TY - JOUR
T1 - Biological properties of a Streptococcus pyogenes mutant generated by Tn916 insertion in mga
AU - Kihlberg, Britt Marie
AU - Cooney, Jakki
AU - Caparon, Michael G.
AU - Olsén, Arne
AU - Björck, Lars
N1 - Funding Information:
We are indebted to Drs Gunnar Lindahl and Ulf SjObring for stimulating discussions and to Ingbritt Gustafsson for expert technical assistance. The assistance of Dr Erik Carlemalm at the Electron microscopy unit, Medical Faculty, Lund University, is gratefully acknowledged. This work was supported by grants from the Swedish Medical Researcl~ Council (project 7480), King Gustaf V's 80-Years Foundation, the Medical Faculty, Lund University, the Foundations of Kock, Schyberg, and (Dsterlund, High Tech Receptor AB, and the Swedish Research Council for Engineering Sciences (project 123).
PY - 1995
Y1 - 1995
N2 - 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 wild-type 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 O, 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.
AB - 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 wild-type 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 O, 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.
KW - gene
KW - hemolysin
KW - mutant
KW - protein
KW - streptococcus
KW - virulence
UR - http://www.scopus.com/inward/record.url?scp=0029572448&partnerID=8YFLogxK
U2 - 10.1016/S0882-4010(96)80003-9
DO - 10.1016/S0882-4010(96)80003-9
M3 - Article
C2 - 8778565
AN - SCOPUS:0029572448
SN - 0882-4010
VL - 19
SP - 299
EP - 315
JO - Microbial Pathogenesis
JF - Microbial Pathogenesis
IS - 5
ER -