IdeS Products

Description

IdeS from Streptococcus pyogenes, originally known as Mac-1, is a unique cysteine protease secreted in mature active form with a high degree of specificity for IgG. The structure of IdeS resembles features of the papain cysteine protease family with two distinct domains that interact through a polar interface containing an active site catalytic triad (1). However, IdeS is unique in that it does not contain disulfide bonds or a propeptide and has a RGD motif, known to be important for recognition by integrins (1). Studies have also found IdeS can inhibit neutrophil effector production of reactive oxygen species to repress immune responses in addition to performing IgG hydrolysis (2). IdeS digests all subclasses of human, and some classes of monkey, rabbit and sheep IgG with limited activity on mouse IgG2a and IgG3. IdeS digests IgG at a specific defined site between two glycines in the lower hinger region of the IgG heavy chain generating a homogenous pool of F(ab‘)2 and Fc/2 fragments. The lower hinge region is implicated as being important for Fc receptor recognition and complement binding (2-4). The high specificity and generation of homogeneous products has led to development of analytical strategies utilizing IdeS to characterize monoclonal therapeutic antibodies and related products such as antibody-drug conjugates, Fc-fusion proteins and bispecific antibodies (5). Additionally, animal models have provided significant proof of concept for use of IdeS as a therapeutic in treatment of IgG-mediated autoimmune diseases leading to some success using IdeS in clinical trials (2, 6). 

Bioinformatics

Uniprot	YP_006932748.1
Alternate Names	IdeS