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Home › Publications › Molecular characterization of L-413C, a P2-related plague diagnostic bacteriophage

Molecular characterization of L-413C, a P2-related plague diagnostic bacteriophage

Published in:

Virology 372(1) , 85-96 (Mar 1 2008)

Author(s):

Garcia, E., Chain, P., Elliott, J. M., Bobrov, A. G., Motin, V. L., Kirillina, O., Lao, V., Calendar, R., Filippov, A. A.

DOI:

DOI 10.1016/j.virol.2007.10.032

Abstract:

Our analysis of the plague diagnostic phage L-413C genome sequence and structure reveals that L-413C is highly similar and collinear with enterobacteriophage P2, though important differences were found. Of special interest was the mosaic nature of the tail fiber protein H in L-413C, given the differentiating specificity of this phage for Yersinia pestis vs. Yersinia pseudotuberculosis. While the N-terminal 207 and C-terminal 137 amino acids of L-413C display significant homology with the P2 H protein, a large (465 amino acid) middle section appears to be derived from a T4-related H protein, with highest similarity to the T6 and RB32 distal tail fibers. This finding along with appropriate preadsorption experiments suggest that the unique H protein of L-413C may be responsible for the specificity of this phage for Y. pestis, and that the Y. pestis receptors that are recognized and bound by L-413C either do not exist in Y. pseudotuberculosis or have a different structure. (C) 2007 Elsevier Inc. All rights reserved.

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