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- W1882922602 abstract "Research Article1 November 1993free access Expression of conformationally constrained adhesion peptide in an antibody CDR loop and inhibition of natural killer cell cytotoxic activity by an antibody antigenized with the RGD motif. M. Zanetti M. Zanetti Department of Medicine, University of California at San Diego, La Jolla 92093-0961. Search for more papers by this author G. Filaci G. Filaci Department of Medicine, University of California at San Diego, La Jolla 92093-0961. Search for more papers by this author R.H. Lee R.H. Lee Department of Medicine, University of California at San Diego, La Jolla 92093-0961. Search for more papers by this author P. del Guercio P. del Guercio Department of Medicine, University of California at San Diego, La Jolla 92093-0961. Search for more papers by this author F. Rossi F. Rossi Department of Medicine, University of California at San Diego, La Jolla 92093-0961. Search for more papers by this author R. Bacchetta R. Bacchetta Department of Medicine, University of California at San Diego, La Jolla 92093-0961. Search for more papers by this author F. Stevenson F. Stevenson Department of Medicine, University of California at San Diego, La Jolla 92093-0961. Search for more papers by this author V. Barnaba V. Barnaba Department of Medicine, University of California at San Diego, La Jolla 92093-0961. Search for more papers by this author R. Billetta R. Billetta Department of Medicine, University of California at San Diego, La Jolla 92093-0961. Search for more papers by this author M. Zanetti M. Zanetti Department of Medicine, University of California at San Diego, La Jolla 92093-0961. Search for more papers by this author G. Filaci G. Filaci Department of Medicine, University of California at San Diego, La Jolla 92093-0961. Search for more papers by this author R.H. Lee R.H. Lee Department of Medicine, University of California at San Diego, La Jolla 92093-0961. Search for more papers by this author P. del Guercio P. del Guercio Department of Medicine, University of California at San Diego, La Jolla 92093-0961. Search for more papers by this author F. Rossi F. Rossi Department of Medicine, University of California at San Diego, La Jolla 92093-0961. Search for more papers by this author R. Bacchetta R. Bacchetta Department of Medicine, University of California at San Diego, La Jolla 92093-0961. Search for more papers by this author F. Stevenson F. Stevenson Department of Medicine, University of California at San Diego, La Jolla 92093-0961. Search for more papers by this author V. Barnaba V. Barnaba Department of Medicine, University of California at San Diego, La Jolla 92093-0961. Search for more papers by this author R. Billetta R. Billetta Department of Medicine, University of California at San Diego, La Jolla 92093-0961. Search for more papers by this author Author Information M. Zanetti1, G. Filaci1, R.H. Lee1, P. Guercio1, F. Rossi1, R. Bacchetta1, F. Stevenson1, V. Barnaba1 and R. Billetta1 1Department of Medicine, University of California at San Diego, La Jolla 92093-0961. The EMBO Journal (1993)12:4375-4384https://doi.org/10.1002/j.1460-2075.1993.tb06122.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info We report that an antibody engineered to express three Arg-Gly-Asp (RGD) repeats in the third complementarity-determining region of the heavy chain (antigenized antibody) efficiently inhibits the lysis of human erythroleukemia K-562 cells by natural killer (NK) cells. Synthetic peptides containing RGD did not inhibit. Inhibition was specific for the (RGD)3-containing loop and required simultaneous occupancy of the Fc receptor (CD16) on effector cells. The antigenized antibody inhibited other forms of cytotoxicity mediated by NK cells but not cytotoxicity mediated by major histocompatibility complex-restricted cytotoxic T lymphocytes (CTL). A three-dimensional model of the engineered antibody loop shows the structure and physicochemical characteristics probably required for the ligand activity. The results indicate that an RGD motif is involved in the productive interaction between NK and target cells. Moreover, they show that peptide expression in the hypervariable loops of an antibody molecule is an efficient procedure for stabilizing oligopeptides within a limited spectrum of tertiary structures. This is a new approach towards imparting ligand properties to antibody molecules and can be used to study the biological function and specificity of short peptide motifs, including those involved in cell adhesion. Previous ArticleNext Article Volume 12Issue 111 November 1993In this issue RelatedDetailsLoading ..." @default.
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- W1882922602 title "Expression of conformationally constrained adhesion peptide in an antibody CDR loop and inhibition of natural killer cell cytotoxic activity by an antibody antigenized with the RGD motif." @default.
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- W1882922602 doi "https://doi.org/10.1002/j.1460-2075.1993.tb06122.x" @default.
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