No abstract

CitationA novel protein quality control mechanism contributes to heat shock resistance of worldwide-distributed Pseudomonas aeruginosa clone C strains. 2015, 17 Pseudomonas aeruginosa is a highly successful nosocomial pathogen capable to cause a wide 26 variety of infections with clone C strains most prevalent worldwide. In this study, we initially 27 characterize a molecular mechanism of survival unique to clone C strains. We identified a P.28 aeruginosa clone C-specific genomic island (PACGI-1) which contains the highly expressed aeruginosa clone C population is significantly more heat shock resistant than genetically 36 unrelated P. aeruginosa strains without sHsp20c, the horizontally acquired shsp20c operon 37 might contributes to survival of world-wide distributed clone C strains.

Background: LMAN1 is an important mammalian cargo receptor for endoplasmic reticulum (ER)-to-Golgi trafficking. Results: Crystal structures pinpoint critical residues on LMAN1 for mannose binding, which is sensitive to Ca

SummaryThe ubiquitous second messenger c-di-GMP regulates the switching of bacterial lifestyles from motility to sessility and acute to chronic virulence to adjust bacterial fitness to altered environmental conditions. Conventionally, EAL proteins being c-di-GMP phosphodiesterases promote motility and acute virulence phenotypes such as invasion into epithelial cells and inhibit biofilm formation. We report here that in contradiction, the EAL-like protein STM1697 of Salmonella typhimurium suppresses motility, invasion into HT-29 epithelial cell line and secretion of the type three secretion system 1 effector protein SipA, whereas it promotes rdar biofilm formation and CsgD expression. STM1697 can, however, functionally replace the EAL-like protein STM1344 and vice versa, whereby both proteins neither degrade nor bind c-di-GMP. Like STM1344, STM1697 suppresses the transcription of class 2 and class 3 flagella regulon genes by binding to FlhD, a component of the master regulator of the flagella regulon FlhD 4C2 and act additively under numerous conditions. Interestingly, the interaction interface of STM1697 with FlhD 2 is distinct from its paralogue STM1344. We predict that the stand alone EAL domain proteins STM1697 and STM1344 belong to a subclass of EAL domain proteins in S. typhimurium, which are all involved in motility, biofilm and virulence regulation through interaction with proteins that regulate flagella function.

a b s t r a c t LMAN1 is a glycoprotein receptor, mediating transfer from the ER to the ER-Golgi intermediate compartment. Together with the co-receptor MCFD2, it transports coagulation factors V and VIII. Mutations in LMAN1 and MCFD2 can cause combined deficiency of factors V and VIII (F5F8D). We present the crystal structure of the LMAN1/MCFD2 complex and relate it to patient mutations. Circular dichroism data show that the majority of the substitution mutations give rise to a disordered or severely destabilized MCFD2 protein. The few stable mutation variants are found in the binding surface of the complex leading to impaired LMAN1 binding and F5F8D. Structured summary:MINT-7557086: lman1 (uniprotkb:P49257) and mcfd2 (uniprotkb:Q8NI22) bind (MI:0407) by X-ray crystallography (MI:0114)