Expression of New Recombinant IgG-Binding Polypeptides and Analysis of Their Capacity to Bind Human IgG.

E A Bormotova, T V Gupalova

Journal: Bulletin of experimental biology and medicine 2019;165(3):373-377

PMID: 30003416

Abstract

Protein G is present in group G streptococcus strain (G4223); the IgG-binding part of this protein contains three IgG-binding domains and binds human IgG with very high activity. We obtained two recombinant polypeptides G4223 and G4223 with high IgG-binding activity. Polypeptide G4223 consisting of three IgG-binding domains and W region has higher molecular weight and is characterized by higher affinity for IgG than polypeptide G4223 consisting of only three IgG-binding domains. It was shown that polypeptide affinity depends on its structure and size.

Address: Department of Molecular Microbiology, Institute of Experimental Medicine, St. Petersburg, Russia.; Department of Molecular Microbiology, Institute of Experimental Medicine, St. Petersburg, Russia. [email protected].

DOI: 10.1007/s10517-018-4173-z

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MeSH Terms: Amino Acid Sequence, Bacterial Proteins, Base Sequence, Binding Sites, Cloning, Molecular, Escherichia coli, Gene Expression, Humans, Immunoglobulin G, Molecular Weight, Peptides, Plasmids, Protein Binding, Protein Interaction Domains and Motifs, Recombinant Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Streptococcus gordonii