Fig. 3.
Neutrophil-binding phage peptide sequences isolated from the cyclic (CL10) phage display library. Selection and sequencing of phage was performed as described in the text. The peptides displayed by the phage recovered from the experiments performed at 4°C are aligned to the consensus motif DLXTSK(M/L)X(V/I/L) that was previously identified with the linear nonapeptide library. Identical residues and conservative substitutions are shown in bold. Underlined residues represent the putative linker sequences which, in several clones, diverge from the linker sequences designed by the library construction (see Fig 1) due to the absence of the cysteine residues. The phage clones recovered from the cell-associated fraction at 20°C are aligned to form the consensus motif CXXGXFLGXWLC. One phage in the eluate fraction at 20°C (first from the top) shows a high degree of homology with the FGPNLTGRW displaying phage recovered with the J404 library under the same experimental conditions, representing a structurally related sequence. Other possible consensus motifs are tentatively grouped and shown in bold.