{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hayashida A"],"funding":["NEI NIH HHS"],"pagination":["e9"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11218895"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["1(3)"],"pubmed_abstract":["A large number of bacterial pathogens bind to host extracellular matrix (ECM) components. For example, many Gram-negative and Gram-positive pathogens express binding proteins for fibronectin (FN) on their cell surface. Mutagenesis studies of bacterial FN-binding proteins have demonstrated their importance in pathogenesis in preclinical animal models. However, means to draw on these findings to design therapeutic approaches that specifically target FN-bacteria interactions have not been successful because bacterial pathogens can elaborate several FN-binding proteins and also because FN is an essential protein and likely a nondruggable target. Here we report that select heparan compounds potently inhibit <i>Streptococcus pneumoniae</i> infection of injured corneas in mice. Using intact hepar"],"journal":["Proteoglycan research"],"pubmed_title":["Sulfated motifs in heparan sulfate inhibit <i>Streptococcus pneumoniae</i> adhesion onto fibronectin and attenuate corneal infection."],"pmcid":["PMC11218895"],"funding_grant_id":["R01 EY021765","R01 EY033025"],"pubmed_authors":["Zhang F","Liu J","Saeed HN","Parks WC","Bispo PJM","Hayashida A","Park PW","Song Y"],"additional_accession":[]},"is_claimable":false,"name":"Sulfated motifs in heparan sulfate inhibit <i>Streptococcus pneumoniae</i> adhesion onto fibronectin and attenuate corneal infection.","description":"A large number of bacterial pathogens bind to host extracellular matrix (ECM) components. For example, many Gram-negative and Gram-positive pathogens express binding proteins for fibronectin (FN) on their cell surface. Mutagenesis studies of bacterial FN-binding proteins have demonstrated their importance in pathogenesis in preclinical animal models. However, means to draw on these findings to design therapeutic approaches that specifically target FN-bacteria interactions have not been successful because bacterial pathogens can elaborate several FN-binding proteins and also because FN is an essential protein and likely a nondruggable target. Here we report that select heparan compounds potently inhibit <i>Streptococcus pneumoniae</i> infection of injured corneas in mice. Using intact hepar","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jul","modification":"2025-04-04T23:54:14.714Z","creation":"2025-04-04T23:54:14.714Z"},"accession":"S-EPMC11218895","cross_references":{"pubmed":["38957622"],"doi":["10.1002/pgr2.9"]}}