Molecular characterization of L-413C, a P2-related plague diagnostic bacteriophage.
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.
Chemistry, Materials and Life Sciences Directorates Lawrence Livermore National Laboratory, Livermore, CA 94550, USA. garcia12@llnl.gov
Emilio
E
Garcia
Patrick
P
Chain
Jeff M
JM
Elliott
Alexander G
AG
Bobrov
Vladimir L
VL
Motin
Olga
O
Kirillina
Victoria
V
Lao
Richard
R
Calendar
Andrey A
AA
Filippov
D017901:Bacteriophage P2 / Q000145:classification* / Q000235:genetics* / Q000302:isolation & purification / Q000502:physiology; D004262:DNA Restriction Enzymes; D004926:Escherichia coli / Q000378:metabolism / Q000821:virology; D016679:Genome, Viral; D008242:Lysogeny; D008969:Molecular Sequence Data; D010930:Plague / Q000382:microbiology; D017422:Sequence Analysis, DNA; D013045:Species Specificity; D014764:Viral Proteins; D015010:Yersinia pestis / Q000821:virology*; D015011:Yersinia pseudotuberculosis / Q000821:virology
D014764:Viral Proteins; D004262:DNA Restriction Enzymes; C089629:endodeoxyribonuclease EcoKI