Iron acquisition systems in the pathogenic Neisseria.

作者: Anthony B. Schryvers , Igor Stojiljkovic

DOI: 10.1046/J.1365-2958.1999.01411.X

关键词:

摘要: Pathogenic neisseriae have a repertoire of high-affinity iron uptake systems to facilitate acquisition this essential element in the human host. They possess surface receptor proteins that directly bind extracellular host iron-binding transferrin and lactoferrin. Alternatively, they siderophore receptors capable scavenging when exogenous siderophores are present. Released intracellular haem present form haemoglobin, haemoglobin-haptoglobin or free can be used as source for growth through direct binding by specific receptors. Although these may vary complexity composition, key protein involved transport (as iron, iron-siderophore) across outer membrane is TonB-dependent with an overall structure presumably similar determined recently Escherichia coli FhuA FepA. The potentially ideal vaccine targets view their critical role survival Preliminary pilot studies indicate receptor-based vaccines protective humans.

参考文章(34)
Edward N. Baker, Bryan F. Anderson, Heather M. Baker, Ross T. A. MacGillivray, Stanley A. Moore, Neil A. Peterson, Steven C. Shewry, John W. Tweedie, Three-dimensional structure of lactoferrin. Implications for function, including comparisons with transferrin. Advances in Experimental Medicine and Biology. ,vol. 443, pp. 1- 14 ,(1998) , 10.1007/978-1-4757-9068-9_1
Kaspar P Locher, Bernard Rees, Ralf Koebnik, André Mitschler, Luc Moulinier, Jurg P Rosenbusch, Dino Moras, Transmembrane Signaling across the Ligand-Gated FhuA Receptor Cell. ,vol. 95, pp. 771- 778 ,(1998) , 10.1016/S0092-8674(00)81700-6
J E Anderson, P F Sparling, C N Cornelissen, Gonococcal transferrin-binding protein 2 facilitates but is not essential for transferrin utilization. Journal of Bacteriology. ,vol. 176, pp. 3162- 3170 ,(1994) , 10.1128/JB.176.11.3162-3170.1994
L Lissolo, G Maitre-Wilmotte, P Dumas, M Mignon, B Danve, M J Quentin-Millet, Evaluation of transferrin-binding protein 2 within the transferrin-binding protein complex as a potential antigen for future meningococcal vaccines. Infection and Immunity. ,vol. 63, pp. 884- 890 ,(1995) , 10.1128/IAI.63.3.884-890.1995
C J Chen, P F Sparling, L A Lewis, D W Dyer, C Elkins, Identification and purification of a hemoglobin-binding outer membrane protein from Neisseria gonorrhoeae. Infection and Immunity. ,vol. 64, pp. 5008- 5014 ,(1996) , 10.1128/IAI.64.12.5008-5014.1996
Christopher M. Bruns, Andrew J. Nowalk, Andrew S. Arvai, Michele A. McTigue, Kevin G. Vaughan, Timothy A. Mietzner, Duncan E. McRee, Structure of Haemophilus influenzae Fe(+3)-binding protein reveals convergent evolution within a superfamily. Nature Structural & Molecular Biology. ,vol. 4, pp. 919- 924 ,(1997) , 10.1038/NSB1197-919
Michèle Legrain, Véronique Mazarin, Scan W. Irwin, Bernadette Bouchon, Marie-José Quentin-Millet, Eric Jacobs, Anthony B. Schryvers, Cloning and characterization of Neisseria meningitidis genes encoding the transferrin-binding proteins Tbp1 and Tbp2 Gene. ,vol. 130, pp. 73- 80 ,(1993) , 10.1016/0378-1119(93)90348-7