<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>12(1)</volume><submitter>Tian K</submitter><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</pubmed_abstract><journal>Scientific reports</journal><pagination>22250</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9789152</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Proline-rich protein from S. mutans can perform a competitive mineralization function to enhance bacterial adhesion to teeth.</pubmed_title><pmcid>PMC9789152</pmcid><pubmed_authors>Zhou M</pubmed_authors><pubmed_authors>Ren X</pubmed_authors><pubmed_authors>Tian K</pubmed_authors><pubmed_authors>Du Q</pubmed_authors><pubmed_authors>Guo J</pubmed_authors><pubmed_authors>Chen Y</pubmed_authors><pubmed_authors>Xiao C</pubmed_authors></additional><is_claimable>false</is_claimable><name>Proline-rich protein from S. mutans can perform a competitive mineralization function to enhance bacterial adhesion to teeth.</name><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</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Dec</publication><modification>2026-07-14T17:37:18.079Z</modification><creation>2025-02-19T03:01:04.854Z</creation></dates><accession>S-EPMC9789152</accession><cross_references><pubmed>36564474</pubmed><doi>10.1038/s41598-022-26303-x</doi></cross_references></HashMap>