aeruginosa (Barraud et al, 2009) and S oneidensis (Plate & Marl

aeruginosa (Barraud et al., 2009) and S. oneidensis (Plate & Marletta, 2012) could not be ruled out in A. brasilense Sp245. The genetic approach to unravel these important mechanisms in A. brasilense will shed light on the biofilm and root colonization development. We thank J.L. Córdoba for his Roxadustat manufacturer technical help with confocal microscopy and F. Lucca for providing key equipment. This

project was funded by Consejo Nacional de Ciencia y Tecnología (CONACyT grant CB-2010-01-154914) awarded to B.E. Baca, SECyT, UNMdP (AGR 285/09) awarded to C.M. Creus and a bilateral grant from Ministerio de Ciencia y Tecnología (MINCYT of Argentina) and CONACyT (México). No author of this work has any conflict of interest. A. Arruebarrena Di Palma and C.M. Pereyra are joint first authors and contributed equally to this work. “
“In this work we report the isolation and the characterization of 79 Streptomyces isolates from a French forest soil. The 16S rRNA gene phylogeny indicated that a great diversity of Streptomyces was present in this soil, with at least nine different and potentially new species. Growth plate assays showed that most Streptomyces lineages exhibit cellulolytic and hemicellulolytic capacities and potentially participate in wood decomposition. Molecular screening for a specific hydrogenase also indicated a widespread potential for CP-868596 in vivo atmospheric H2 uptake. Co-culture experiments with representative

strains showed antagonistic effects between Streptomyces of the same population and between Streptomyces and various fungi. Interestingly, in certain conditions, growth promotion of some fungi

also occurred. We conclude that in forest soil, Streptomyces populations exhibit many important functions involved in different biogeochemical cycles and also influence the structure of soil microbial communities. “
“U.S. Department of Agriculture, Glycogen branching enzyme Agricultural Research Service, Crop Diseases, Pests, and Genetics Unit, Parlier, CA, USA The Mycoplasma pulmonisVsa proteins are a family of size- and phase-variable lipoproteins that shield the mycoplasmas from complement and modulate attachment to abiotic surfaces. Mycoplasmas producing a long Vsa protein hemadsorb poorly and yet are proficient at colonizing rats and mice. The effect of the length of the Vsa protein on the attachment of mycoplasmas to epithelial cells has not been previously explored. We find that independent of Vsa isotype, mycoplasmas producing a long Vsa protein with many tandem repeats adhere poorly to murine MLE-12 cells compared with mycoplasmas producing a short Vsa. We also find that mutants lacking the EPS-I polysaccharide of M. pulmonis exhibited decreased adherence to MLE-12 cells, even though it has been shown previously that such mutants have an enhanced ability to form a biofilm. The mycoplasmas are prokaryotic pathogens of humans and other animals, distinguished by the lack of a cell wall, diminutive size, and a limited genome.

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