Rueda, Cristian Ruiz - California State University, Northridge

个人简介

Adjunct Assistant Professor (2015–). Dept. Microbiol. & Immunol., Weill Cornell Medical College, New York, NY. Research Associate (2013–2015) with Dr. Francis Barany, Dept. Microbiol. & Immunol., Weill Cornell Medical College, New York, NY. Research Associate (2009–2012) / Postdoctoral fellow (2006–2012) with Dr. Stuart Levy, Dept. Molecular Biol. & Microbiology, Tufts University School of Medicine, Boston, MA. Ph.D. cum laude (highest mark) in Microbiology (2005) with Dr. Pilar Diaz, Dept. Microbiol., University of Barcelona, Barcelona, Spain. Ph.D. European mention award (2005) by the consortium of European universities. Extraordinary Ph.D. thesis award (2005) by the University of Barcelona. M.Phil. Microbiology (2001). Dept. Microbiol., University of Barcelona, Barcelona, Spain. B.S. Biology (1999). University of Barcelona, Barcelona, Spain.

研究领域

The ultimate goal of my research is to develop novel ways of preventing and treating infectious diseases caused by bacteria resistant to multiple antibiotics. These bacteria have become a major problem in the U.S. and abroad, from failed treatment of previously curable diseases to increased hospital costs. There are about 2 million hospital-acquired infections in the U.S. each year, with more than 99,000 deaths occurring mostly due to antibiotic resistant pathogens. World health leaders have described antibiotic resistant pathogens as “nightmare bacteria that pose a catastrophic threat to people in every country in the world”. My laboratory uses a multidisciplinary approach that includes bacterial genetics and biochemistry, molecular biology, gene expression experiments, and “omics” to study multidrug resistance in bacteria. Our current main projects are: 1) Studying the regulation and physiological role of the AcrAB-TolC multidrug efflux pump. This pump is the main multidrug efflux pump in Escherichia coli and many other pathogenic Enterobacteriaceae. The AcrAB-TolC pump effluxes multiple classes of antibiotics, bile salts and other exogenous toxic compounds. A better understanding of its regulation and physiological substrates is essential to develop novel efflux inhibitors capable of restoring antibiotic efficacy. 2) Identification of carbapenem-resistant bacteria and genes. Carbapenems are last resort antibiotics used in healthcare facilities to treat multidrug resistant bacteria. Carbapenem-resistant bacteria, especially Gram-negatives, are often untreatable and are associated with mortality. The CDC has designated them as an urgent threat. Our overall goal is to examine the distribution, frequency and type of carbapenem-resistant bacteria found in different locations to better predict and prevent potential outbreaks in the future. We are especially interested in identifying novel genes and genetic mobile elements conferring resistance to carbapenems.

近期论文

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Ruiz, C. and Levy, S.B. 2014. Regulation of acrAB expression by cellular metabolites in Escherichia coli. J. Antimicrob. Chemother. 69: 390-399. [Link] Harmon, D.E., Murphy J.L., Davis, A.J., and Mecsas, J. 2013. A mutant with aberrant extracellular LcrV-YscF interactions fails to form pores and translocate Yop effector proteins but retains the ability to trigger Yop secretion in response to host cell contact. J. Bacteriol. 195: 2244–54. [Link] Ruiz, C. and Levy, S.B. 2011. Use of Functional Interactions with MarA to Discover Chromosomal Genes Affecting Antibiotic Susceptibility in Escherichia coli. Int. J. Antimicrob. Agents 37: 177–178. [Link] Harmon, D.E., Davis, A.J., Castillo, C., and Mecsas, J. 2010. Identification and Characterization of Small-Molecule Inhibitors of Yop Translocation in Yersinia pseudotuberculosis. Antimicrob. Agents Chemother. 54: 3241–54. [Link] Ruiz, C. and Levy, S.B. 2010. Many Chromosomal Genes Modulate MarA-Mediated Multidrug Resistance in Escherichia coli. Antimicrob. Agents Chemother. 54: 2125–2134. [Link] Ruiz, C., McMurry, L.M. and Levy, S.B. 2008. Role of the multidrug resistance regulator MarA in global regulation of the hdeAB acid resistance operon in Escherichia coli. J. Bacteriol. 190: 1290–1297. [Link] Ruiz, C., Falcocchio, S., Pastor, F.I.J., Saso, L. and Díaz, P. 2007. EstV, a novel bacterial lipase belonging to family V, is the first lipase from the pathogen Helicobacter pylori, and also from an epsilon-proteobacterium, cloned and characterized. Appl. Environ. Microbiol. 73: 2423–2431. [Link] Ruiz, C., Falcocchio, S., Xoxi, E., Villo, L., Nicolosi, G., Pastor, F.I.J., Díaz, P. and Saso, L. 2006. Inhibition of Candida rugosa lipase by saponins, flavonoids and alkaloids. J. Mol. Catal. B Enzym. 40: 138-143. [Link] Falcocchio, S., Ruiz, C., Pastor, F.I.J., Saso, L. and Díaz, P. 2006. Propionibacterium acnes GehA lipase, involved in acne development, can be successfully inhibited by selected natural substances. J. Mol. Catal. B Enzym. 40: 132–137. [Link] Ruiz, C., Pastor, F.I.J. and Díaz, P. 2005. Isolation of lipid- and polysaccharide-degrading microorganisms from subtropical forest soil, and analysis of lipolytic strain Bacillus sp. CR-179. Lett. Appl. Microbiol. 40: 218–222. [Link] Falcocchio, S., Ruiz, C., Pastor, F.I.J., Saso, L., and Díaz, P. 2005. Identification of a carboxylesterase-producing Rhodococcus soil isolate. Can. J. Microbiol. 51: 753–758. [Link] Ruiz, C., Falcocchio, S., Xoxi, E., Pastor, F.I.J., Díaz, P. and Saso, L. 2004. Activation and inhibition of Candida rugosa and Bacillus-related lipases by saturated fatty acids, evaluated by a new colorimetric microassay. Biochim. Biophys. Acta 1672: 184–191. [Link] Ruiz, C., Pastor, F.I.J. and Díaz, P. 2003. Isolation and characterization of Bacillus sp. BP-6 LipA, a ubiquitous lipase among mesophilic Bacillus species. Lett. Appl. Microbiol. 37: 354–359. [Link] Prim, N., Sánchez M., Ruiz, C., Pastor, F.I.J. and Díaz, P. 2003. Use of methylumbeliferyl-derivative substrates for lipase activity characterization. J. Mol. Catal. B Enzym. 22: 339–346. [Link] Ruiz, C., Blanco, A., Pastor, F.I.J. and Díaz, P. 2002. Analysis of Bacillus megaterium lipolytic system and cloning of LipA, a novel subfamily I.4 bacterial lipase. FEMS Microbiol. Lett. 217: 263–267. [Link]