个人简介

B.Sc. (Bachelor of Science) M.D. (Doctor of Medicine) Ph.D. (Doctor of Philosophy)

研究领域

Genomics Proteomics and Bioinformatics

Our laboratory is interested in the pathogenesis of bacterial infections and the development of vaccines for their prevention. The primary focus is on a system we discovered that allows certain Gram-negative bacteria to obtain iron for growth in vivo by directly obtaining iron from the host's iron binding proteins, transferrin and lactoferrin. This system involves receptors at the bacterial surface that bind transferrin or lactoferrin as a first step in the iron acquisition process. The two main goals of our research are to determine the detailed mechanisms involved in the iron uptake pathway and to develop effective vaccines and therapeutic agents against pathway components. The surface receptors are essential for survival of the bacteria in vivo, indicating that they are ideal vaccine targets. Receptor proteins from different bacteria that cause meningitis, lung infections and ear infections in humans and pneumonia in cattle and pigs have been tested for efficacy and licensed to companies interested in developing human and veterinary vaccines. However, vaccine development is currently hampered by antigenic variation of the receptor proteins. Our goal is to develop effective, broad-spectrum, long-lasting vaccines based on the conserved regions of the receptor proteins that are required for function.

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Nemish, U., R.-H. Yu, L. W. Tari, K. Krewulak, and A. B. Schryvers. The bacterial receptor protein, transferrin-binding protein B, does not independently facilitate the release of metal ion from human transferrin. Biochemistry and Cell Biology 81:275-283. 2003. Shouldice, S. R., D. A. Dougan, P. W. Williams, R. J. Skene, G. Snell, D. Scheibe, S. M. Kirby, D. J. Hosfield, D. E. McRee, A. B. Schryvers, and L. W. Tari. Crystal structure of Pasteurella haemolytica ferric ion-binding protein A reveals a novel class of bacterial iron binding proteins. Journal of Biological Chemistry 278:41093-8. 2003 Shouldice, S. R., D. R. Dougan, R. J. Skene, L. W. Tari, D. E. McRee, R.-H. Yu, and A. B. Schryvers. High Resolution Structure of an Alternate Form of the Ferric-ion Binding Protein from Haemophilus influenzae. Journal of Biological Chemistry 278:11513 - 11519. 2003 Sims, K. L., and A. B. Schryvers. Peptide-peptide interactions between human transferrin and transferrin binding protein B from Moraxella catarrhalis. Journal of Bacteriology 185:2603-2610. 2003 Wong, H., and A. B. Schryvers. Bacterial Lactoferrin Binding Protein A Binds to Both Domains of the Human Lactoferrin C-Lobe. Microbiology 149:1729-1737. 2003 Shouldice SR, Dougan DR, Williams PA, Skene RJ, Snell G, Scheibe D, Kirby S, Hosfield DJ, McRee DE, Schryvers AB, Tari LW. Crystal structure of Pasteurella haemolytica ferric ion-binding protein A reveals a novel class of bacterial iron-binding proteins. J Biol Chem. 278:41093-8. 2003 Shouldice SR, Skene RJ, Dougan DR, McRee DE, Tari LW, Schryvers AB. Presence of ferric hydroxide clusters in mutants of Haemophilus influenzae ferric ion-binding protein A. Biochemistry. 42:11908-14. 2003 Nemish U, Yu RH, Tari LW, Krewulak K, Schryvers AB. The bacterial receptor protein, transferrin-binding protein B, does not independently facilitate the release of metal ion from human transferrin. Biochem Cell Biol. 81:275-83. 2003 Lam SL, Kirby S, Schryvers AB. Foreign signal peptides can constitute a barrier to functional expression of periplasmic proteins in Haemophilus influenzae. Microbiology. 149:3155-64. 2003 Shouldice SR, Skene RJ, Dougan DR, Snell G, McRee DE, Schryvers AB, Tari LW. Structural basis for ion binding and release by a novel class of periplasmic iron-binding proteins found in gram-negative pathogens. J Bacteriol. 186(12):3903-10, 2004 Ekins A, Khan AG, Shouldice SR, Schryvers AB. Lactoferrin receptors in gram-negative bacteria: insights into the iron acquisition process. Biometals. 17(3):235-43. 2004 Shouldice SR, McRee DE, Dougan DR, Tari LW, Schryvers AB. Novel, anion-independent iron coordination by members of a third class of bacterial periplasmic Ferric Ion-binding proteins. J Biol Chem. 280(7):5820-7, 2005 Ling JM, Schryvers AB. Perspectives on interactions between lactoferrin and bacteria. Biochem Cell Biol. 84(3):275-81. 2006 Khan AG, Shouldice SR, Tari LW, Schryvers AB. The role of the synergistic phosphate anion in iron transport by the periplasmic iron-binding protein from Haemophilus influenzae. Biochem J 403(1): 43-8. 2007. Khan AG, Shouldice SR, Kirby SK, Yu RH, Tari LW, Schryvers AB. High-affinity binding by the periplasmic iron-binding protein from Haemophilus influenzae is required for acquiring iron from trans