المؤلفون: Kang, Eugene, Crouse, Alanna, Chevallier, Lucie, Pontier, Stéphanie M., Alzahrani, Ashwag, Silué, Navoun, Campbell-Valois, François-Xavier, Montagutelli, Xavier, Gruenheid, Samantha, Malo, Danielle

المصدر: Mammalian Genome; Aug2018, Vol. 29 Issue 7/8, p558-576, 19p

مصطلحات موضوعية: ENTEROBACTERIACEAE, DISEASE susceptibility, NATURAL immunity, INTESTINAL diseases, MENDEL'S law

مستخلص: Enterobacteriaceae are a large family of Gram-negative, non-spore-forming bacteria. Although many species exist as part of the natural flora of animals including humans, some members are associated with both intestinal and extraintestinal diseases. In this review, we focus on members of this family that have important roles in human disease: Salmonella, Escherichia, Shigella, and Yersinia, providing a brief overview of the disease caused by these bacteria, highlighting the contribution of animal models to our understanding of their pathogenesis and of host genetic determinants involved in susceptibility or resistance to infection. [ABSTRACT FROM AUTHOR]

: Copyright of Mammalian Genome is the property of Springer Nature and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

المؤلفون: Walker, John M., Arndt, Katja M., Müller, Kristian M., Campbell-Valois, François-Xavier, Michnick, Stephen W.

المصدر: Protein Engineering Protocols; 2007, p249-274, 26p

مستخلص: The protein-engineering field is mainly concerned with the design of novel enzyme activities or folds and with understanding the fundamental sequence determinants of protein folding and stability. Much effort has been put into the design of methods to generate and screen libraries of polypeptides. Screening for the ability of proteins to bind with high affinity and/or specificity is most often approached with phage display technologies. In this chapter, we present an alternative to phage display, performed totally in vivo, based on the dihydrofolate reductase (DHFR) protein-fragment complementation assay (PCA). We describe the application of the DHFR PCA to the selection of degenerated sequences of the ras-binding domain (RBD) of raf for correct folding and binding to ras. Our screening system allows for enrichment of the libraries for the best-behaving sequences through iterative competition experiments, without the discrete library screening and expansion steps that are necessary in in vitro approaches. Moreover, the selected clones can be processed rapidly to purification by Ni-nitrilotriacetic acid (NTA) affinity chromatography in 96-well plates. Our methods are particularly suitable for the designing and screening of libraries aimed at studying sequence folding and binding determinants. Finally, it can be adapted for library-against-library screening, thus, allowing for coevolution of interacting proteins simultaneously. [ABSTRACT FROM AUTHOR]

: Copyright of Protein Engineering Protocols is the property of Springer eBooks and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)