IdeS and SpeB:: immunoglobulin-degrading cysteine proteinases of Streptococcus pyogenes

被引:69
作者
von Pawel-Rammingen, U [1 ]
Björck, L [1 ]
机构
[1] Lund Univ, Sect Mol Pathogenesis, Dept Cell & Mol Biol, Biomed Res Ctr, SE-22184 Lund, Sweden
关键词
D O I
10.1016/S1369-5274(03)00003-1
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The Gram-positive bacterium Streptococcus pyogenes is a major human pathogen causing substantial morbidity and mortality in society. S. pyogenes has evolved numerous molecular mechanisms to avoid the various actions of the human immune system and has established means to modulate both adaptive and innate immune responses. S. pyogenes produces and secretes proteolytic enzymes, which have an important impact on the ability of the bacteria to survive in the human host. Prominent among these are two immunoglobulin-degrading enzymes: the newly discovered streptococcal cysteine proteinase, IdeS, and the classical cysteine proteinase of S. pyogenes, SpeB.
引用
收藏
页码:50 / 55
页数:6
相关论文
共 45 条
[1]   Protein SIC, a novel extracellular protein of Streptococcus pyogenes interfering with complement function [J].
Akesson, P ;
Sjoholm, AG ;
Bjorck, L .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (02) :1081-1088
[2]   Streptococcal protein H forms soluble complement-activating complexes with IgG, but inhibits complement activation by IgG-coated targets [J].
Berge, A ;
Kihlberg, BM ;
Sjoholm, AG ;
Bjorck, L .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (33) :20774-20781
[3]   STREPTOCOCCAL CYSTEINE PROTEINASE RELEASES BIOLOGICALLY-ACTIVE FRAGMENTS OF STREPTOCOCCAL SURFACE-PROTEINS [J].
BERGE, A ;
BJORCK, L .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (17) :9862-9867
[4]   IMMUNOGLOBULIN-G - FUNCTIONAL SITES [J].
BURTON, DR .
MOLECULAR IMMUNOLOGY, 1985, 22 (03) :161-206
[5]   Temporal production of streptococcal erythrogenic toxin B (streptococcal cysteine proteinase) in response to nutrient depletion [J].
Chaussee, MS ;
Phillips, ER ;
Ferretti, JJ .
INFECTION AND IMMUNITY, 1997, 65 (05) :1956-1959
[6]   EndoS and SpeB from Streptococcus pyogenes inhibit immunoglobulin-mediated opsonophagocytosis [J].
Collin, M ;
Svensson, MD ;
Sjöholm, AG ;
Jensenius, JC ;
Sjöbring, U ;
Olsén, A .
INFECTION AND IMMUNITY, 2002, 70 (12) :6646-6651
[7]   EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG [J].
Collin, M ;
Olsén, A .
EMBO JOURNAL, 2001, 20 (12) :3046-3055
[8]   Effect of SpeB and EndoS from Streptococcus pyogenes on human immunoglobulins [J].
Collin, M ;
Olsén, A .
INFECTION AND IMMUNITY, 2001, 69 (11) :7187-7189
[9]   Pathogenesis of group A streptococcal infections [J].
Cunningham, MW .
CLINICAL MICROBIOLOGY REVIEWS, 2000, 13 (03) :470-+
[10]   Molecular characterisation of group A streptococci from invasive and non-invasive disease episodes in Belgium during 1993-1994 [J].
Descheemaeker, P ;
Van Loock, F ;
Hauchecorne, M ;
Vandamme, P ;
Goossens, H .
JOURNAL OF MEDICAL MICROBIOLOGY, 2000, 49 (05) :467-471