{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Proctor EJ"],"funding":["National Health and Medical Research Council"],"pagination":["105623"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10844976"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["300(2)"],"pubmed_abstract":["Group A Streptococcal M-related proteins (Mrps) are dimeric α-helical-coiled-coil cell membrane-bound surface proteins. During infection, Mrp recruit the fragment crystallizable region of human immunoglobulin G via their A-repeat regions to the bacterial surface, conferring upon the bacteria enhanced phagocytosis resistance and augmented growth in human blood. However, Mrps show a high degree of sequence diversity, and it is currently not known whether this diversity affects the Mrp-IgG interaction. Herein, we report that diverse Mrps all bind human IgG subclasses with nanomolar affinity, with differences in affinity which ranged from 3.7 to 11.1 nM for mixed IgG. Using surface plasmon resonance, we confirmed Mrps display preferential IgG-subclass binding. All Mrps were found to have a sig"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Molecular characterization of the interaction between human IgG and the M-related proteins from Streptococcus pyogenes."],"pmcid":["PMC10844976"],"funding_grant_id":["APP1143266"],"pubmed_authors":["Botteaux A","McArthur J","De Oliveira DMP","Gorman J","Sanderson-Smith M","Botquin G","Urbaniec J","Davies MR","Frost HR","Satapathy S","Proctor EJ","Smeesters P"],"additional_accession":[]},"is_claimable":false,"name":"Molecular characterization of the interaction between human IgG and the M-related proteins from Streptococcus pyogenes.","description":"Group A Streptococcal M-related proteins (Mrps) are dimeric α-helical-coiled-coil cell membrane-bound surface proteins. During infection, Mrp recruit the fragment crystallizable region of human immunoglobulin G via their A-repeat regions to the bacterial surface, conferring upon the bacteria enhanced phagocytosis resistance and augmented growth in human blood. However, Mrps show a high degree of sequence diversity, and it is currently not known whether this diversity affects the Mrp-IgG interaction. Herein, we report that diverse Mrps all bind human IgG subclasses with nanomolar affinity, with differences in affinity which ranged from 3.7 to 11.1 nM for mixed IgG. Using surface plasmon resonance, we confirmed Mrps display preferential IgG-subclass binding. All Mrps were found to have a sig","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jan","modification":"2025-04-22T03:22:32.861Z","creation":"2025-04-05T20:40:55.398Z"},"accession":"S-EPMC10844976","cross_references":{"pubmed":["38176650"],"doi":["10.1016/j.jbc.2023.105623"]}}