from host antimicrobial defences, allows access to deeper tissues and provides a reservoir for persistent or recurring infections. FnBPs contain multiple tandem fibronectin-binding repeats (FnBRs) which bind fibronectin with varying affinity but it is unclear what selects for this configuration. Since

detected an expanded footprinted region in D. funebris that contains various adjacent binding sites with different binding affinities. ADF-1 was described to direct sequence-specific DNA binding to sites consisting of the multiple trinucleotide repeat GC=T C=T 45. The ADF-1 recognition sites with high

:403-410) fails to detect significant pairwise similarity between any of the sequences, the repeats present in these outer membrane proteins, taken as a whole, are highly significant (based on a generally applicable statisti-cal test for motifs described here). Analysis of bacterial porins with known trimeric 0

-pacity to bind 125l-fibronectln as well as fibronectin-coated sheep erythrocytes. The bind-ing of ‘25I-flbronectln-gelatin complexes was inhibited by excess unlabeled fibronectin. We calculated that specific high-affinity (Kd = 7.46 x iO M) binding sites for fibronectin exist on Kupfter cells

MEME (Multiple EM for Motif Elicitation) is one of the most widely used tools for searching for novel ‘signals ’ in sets of biological sequences. Applica-tions include the discovery of new transcription factor binding sites and protein domains. MEME worksbysearching for repeated, ungappedsequence

, but not on polylysine or on uncoated plastic. Integrin mediation of this effect was suggested by finding the same pattern of elevated tyrosine phosphorylation in cells plated on the cell-binding fragment of fibronectin and in ceils plated on a synthetic polymer containing multiple RGD sequences. We have identified one

high-affinity Fn-binding region of LigB has been localized to LigBCen2, which contains the partial 11th and full 12th Ig-like repeats (LigBCen2R) and 47 amino acids of the non-repeat region (LigBCen2NR) of LigB. In this study, the gelatin binding domain of fibronectin was shown to interact with Lig

DNA sequence of the serum opacity factor of group A streptococci: identification of a fibronectin-binding repeat domain.

binding and self-assembly. Here, we use single-molecule force spectroscopy to examine the mechanical properties of fibronectin (FN) and its individual FNIII domains. We found that fibronectin is highly extensible due to the unfolding of its FNIII domains. We found that the native FNIII region displays

-specific antibody immunity. No patient developed HER-2/neu protein-specific T cell or antibody immunity. The majority of peptides exhibited high binding affinity, in vitro,to>3 of the 14 DR alleles analyzed. Conclusion: The group of peptides used in this study demonstrated high binding affinity to multiple DR