University of Calgary

DR. ANTHONY B. SCHRYVERS

 

B.Sc. Honours, University of Saskatchewan, 1976 Ph.D., Biochemistry, University of Alberta, 1981 M.D., University of Calgary, 1984

Research Interests:

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.

 

Lab Web site

 

Personnel:

Amanda Beddeck  PDF
 Dave Curran  Graduate Student
 Rong-hu Yu  Technician
 Jinny Park  Technician

 

 

 

 

View Pub Med for Recent publications & abstracts

Recent Publications:

  • 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 transferrin. Biochem J 404(2): 217-225, 2007

 

Contact Information:

The University of Calgary
O"Brien Center-Room G503
3330 Hospital Drive NW
Calgary, Alberta  T2N 2V1
Phone: (403) 220-3703
Fax: (403) 270-2772
Email: schryver [at] ucalgary [dot] ca

 

Contact Info

Departmental Office
Health Research Innovation Centre,
Room GAC60
3280 Hospital Dr. NW, Calgary, Alberta, Canada
T2N 4Z6
Phone: (403) 220-4483
Fax: (403) 210-8105
Email: bmb [at] ucalgary [dot] ca