PLoS Med 2006,3(9):e353.PubMedCrossRef 20. Lindberg AA (Ed): Bacterial surface polysaccharides and phage adsorption New York: Academic Press; 1977. 21.

Xia S, Xu B, Huang L, Zhao JY, Ran L, Zhang J, Chen H, Pulsrikarn C, Pornruangwong S, Aarestrup FM, et al.: Prevalence and characterization of human Selleck VX-689 Shigella infections in Henan Province, China, in 2006. J Clin Microbiol 2011,49(1):232–242.PubMedCrossRef 22. Sambrook J, Fritsch EF, Maniatis T: Molecular Cloning: a Laboratory Manual. 2nd edition. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory; 1989. 23. Hitchcock PJ, Brown TM: Morphological heterogeneity among Salmonella lipopolysaccharide chemotypes in silver-stained polyacrylamide gels. J Bacteriol 1983,154(1):269–277.PubMed Authors’ contributions JX and QS designed the study, and co-drafted the manuscript. RL participated Stem Cells inhibitor in the design of the study and preparation of the manuscript. YW participated in the BIBF 1120 ic50 construction of the new serotype. JW carried out the PCR amplification and DNA sequencing. XL performed the LPS Western-blot assay. SZ carried out the serological identification. PL participated in the phage induction and infection. CY and HJ participated in the isolation of clinical

strains. YW participated in the sequence alignment. All authors read and approved the final manuscript.”
“Background Cells possess several mechanisms to control the quality of their components, such as proteins [1]. One of these mechanisms ensures proper folding and function of proteins, sending misfolded proteins to be degraded by the ubiquitin-proteasome system and represents the best characterized protein quality control process [2–4]. In the lumen of endoplasmic reticulum (ER), one relevant protein quality control mechanism

operates, where misfolded proteins are recognized by ER chaperones and some of them are eventually translocated to the cytosol, in the interface with the ER membrane. Finally, the degradation of non-functional proteins can take place by the ubiquitin-proteasome system in a process known as ER-associated degradation (ERAD) [2–4]. The importance of protein quality control acetylcholine mechanisms is evident if it is taken into account that as much as 30% of all nascent polypeptides are misfolded [5, 6]. E3 ubiquitin ligases are associated with ribosomes to degrade proteins with aberrant folds, which mean that several proteins can be degraded during translation [7]. Therefore, it is not surprising that several mutants of genes encoding critical proteasome subunits are lethal. Remarkably, accumulation of misfolded proteins is implicated with several human diseases, especially neurodegenerative illnesses that are associated with protein aggregates [8–10]. Proteins that enter the secretory pathway are directed to the ER, where their folding and post-translational modifications occur.