{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["83(11)"],"submitter":["Lee JH"],"pubmed_abstract":["The cell envelopes of many Gram-positive bacteria contain wall teichoic acids (WTAs). Staphylococcus aureus WTAs are composed of ribitol phosphate (RboP) or glycerol phosphate (GroP) backbones substituted with D-alanine and N-acetyl-D-glucosamine (GlcNAc) or N-acetyl-D-galactosamine (GalNAc). Two WTA glycosyltransferases, TarM and TarS, are responsible for modifying the RboP WTA with α-GlcNAc and β-GlcNAc, respectively. We recently reported that purified human serum anti-WTA IgG specifically recognizes β-GlcNAc of the staphylococcal RboP WTA and then facilitates complement C3 deposition and opsonophagocytosis of S. aureus laboratory strains. This prompted us to examine whether anti-WTA IgG can induce C3 deposition on a diverse set of clinical S. aureus isolates. To this end, we compared an"],"journal":["Infection and immunity"],"pagination":["4247-55"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4598408"],"repository":["biostudies-literature"],"pubmed_title":["Surface Glycopolymers Are Crucial for In Vitro Anti-Wall Teichoic Acid IgG-Mediated Complement Activation and Opsonophagocytosis of Staphylococcus aureus."],"pmcid":["PMC4598408"],"pubmed_authors":["Winstel V","Lee BL","Peschel A","An JH","Seong MY","Khan A","Kurokawa K","Larsen J","Andersen PS","Kim NH","Lee JH","Lee MJ"],"additional_accession":[]},"is_claimable":false,"name":"Surface Glycopolymers Are Crucial for In Vitro Anti-Wall Teichoic Acid IgG-Mediated Complement Activation and Opsonophagocytosis of Staphylococcus aureus.","description":"The cell envelopes of many Gram-positive bacteria contain wall teichoic acids (WTAs). Staphylococcus aureus WTAs are composed of ribitol phosphate (RboP) or glycerol phosphate (GroP) backbones substituted with D-alanine and N-acetyl-D-glucosamine (GlcNAc) or N-acetyl-D-galactosamine (GalNAc). Two WTA glycosyltransferases, TarM and TarS, are responsible for modifying the RboP WTA with α-GlcNAc and β-GlcNAc, respectively. We recently reported that purified human serum anti-WTA IgG specifically recognizes β-GlcNAc of the staphylococcal RboP WTA and then facilitates complement C3 deposition and opsonophagocytosis of S. aureus laboratory strains. This prompted us to examine whether anti-WTA IgG can induce C3 deposition on a diverse set of clinical S. aureus isolates. To this end, we compared an","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Nov","modification":"2026-05-03T07:44:03.562Z","creation":"2019-03-27T01:59:44Z"},"accession":"S-EPMC4598408","cross_references":{"pubmed":["26283333"],"doi":["10.1128/IAI.00767-15","10.1128/iai.00767-15"]}}