{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["12(1)"],"submitter":["Tian K"],"pubmed_abstract":["A proline-rich region was found in Streptococcus mutans (S. mutans) surface antigen I/II (Ag I/II). The functions of this region were explored to determine its role in the cariogenic abilities of S. mutans; specifically, the proline-rich region was compared with human amelogenin. The full-length amelogenin genes were cloned from human (AmH) and surface antigen I/II genes from S. mutans. Then, the genes expressed and purified. We analyzed the structure and self-assembly ability of AmH and Ag I/II, compared their capacities to induce mineralization, and assessed the adhesion ability of S. mutans to AmH- and Ag I/II-coated tooth slices. AmH formed ordered chains and net frames in the early stage of protein self-assembly, while Ag I/II formed irregular and overlapping structures. AmH induced m"],"journal":["Scientific reports"],"pagination":["22250"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9789152"],"repository":["biostudies-literature"],"pubmed_title":["Proline-rich protein from S. mutans can perform a competitive mineralization function to enhance bacterial adhesion to teeth."],"pmcid":["PMC9789152"],"pubmed_authors":["Zhou M","Ren X","Tian K","Du Q","Guo J","Chen Y","Xiao C"],"additional_accession":[]},"is_claimable":false,"name":"Proline-rich protein from S. mutans can perform a competitive mineralization function to enhance bacterial adhesion to teeth.","description":"A proline-rich region was found in Streptococcus mutans (S. mutans) surface antigen I/II (Ag I/II). The functions of this region were explored to determine its role in the cariogenic abilities of S. mutans; specifically, the proline-rich region was compared with human amelogenin. The full-length amelogenin genes were cloned from human (AmH) and surface antigen I/II genes from S. mutans. Then, the genes expressed and purified. We analyzed the structure and self-assembly ability of AmH and Ag I/II, compared their capacities to induce mineralization, and assessed the adhesion ability of S. mutans to AmH- and Ag I/II-coated tooth slices. AmH formed ordered chains and net frames in the early stage of protein self-assembly, while Ag I/II formed irregular and overlapping structures. AmH induced m","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2026-07-14T17:37:18.079Z","creation":"2025-02-19T03:01:04.854Z"},"accession":"S-EPMC9789152","cross_references":{"pubmed":["36564474"],"doi":["10.1038/s41598-022-26303-x"]}}