Plague Research Today is a free monthly online journal that collates and summarizes the latest research about Plague, including details on bubonic plague, yersinia pestis, infection, types, treatment.

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

Garcia E, Chain P, Elliott JM, Bobrov AG, Motin VL, Kirillina O, Lao V, Calendar R, Filippov AA

Chemistry, Materials and Life Sciences Directorates Lawrence Livermore National Laboratory, Livermore, CA 94550, USA. garcia12@llnl.gov

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.

Published 15 February 2008 in Virology, 372(1): 85-96.
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