, 62 5%) were also predicted not to be secreted by each of

, 62.5%) were also predicted not to be secreted by each of GSK1210151A ic50 the in silico methods, but among the 11 proteins that we showed or confirmed to be T3S substrates, 10 (i.e., 83%) were also predicted to be secreted by at least one of the in silico methods. Overall, this indicates some correlation between our experimental

data and the in silico methods that predict T3S substrates. However, for many proteins, each of these in silico methods generates different predictions (see Additional file 3: Table S3). It is possible that the quantitative data on T3S such as the one we generated in this and in a previous study [45], can be used to normalize and improve the predictive value of such methods. Conclusions We found 10 C. {Selleck Anti-diabetic Compound Library|Selleck Antidiabetic Compound Library|Selleck Anti-diabetic Compound Library|Selleck Antidiabetic Compound Library|Selleckchem Anti-diabetic Compound Library|Selleckchem Antidiabetic Compound Library|Selleckchem Anti-diabetic Compound Library|Selleckchem Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|buy Anti-diabetic Compound Library|Anti-diabetic Compound Library ic50|Anti-diabetic Compound Library price|Anti-diabetic Compound Library cost|Anti-diabetic Compound Library solubility dmso|Anti-diabetic Compound Library purchase|Anti-diabetic Compound Library manufacturer|Anti-diabetic Compound Library research buy|Anti-diabetic Compound Library order|Anti-diabetic Compound Library mouse|Anti-diabetic Compound Library chemical structure|Anti-diabetic Compound Library mw|Anti-diabetic Compound Library molecular weight|Anti-diabetic Compound Library datasheet|Anti-diabetic Compound Library supplier|Anti-diabetic Compound Library in vitro|Anti-diabetic Compound Library cell line|Anti-diabetic Compound Library concentration|Anti-diabetic Compound Library nmr|Anti-diabetic Compound Library in vivo|Anti-diabetic Compound Library clinical trial|Anti-diabetic Compound Library cell assay|Anti-diabetic Compound Library screening|Anti-diabetic Compound Library high throughput|buy Antidiabetic Compound Library|Antidiabetic Compound Library ic50|Antidiabetic Compound Library price|Antidiabetic Compound Library cost|Antidiabetic Compound Library solubility dmso|Antidiabetic Compound Library purchase|Antidiabetic Compound Library manufacturer|Antidiabetic Compound Library research buy|Antidiabetic Compound Library order|Antidiabetic Compound Library chemical structure|Antidiabetic Compound Library datasheet|Antidiabetic Compound Library supplier|Antidiabetic Compound Library in vitro|Antidiabetic Compound Library cell line|Antidiabetic Compound Library concentration|Antidiabetic Compound Library clinical trial|Antidiabetic Compound Library cell assay|Antidiabetic Compound Library screening|Antidiabetic Compound Library high throughput|Anti-diabetic Compound high throughput screening| trachomatis proteins (CT053, CT105, CT142, CT143, CT144, CT161, CT338, CT429, CT656, and CT849) with a high likelihood BIX 1294 manufacturer of being T3S substrates, and therefore possible effectors delivered by the bacteria into host cells. For 6 of these proteins (CT053, CT105, CT142, CT143, CT338, and CT429), the hypothesis that they could be effectors was supported by their capacity of being translocated into host cells and by the expression of their encoding genes by C. trachomatis. The identification of all C. trachomatis effectors is a crucial step towards a comprehensive understanding of the mechanisms by which this pathogen subverts host cells. The recently developed methods for genetic manipulation of

Chlamydia indicate that it should be possible to ectopically express candidate effectors in C. trachomatis[17, 78], which would facilitate the analysis of their translocation into host cells. Our work highlights C. trachomatis proteins that should

be prioritized in such studies, thus aiding many the future identification of chlamydial effectors. Furthermore, the quantitative analysis of T3S of TEM-1 hybrid proteins that we carried out could help to further develop the in silico methods for identification of T3S substrates [28–30, 56]. Acknowledgements This work was supported by Fundação para a Ciência e a Tecnologia (FCT) through grants ERA-PTG/0005/2010 (in the frame of ERA-NET PathoGenoMics) to LJM, ERA-PTG/0004/2010 (in the frame of ERA-NET PathoGenoMics) to JPG, and PEst-OE/EQB/LA0004/2011; by the European Commission through a Marie Curie European Re-integration Grant (PERG03-GA-2008-230954) to LJM; and by a European Society for Clinical Microbiology and Infectious Diseases (ESCMID) research grant to LJM. MdC, FA, and VB hold PhD fellowships SFRH/BD/62728/2009, SFRH/BD/73545/2010, and SFRH/BD/68527/2010, respectively, from FCT. Electronic supplementary material Additional file 1: Table S1: Plasmids used and constructed in this work. (PDF 105 KB) Additional file 2: Table S2: Primers used in this work for construction of plasmids. (PDF 207 KB) Additional file 3: Table S3: Summary of results obtained in analyses of T3S signals in proteins of Chlamydia trachomatis and comparison to in silico prediction methods. (XLSX 18 KB) References 1.

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