SLE: Unusual Recombinant Monoclonal Light Chain NGTA3-Pro-DNase Possessing Three Different Activities Trypsin-like, Metalloprotease and DNase
Received Date: Apr 17, 2017 / Accepted Date: May 20, 2017 / Published Date: May 29, 2017
Objective: DNA- and myelin basic protein (MBP)-hydrolyzing antibodies can play an important role in the pathogenesis of systemic lupus erythematosus (SLE), therefore their analysis seems to be important.
Results: In mammalians there are serine proteases, metalloproteases, and DNases. Each of these and many other enzymes catalyze only one chemical reaction. Very unusual and unpredictable situation was revealed by us in the case of monoclonal abzymes corresponding to the sera of patients with SLE. The small pools of phage particles displaying light chains with different affinity for myelin basic protein (MBP) were isolated by affinity chromatography on MBP-Sepharose. In contrast to canonical enzymes, one of twenty five MLChs demonstrated three different enzymatic activities; it efficiently hydrolyzed MBP (but not other proteins) and DNA. Other twenty four MLChs hydrolyzed only MBP. The proteolytic activity of NGTA3-pro-DNase was efficiently inhibited by specific inhibitors of serine-like (PMSF) and metalloproteases (EDTA). Protease and DNase properties of NGTA3-pro-DNase differ significantly from those for the corresponding canonical enzymes.
Conclusion: This is the first example of monoclonal antibodies with three different catalytic activities. The principal possibility of the existence of monoclonal antibodies with several different enzymatic activities is unexpected but very important for the further understanding of unknown biological functions of human immunoglobulins.
Keywords: Systemic lupus erythematosus; Recombinant monoclonal light chain; Hydrolysis of myelin basic protein and DNA
Citation: Timofeeva AM, Buneva VN, Nevinsky GA (2017) SLE: Unusual Recombinant Monoclonal Light Chain NGTA3-Pro-DNase Possessing Three Different Activities Trypsin-like, Metalloprotease and DNase. Lupus Open Access 2:127.
Copyright: © 2017 Timofeeva AM, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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