Summary and Conclusions
We tried to determine amino acid motifs of Y. pestis plasminogen activator (Pla) involved in laminin binding. We selected heptamer peptides using a random phage library which was tested against immobilised laminin. Two sequences seemed to inhibit Pla mediated laminin binding of E. coli and exhibited a strong laminin binding capacity revealing a competition with Pla for the same laminin binding site. The motifs are also involved in plasminogen activation because they caused fibrinolysis on fibrin films. The patterns were localised outside the putative surface-exposed loops (Kukkonen et al., 2001).
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References
Kukkonen, M, Lähteenmäki, K, Suomalainen, M, Kalkkinen, N, Emödy, L, Lång, H, Korhonen, T. K. 2001. Protein regions important for plasminogen activation and inactivation of alpha 2-antiplasmin in the surface protease Pla of Yersinia pestis. Mol Microbiol, 40: 1097–1111
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© 2004 Kluwer Academic Publishers
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Benedek, O., Bene, J., Melegh, B., Emődy, L. (2004). Mapping of Possible Laminin Binding Sites of Y. pestis Plasminogen Activator (Pla) via Phage Display. In: Skurnik, M., Bengoechea, J.A., Granfors, K. (eds) The Genus Yersinia. Advances in Experimental Medicine and Biology, vol 529. Springer, Boston, MA. https://doi.org/10.1007/0-306-48416-1_18
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DOI: https://doi.org/10.1007/0-306-48416-1_18
Publisher Name: Springer, Boston, MA
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