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This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Mazzucchelli, L. Articles by Parkos, C. A. Search for Related Content PubMed PubMed Citation Articles by Mazzucchelli, L. Articles by Parkos, C. A. Related Collections Phagocytes Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, Vol. 93 No. 5 (March 1), 1999: pp. 1738-1748 Cell-Specific Peptide Binding by Human Neutrophils Luca Mazzucchelli, James B. Burritt, Algirdas J. Jesaitis, Asma Nusrat, Tony W. Liang, Andrew T. Gewirtz, Frederick J. Schnell, and Charles A. Parkos From the Department of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, MA; the Department of Pathology and Laboratory Medicine, Emory University, Atlanta, GA; and the Department of Microbiology, Montana State University, Bozeman, MT. Analysis of peptide binding to human neutrophils (PMN) using phage display techniques has revealed cell-specific motifs reactive with the PMN surface. Phage libraries displaying either linear 9-mer or cyclic 10-mer and 6-mer peptides were incubated with normal human neutrophils followed by elution of bound phage with low pH (pH 2.2) and non-ionic detergent. Three rounds of selection generated several related peptide sequences that bound with high avidity to PMN. Using the linear 9-mer library, PMN-binding phage expressed peptides with the motif (G/A)PNLTGRW. The binding of phage bearing this motif was highly specific since no binding was observed on lymphocytes, fibroblasts, epithelial, or endothelial cells. Functional assays revealed that phage bearing the sequence FGPNLTGRW induced a pertussis toxin-sensitive increase in PMN cytosolic calcium analogous to that observed with Gi coupled receptors. Other prominent motifs identified included phage bearing the consensus DLXTSK(M/L)X(V/I/L), where X represents a non-conserved position. Phage with this motif bound exclusively to a sub population of human PMN that comprised approximately 50% of the total and did not elicit a calcium response. The binding of such phage to PMN was prevented by co-incubation with competing peptides displaying identical or similar sequences (IC50 range from 0.6 µmol/L to 50 µmol/L for DLXTSK and GPNLTG, respectively). We speculate that these techniques will be useful in identifying functional cell-specific binding motifs and contribute to the development of new therapeutic and diagnostic strategies in human disease. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? 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