EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG

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EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG. / Collin, Mattias; Olsén, Arne.

In: EMBO Journal, Vol. 20, No. 12, 2001, p. 3046-3055.

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TY - JOUR

T1 - EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG

AU - Collin, Mattias

AU - Olsén, Arne

PY - 2001

Y1 - 2001

N2 - Streptococcus pyogenes is an important human pathogen that selectively interacts with proteins involved in the humoral defense system, such as immunoglobulins and complement factors. In this report we show that S.pyogenes has the ability to hydrolyze the chitobiose core of the asparagine-linked glycan on immuno globulin G (IgG) when bacteria are grown in the presence of human plasma. This activity is associated with the secretion of a novel 108 kDa protein denoted EndoS. EndoS has endoglycosidase activity on purified soluble IgG as well as IgG bound to the bacterial surface. EndoS is required for the activity on IgG, as an isogenic EndoS mutant could not hydrolyze the glycan on IgG. In addition, we show that the secreted streptococcal cysteine proteinase SpeB cleaves IgG in the hinge region in a papain-like manner. This is the first example of an endoglycosidase produced by a bacterial pathogen that selectively hydrolyzes human IgG, and reveals a novel mechanism which may contribute to S.pyogenes pathogenesis.

AB - Streptococcus pyogenes is an important human pathogen that selectively interacts with proteins involved in the humoral defense system, such as immunoglobulins and complement factors. In this report we show that S.pyogenes has the ability to hydrolyze the chitobiose core of the asparagine-linked glycan on immuno globulin G (IgG) when bacteria are grown in the presence of human plasma. This activity is associated with the secretion of a novel 108 kDa protein denoted EndoS. EndoS has endoglycosidase activity on purified soluble IgG as well as IgG bound to the bacterial surface. EndoS is required for the activity on IgG, as an isogenic EndoS mutant could not hydrolyze the glycan on IgG. In addition, we show that the secreted streptococcal cysteine proteinase SpeB cleaves IgG in the hinge region in a papain-like manner. This is the first example of an endoglycosidase produced by a bacterial pathogen that selectively hydrolyzes human IgG, and reveals a novel mechanism which may contribute to S.pyogenes pathogenesis.

KW - cysteine proteinase

KW - endo-beta-N-acetylglucos aminidase

KW - endoglycosidase

KW - IgG

KW - Streptococcus pyogenes

U2 - 10.1093/emboj/20.12.3046

DO - 10.1093/emboj/20.12.3046

M3 - Article

VL - 20

SP - 3046

EP - 3055

JO - EMBO Journal

T2 - EMBO Journal

JF - EMBO Journal

SN - 1460-2075

IS - 12

ER -