José M. Argüello
Professor
Chemistry & Biochemistry
Worcester Polytechnic Institute
United States of America
Biography
Education: Biological Chemist Universidad Nacional de Córdoba, Argentina 1979 PhD (Biological Sciences) Universidad Nacional de Río Cuarto, Argentina 1985 Micronutrient transition metals (copper, zinc, cobalt, nickel, iron, and manganese) play a central role in the interaction of pathogenic (and beneficial) bacteria with higher eukaryote hosts. Our research is directed to understand the bacterial mechanisms of metal homeostasis required for these interactions. In particular, we focus on the functions of transmembrane transporters and chaperone molecules that tightly control metal uptake and distribution. These molecules appear to be key determinants of virulence in pathological bacteria like Mycobacterium tuberculosis and Pseudomonas aeruginosa, or symbionts such as Rhizobium meliloti. In addition, we study the molecular structure and biochemical mechanisms of metal selectivity in transmembrane transport ATPases. Our multidisciplinary approaches include structural and molecular biology, enzymology, biophysics, protein chemistry, fluorescence microscopy, and microbiology. Through a number of ongoing collaborations, we also employ crystallography, X-ray fluorescence and spectroscopy, and bioinformatics to gain insights into the role of metals in bacterial virulence. Collaboration and camaraderie among postdoctoral fellows, graduate students, and undergraduate students are hallmarks of our work. I enjoy mentoring these young colleagues and guiding their progress into a scientific career.
Research Interest
Homeostasis of micronutrient metals; Ion transport across membranes; Bacterial virulence; Host-bacterial interactions.
Publications
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Characterization of a thermophilic P-type Ag+/Cu+-ATPase from the extremophile Archaeoglobus fulgidus - 2002
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Reactivity of cysteines in the transmembrane region of the Na, K-ATPase alpha subunit probed with Hg(2+) - 2000
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The role of Na,K-ATPase alpha subunit serine 775 and glutamate 779 in determining the extracellular K+ and membrane potential-dependent properties of the Na,K-pump - 2000
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Electrogenic sodium-sodium exchange carried out by Na,K-ATPase containing the amino acid substitution Glu779Ala - 2000
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Functional role of cysteine residues in the (Na,K)-ATPase alpha subunit - 2000