Literature summary for 3.4.22.10 extracted from

Soederberg, J.J.; von Pawel-Rammingen, U.
The streptococcal protease IdeS modulates bacterial IgGFc binding and generates 1/2Fc fragments with the ability to prime polymorphonuclear leucocytes (2008), Mol. Immunol., 45, 3347-3353.

Search for more literature for 3.4.22.10

Cloned(Commentary)

Cloned (Comment)	Organism
IdeS GST-fusion protein is expressed in Escherichia coli BL21	Streptococcus pyogenes

Organism

Organism	UniProt	Comment	Textmining
Streptococcus pyogenes	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
immunoglobulin G + H2O	non-immune binding of IgG to the bacterial surface is followed by the proteolytic cleavage of the antibody by the IgG-endopeptidase IdeS. IdeS generated 1/2Fc fragments do not compete efficiently with intact IgG in binding to the bacterial surface and rapid dissociation of 1/2Fc allows binding of new IgG. A correlated binding and proteolytic cleavage of IgG increases the probability that the bacteria can resist specific IgG, despite the presence of a large excess of non-specific IgG in the circulation. As a consequence of IdeS activity, circulating 1/2Fc fragments are generated. These 1/2Fc fragments are shown to be biological active by acting as priming agents for polymorphonuclear leucocytes	Streptococcus pyogenes	F(ab')2 + 1/2Fc	-	?

Synonyms

Synonyms	Comment	Organism
IdeS	-	Streptococcus pyogenes

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Streptococcus pyogenes

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Release 2023.1 (January 2023)