Literature DB >> 7488001

The synthetic [Tyr5,12,Lys7]-polyphemusin II peptide (T22) binds to the CD4 cell surface molecule.

B S Weeks1, M Nomizu, A Otaka, C A Weston, A Okusu, H Tamamura, N Yamamoto, N Fujii.   

Abstract

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.

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Year:  1995        PMID: 7488001     DOI: 10.1006/bbrc.1995.2510

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  1 in total

1.  Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database.

Authors:  Guangshun Wang; Karen M Watson; Alan Peterkofsky; Robert W Buckheit
Journal:  Antimicrob Agents Chemother       Date:  2010-01-19       Impact factor: 5.191

  1 in total

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