Combining sites of bacterial fimbriae

被引:37
作者
De Greve, Henri [1 ]
Wyns, Lode [1 ]
Bouckaert, Julie [1 ]
机构
[1] Vrije Univ Brussels, Dept Mol & Cell Interact, Ultrastrutture Lab, B-1050 Brussels, Belgium
关键词
D O I
10.1016/j.sbi.2007.06.011
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The few known crystal structures of receptor-binding domains of fimbrial tip adhesins, FimH, PapGII, and F17G, tell us that each of these structures is unique and surprising. Despite little to no sequence identity, common to them all is their variable immunoglobulin (Ig)-fold. Nevertheless, their glycan-bincling sites have evolved in different locations onto this similar scaffold, and with distinct, highly specific binding properties. Difficult to capture is the often dominant role played by the fimbrial shaft in host cell recognition and biofilm formation. The major pilin FaeG, building up the shaft of F4 fimbriae, also harbors the carbohydrate receptor-binding property and has thereto an enlarged Ig-domain, with the insertion of two P-strands and two alpha-helices. Bordetella and CFA/I fimbriae combine a tip adhesin with major subunit adhesins. Still other fimbriae incorporate a specialized invasin at the very tip of polyadhesive fibers for uptake of bacteria in cells of the immune system and host epithelia. Finally, glycan recognition by fimbrial adhesins has often been found to coincide with the binding of cell-surface integrins and components of the extracellular matrix, such as collagen IV and laminin.
引用
收藏
页码:506 / 512
页数:7
相关论文
共 39 条
[1]   An atomic resolution model for assembly, architecture, and function of the Dr adhesins [J].
Anderson, KL ;
Billington, J ;
Pettigrew, D ;
Cota, E ;
Simpson, P ;
Roversi, P ;
Chen, HA ;
Urvil, P ;
du Merle, L ;
Barlow, PN ;
Medof, ME ;
Smith, RAG ;
Nowicki, B ;
Le Bouguénec, C ;
Lea, SM ;
Matthews, S .
MOLECULAR CELL, 2004, 15 (04) :647-657
[2]   Nontypeable Haemophilus influenzae-binding gangliosides of human respiratory (HEp-2) cells have a requisite lacto/neolacto core structure [J].
Berenson, CS ;
Sayles, KB ;
Huang, J ;
Reinhold, VN ;
Garlipp, MA ;
Yohe, HC .
FEMS IMMUNOLOGY AND MEDICAL MICROBIOLOGY, 2005, 45 (02) :171-182
[3]   Receptor binding studies disclose a novel class of high-affinity inhibitors of the Escherichia coli FimH adhesin [J].
Bouckaert, J ;
Berglund, J ;
Schembri, M ;
De Genst, E ;
Cools, L ;
Wuhrer, M ;
Hung, CS ;
Pinkner, J ;
Slättegård, R ;
Zavialov, A ;
Choudhury, D ;
Langermann, S ;
Hultgren, SJ ;
Wyns, L ;
Klemm, P ;
Oscarson, S ;
Knight, SD ;
De Greve, H .
MOLECULAR MICROBIOLOGY, 2005, 55 (02) :441-455
[4]   The affinity of the FimH fimbrial adhesin is receptor-driven and quasi-independent of Escherichia coli pathotypes [J].
Bouckaert, Julie ;
Mackenzie, Jenny ;
de Paz, Jose L. ;
Chipwaza, Beatrice ;
Choudhury, Devapriya ;
Zavialov, Anton ;
Mannerstedt, Karin ;
Anderson, Jennifer ;
Pierard, Denis ;
Wyns, Lode ;
Seeberger, Peter H. ;
Oscarson, Stefan ;
De Greve, Henri ;
Knight, Stefan D. .
MOLECULAR MICROBIOLOGY, 2006, 61 (06) :1556-1568
[5]   The fimbrial adhesin F17-G of enterotoxigenic Escherichia coli has an immunoglobulin-like lectin domain that binds N-acetylglucosamine [J].
Buts, L ;
Bouckaert, J ;
De Genst, E ;
Loris, R ;
Oscarson, S ;
Lahmann, M ;
Messens, J ;
Brosens, E ;
Wyns, L ;
De Greve, H .
MOLECULAR MICROBIOLOGY, 2003, 49 (03) :705-715
[6]   The solution structure of the invasive tip complex from Afa/Dr fibrils [J].
Cota, Ernesto ;
Jones, Celine ;
Simpson, Peter ;
Altroff, Harri ;
Anderson, Kirstine L. ;
du Merle, Laurence ;
Guignot, Julie ;
Servin, Alain ;
Le Bouguenec, Chantal ;
Mardon, Helen ;
Matthews, Stephen .
MOLECULAR MICROBIOLOGY, 2006, 62 (02) :356-366
[7]   N-terminal truncation enables crystallization of the receptor-binding domain of the FedF bacterial adhesin [J].
De Kerpel, Maia ;
Van Molle, Inge ;
Brys, Lea ;
Wyns, Lode ;
De Greve, Henri ;
Bouckaert, Julie .
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2006, 62 :1278-1282
[8]   Structural basis of the interaction of the pyelonephritic E. coli adhesin to its human kidney receptor [J].
Dodson, KW ;
Pinkner, JS ;
Rose, T ;
Magnusson, G ;
Hultgren, SJ ;
Waksman, G .
CELL, 2001, 105 (06) :733-743
[9]   The distinct binding specificities exhibited by enterobacterial type 1 fimbriae are determined by their fimbrial shafts [J].
Duncan, MJ ;
Mann, EL ;
Cohen, MS ;
Ofek, I ;
Sharon, N ;
Abraham, SN .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (45) :37707-37716
[10]   CARBOHYDRATE-BINDING SITES OF THE MANNOSE-SPECIFIC FIMBRIAL LECTINS OF ENTEROBACTERIA [J].
FIRON, N ;
OFEK, I ;
SHARON, N .
INFECTION AND IMMUNITY, 1984, 43 (03) :1088-1090