J Microbiol Biotech Food Sci 2012,1(5):1250–1258 34 Alexander J

J Microbiol Biotech Food Sci 2012,1(5):1250–1258. 34. Alexander JW, Solomkin JS, Edwards MJ: Updated recommendations for control of surgical site infections. Ann Surg 2011,253(6):1082–1093. 10.1097/SLA.0b013e31821175f8PubMedCrossRef 35. Han S, Yang Y: Antimicrobial activity of wool fabric treated with curcumin. Dyes Pigm 2005, 64:157–161. 10.1016/j.dyepig.2004.05.008CrossRef 36. Safavy A, Raisch KP, Mantena S, Sanford LL, Sham SW, Krishna R, Bonner JA: Design and development of water-soluble

curcumin conjugates as potential anticancer agents. J Med Chem 2009, 50:6284–6288.CrossRef Competing interests Both authors declare no conflict of interest in the design and execution of this study. No external funding was available to undertake this work. Authors’ contributions

JB carried Tipifarnib out the experimental procedures, JB and DW designed the study and contributed selleck products equally to the analysis and production of the final manuscript.”
“Background Bacterial genomes usually contain a significant portion of open reading frames (ORFs) that encode lipoproteins. For example, the genome of Neisseria meningitidis group B strain MC58 has 70 ORFs that encode surface-exposed or exported putative NF-��B inhibitor lipoproteins [1]. Approximately 8% of the ORFs of Borrelia burgdorferi encode putative lipoproteins [2]. The presence of numerous lipoproteins in bacterial genomes suggests their importance for bacterial survival and pathogenesis. Lipoproteins have been demonstrated to have roles in preserving membrane structure, functioning as enzymes, and serving as transporters or toxins. Lipoproteins also serve as Edoxaban immunogens; for example, the lipoprotein outer surface protein A (OspA), which plays important roles in B. burgdorferi’s biology, was used to develop an OspA-based vaccine

[3, 4]. Haemophilus ducreyi, the etiologic agent of the sexually transmitted genital ulcer disease chancroid, has the capacity to express 67 putative lipoproteins (GenBank accession number AE017143), only four of which have been well characterized: the peptidoglycan associated lipoprotein (PAL), the fibrinogen binding protein (FgbA), the ducreyi lectin A (DltA), and H. ducreyi lipoprotein (Hlp) [5–7]. PAL is conserved among H. ducreyi strains and contains a surface-exposed epitope defined by the monoclonal antibody 3B9 [8]. An isogenic PAL mutant is unable to cause pustules in the human infection model [9]. FgbA and DltA also contribute to H. ducreyi virulence in humans [5, 10]. The roles of other lipoproteins in H. ducreyi pathogenesis have not yet been delineated. In order to better understand the bacterial factors that contribute to the pathogenesis of H. ducreyi, an experimental human model of infection was developed [11, 12]. In this model, adult volunteers are inoculated with H. ducreyi strain 35000HP, or its isogenic derivatives, on the skin overlying the upper deltoid.

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