Biological properties of a Streptococcus pyogenes mutant generated by Tn916 insertion in mga

被引:88
作者
Kihlberg, BM
Cooney, J
Caparon, MG
Olsen, A
Bjorck, L
机构
[1] LUND UNIV, DEPT MOLEC & CELL BIOL, MOLEC PATHOGENESIS SECT, S-22100 LUND, SWEDEN
[2] WASHINGTON UNIV, SCH MED, DEPT MOLEC MICROBIOL, ST LOUIS, MO 63110 USA
基金
瑞典研究理事会;
关键词
streptococcus; mutant; gene; protein; hemolysin; virulence;
D O I
10.1016/S0882-4010(96)80003-9
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
The mga regulon of Streptococcus pyogenes contains genes which contribute to the pathogenicity and virulence of this significant human pathogen. Transposon insertional inactivation of the regulatory mga gene in a S. pyogenes strain of the clinically important M1 serotype, blocked the expression of four genes located downstream of mga. These genes encode the M1 protein, the IgG-binding protein H, protein SIC which is an extracellular inhibitor of complement, and the C5a peptidase which interferes with granulocyte migration. The wildtype strain is resistant to phagocytosis and adheres to human skin tissue sections; properties that were lost in the transposon mutant. Moreover, the mutant was less virulent to mice but more cytolytic to human lymphocytes, the latter due to an increased activity of streptolysin S, whereas the production of streptolysin 0, another toxin of S. pyogenes, was not affected. The mga mutation was complemented in trans with an intact mga gene which restored the phenotype of the wild-type strain. (C) 1995 Academic Press Limited
引用
收藏
页码:299 / 315
页数:17
相关论文
共 63 条
[1]   PROTEIN-H - A NOVEL IGG BINDING BACTERIAL PROTEIN [J].
AKESSON, P ;
COONEY, J ;
KISHIMOTO, F ;
BJORCK, L .
MOLECULAR IMMUNOLOGY, 1990, 27 (06) :523-531
[2]   M1-PROTEIN AND PROTEIN-H - IGGFC-BINDING AND ALBUMIN-BINDING STREPTOCOCCAL SURFACE-PROTEINS ENCODED BY ADJACENT GENES [J].
AKESSON, P ;
SCHMIDT, KH ;
COONEY, J ;
BJORCK, L .
BIOCHEMICAL JOURNAL, 1994, 300 :877-886
[3]  
AKESSON P, 1995, IN PRESS J BIOL CHEM
[4]   STREPTOCOCCAL TOXINS (STREPTOLYSIN-O, STREPTOLYSIN-S, ERYTHROGENIC TOXIN) [J].
ALOUF, JE .
PHARMACOLOGY & THERAPEUTICS, 1980, 11 (03) :661-717
[5]  
ALOUF JE, 1991, SOURCEBOOK BACTERIAL, P367
[6]  
ALOUF JE, 1991, PHARMACOL THERAPEUT, P367
[7]   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
[8]   STREPTOCOCCAL PROTEIN-G, EXPRESSED BY STREPTOCOCCI OR BY ESCHERICHIA-COLI, HAS SEPARATE BINDING-SITES FOR HUMAN-ALBUMIN AND IGG [J].
BJORCK, L ;
KASTERN, W ;
LINDAHL, G ;
WIDEBACK, K .
MOLECULAR IMMUNOLOGY, 1987, 24 (10) :1113-1122
[9]   BACTERIAL-GROWTH BLOCKED BY A SYNTHETIC PEPTIDE BASED ON THE STRUCTURE OF A HUMAN PROTEINASE-INHIBITOR [J].
BJORCK, L ;
AKESSON, P ;
BOHUS, M ;
TROJNAR, J ;
ABRAHAMSON, M ;
OLAFSSON, I ;
GRUBB, A .
NATURE, 1989, 337 (6205) :385-386
[10]  
CAPARON MG, 1991, METHOD ENZYMOL, V204, P556