Adherence molecules of pathogenic pneumococci

被引:110
作者
Hammerschmidt, S [1 ]
机构
[1] Univ Wurzburg, Res Ctr Infect Dis, D-97070 Wurzburg, Germany
关键词
D O I
10.1016/j.mib.2005.11.001
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Adherence molecules are key players in pathogen-host interactions. These are usually surface-exposed structures that facilitate adherence to host cells, or target host serum proteins of the extracellular matrix. Our knowledge of the function of pneumococcal cell-surface structures, and the basic mechanisms underlying their interaction with host receptor molecules has dramatically increased, through molecular and structural analysis of adherence molecules. In particular, choline-binding proteins have received considerable attention because of their versatility, and their sophisticated role in the interaction with host proteins. Interestingly, subversion of host-protein functions to facilitate host invasion and immune evasion has also been attributed to intracellular or surface-exposed proteins of the pathogen. Many of these molecules do not possess the classic features of bacterial surface proteins.
引用
收藏
页码:12 / 20
页数:9
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共 60 条
[1]   The nine residue plasminogen-binding motif of the pneumococcal enolase is the major cofactor of plasmin-mediated degradation of extracellular matrix, dissolution of fibrin and transmigration [J].
Bergmann, S ;
Rohde, M ;
Preissner, KT ;
Hammerschmidt, S .
THROMBOSIS AND HAEMOSTASIS, 2005, 94 (02) :304-311
[2]   Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein [J].
Bergmann, S ;
Rohde, M ;
Hammerschmidt, S .
INFECTION AND IMMUNITY, 2004, 72 (04) :2416-2419
[3]   Identification of a novel plasmin(ogen)-binding motif in surface displayed α-enolase of Streptococcus pneumoniae [J].
Bergmann, S ;
Wild, D ;
Diekmann, O ;
Frank, R ;
Bracht, D ;
Chhatwal, GS ;
Hammerschmidt, S .
MOLECULAR MICROBIOLOGY, 2003, 49 (02) :411-423
[4]   α-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface [J].
Bergmann, S ;
Rohde, M ;
Chhatwal, GS ;
Hammerschmidt, S .
MOLECULAR MICROBIOLOGY, 2001, 40 (06) :1273-1287
[5]   Sequence heterogeneity of PsaA, a 37-kilodalton putative adhesin essential for virulence of Streptococcus pneumoniae [J].
Berry, AM ;
Paton, JC .
INFECTION AND IMMUNITY, 1996, 64 (12) :5255-5262
[6]   The human polymeric immunoglobulin receptor facilitates invasion of epithelial cells by Streptococcus pneumoniae in a strain-specific and cell type-specific manner [J].
Brock, SC ;
McGraw, PA ;
Wright, PF ;
Crowe, JE .
INFECTION AND IMMUNITY, 2002, 70 (09) :5091-5095
[7]   Pneumococcal disease in western Europe: burden of disease, antibiotic resistance and management [J].
Cartwright, K .
EUROPEAN JOURNAL OF PEDIATRICS, 2002, 161 (04) :188-195
[8]   STREPTOCOCCUS-PNEUMONIAE ANCHOR TO ACTIVATED HUMAN-CELLS BY THE RECEPTOR FOR PLATELET-ACTIVATING-FACTOR [J].
CUNDELL, DR ;
GERARD, NP ;
GERARD, C ;
IDANPAANHEIKKILA, I ;
TUOMANEN, EI .
NATURE, 1995, 377 (6548) :435-438
[9]   Dual roles of PspC, a surface protein of Streptococcus pneumoniae, in binding human secretory IgA and factor H [J].
Dave, S ;
Carmicle, S ;
Hammerschmidt, S ;
Pangburn, MK ;
McDaniel, LS .
JOURNAL OF IMMUNOLOGY, 2004, 173 (01) :471-477
[10]   PspC, a pneumococcal surface protein, binds human factor H [J].
Dave, S ;
Brooks-Walter, A ;
Pangburn, MK ;
McDaniel, LS .
INFECTION AND IMMUNITY, 2001, 69 (05) :3435-3437