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Infection and Immunity, June 2000, p. 3226-3232, Vol. 68, No. 6
Laboratory of Human Bacterial Pathogenesis,
Rocky Mountain Laboratories, National Institute of Allergy and
Infectious Diseases, National Institutes of Health, Hamilton, Montana
59840,1 and Institute of Infectious
Diseases and Immunology, University of Utrecht, NL-3584 CL Utrecht, The
Netherlands2
Received 18 January 2000/Returned for modification 23 February
2000/Accepted 20 March 2000
Streptococcus pyogenes secretes several proteins that
influence host-pathogen interactions. A tissue-culture model was used to study the influence of the secreted cysteine protease streptococcal erythrogenic toxin B (SPE B) on the interaction between S. pyogenes strain NZ131 (serotype M49) and mammalian cells.
Inactivation of the speB gene enhanced
fibronectin-dependent uptake of the pathogen by Chinese hamster ovary
(CHO-K1) cells compared to that in the isogenic wild-type strain.
Preincubation of the NZ131 speB mutant with purified SPE B
protease significantly inhibited fibronectin-dependent uptake by both
CHO-K1 and CHO-pgs745 cells. The effect was attributed to
an abrogation of fibronectin binding to the surface of the bacteria
that did not involve either the M49 protein or the streptococcal fibronectin-binding protein SfbI. In contrast, pretreatment of the
NZ131 speB mutant with SPE B did not influence sulfated
polysaccharide-mediated uptake by CHO-pgs745 cells. The
results indicate that the SPE B protease specifically alters bacterial
cell surface proteins and thereby influences pathogen uptake.
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Streptococcal Erythrogenic Toxin B Abrogates
Fibronectin-Dependent Internalization of Streptococcus
pyogenes by Cultured Mammalian Cells
*
Corresponding author. Mailing address: Rocky Mountain
Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 903 South Fourth St., Hamilton, MT
59840. Phone: (406) 363-9306. Fax: (406) 363-9204. E-mail: mchaussee{at}nih.gov.
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