Different genes with the same predicted function, such as putative metallopeptidases (LIC11149 and LIC10271),
sensor or receiver proteins of two-component response regulators (LIC20012, LIC11201, LIC12807, LIC12979 and LIC13289), and adenylate/guanylate cyclase (LIC10900 and LIC11095) were found to be regulated in opposite directions. GSK1210151A molecular weight LIC20012, an ortholog of hklep {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| encoding a sensor kinase of the Hklep/Rrlep two-component system involved in heme biosynthesis in L. biflexa [54], was down-regulated. However, an ortholog of rrlep regulator (LIC20013) was not differentially expressed. Moreover, predicted anti-sigma factor (LIC13344) and anti-sigma factor antagonists (LIC10344 and LIC20108) were down-regulated in response to serum. Bacterial anti-sigma factors and anti-sigma factor antagonists are regulatory proteins that control sigma-factor functions in promoter recognition and initiation of RNA polymerase required for cell viability and stress response [55]. Anti-sigma factors bind to and block their cognate sigma factors, while anti-sigma factor antagonists
(or anti-anti-sigma factors) form complexes with anti-sigma factors to inhibit their activity. These findings may be attributed to the fact that the genome of L. interrogans is predicted to contain at least 79 genes encoding two-component sensor histidine kinase-response Selleckchem BIX 1294 regulator proteins, 9 anti-sigma factors, and 19 anti-sigma factor antagonists required for response to various environmental signals [34]. Therefore, complex stimuli in serum encountered by Leptospira may simultaneously cause induction and repression of multiple genes involved in signal transduction networks and transcriptional regulation, possibly leading to expression of genes essential for survival under stress conditions and/or pathogenicity of leptospires inside the host. Detailed study of these individual genes is thus clearly warranted. The gene encoding many the LigB lipoprotein was up-regulated in response to serum. LigB interacts with fibronectin and may
serve as an adhesin by binding to host extracellular matrix during the early stages of infection [56–58]. However, recent studies with site-directed mutagenesis of ligB did not show attenuation of a ligB mutant in the hamster model of leptospirosis [59]. This finding does not exclude the role of LigB as a virulence determinant, since previous studies have shown redundancy in extracellular matrix-binding function of leptospiral proteins including a 36-kDa fibronectin-binding protein [60], Lsa24 (also known as LfhA and LenA)[61, 62], LigA [16], Len proteins [62], LipL32 [63], and Lsa21 [17]. Our finding is therefore consistent with the hypothesis that LigB plays a role in virulence, but is not essential. The lpxD (LIC13469) gene encoding UDP-3-O-(3-hydroxymyristoyl) glucosamine N-acyltransferase, which catalyzes the third step of lipid A biosynthesis [64], was up-regulated in response to serum.