and supports the hypothesis that T22 inhibits HIV-1
       replication by binding to the cell surface CD4 molecule and inhibiting
       uptake of the virus.
 DE    Amino Acid Sequence  Antigens, CD/ISOLATION & PURIF/*PHYSIOLOGY
       Antigens, CD4/ISOLATION & PURIF/*PHYSIOLOGY  Antiviral
       Agents/CHEMISTRY/*METABOLISM/PHARMACOLOGY  Binding Sites  Binding,
       Competitive  Cell Adhesion/DRUG EFFECTS  Cell Line  Chromatography,
       Affinity  Hela Cells  Human  HIV-1/DRUG EFFECTS/*PHYSIOLOGY  Kinetics
       Molecular Sequence Data  Peptides/CHEMISTRY/*METABOLISM/PHARMACOLOGY
       Protein Conformation  Virus Replication/DRUG EFFECTS  JOURNAL ARTICLE

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

