This specificity of PmtMtu functionality means that expression of M. tuberculosis glycoproteins will be better achieved by using a related host-like S. coelicolor with a homologous glycosylation

system, rather than by attempting the heterologous expression of the M. tuberculosis glycosylation system. We are grateful to Dr. Y. López-Vidal for the gift of M. tuberculosis H37Rv DNA, to Dr. Antonio Vallecillo for providing M. smegmatis mc2155 cells, to Dr. F. Bigi for providing the bacterial two-hybrid system, and to the Unidad de Biología Molecular of the Instituto de Fisiología Celular-UNAM LGK-974 solubility dmso for DNA sequencing. This work was supported by research grant 103214 from the SEP-CONACyT mixed fund and by a scholarship to L.E.C.-D. from Consejo Nacional de Ciencia y Tecnología (Mexico) to support her PhD studies at the Programa de Doctorado en Ciencias Biomédicas, Universidad Nacional Autónoma de México. “
“In-Q-Tel, Inc., Arlington, Vincristine VA, USA TMG Biosciences, LLC, Incline Village, NV, USA Systematic Entomology Laboratory,

United States Department of Agriculture, Washington, DC, USA We describe here a strain of Yersinia pestis, G1670A, which exhibits a baseline mutation rate elevated 250-fold over wild-type Y. pestis. The responsible mutation, a C to T substitution in the mutS gene, results in the transition of a highly conserved leucine at position 689 to arginine (mutS(L689R)). When the MutSL689R protein of G1670A was expressed in a ΔmutS derivative of Y. pestis strain EV76, mutation rates observed were equivalent to those observed in G1670A, consistent with a causal association between the mutS mutation and the mutator phenotype. The observation of a mutator allele in Yersinia pestis has potential implications for the study of evolution of this and other

especially dangerous pathogens. “
“Université d’Angers, UMR1345, Institut de Recherches en Horticulture et Semences, Beaucouzé Cedex, France Insitut Micalis (UMR 1319/INRA-Agroparistech) INRA, Jouy en Josas Cedex, France The bacterium Erwinia amylovora causes fire blight, an invasive Y-27632 concentration disease that threatens apple trees, pear trees and other plants of the Rosaceae family. Erwinia amylovora pathogenicity relies on a type III secretion system and on a single effector DspA/E. This effector belongs to the widespread AvrE family of effectors whose biological function is unknown. In this manuscript, we performed a bioinformatic analysis of DspA/E- and AvrE-related effectors. Motif search identified nuclear localization signals, peroxisome targeting signals, endoplasmic reticulum membrane retention signals and leucine zipper motifs, but none of these motifs were present in all the AvrE-related effectors analysed. Protein threading analysis, however, predicted a conserved double β-propeller domain in the N-terminal part of all the analysed effector sequences.