Staphylococcus aureus is the most important Gram-positive colonizer of human skin and nasal passage,causing high morbidity and mortality.SD-repeat containing protein D(SdrD),an MSCRAMM(Microbial Surface Components Rec...Staphylococcus aureus is the most important Gram-positive colonizer of human skin and nasal passage,causing high morbidity and mortality.SD-repeat containing protein D(SdrD),an MSCRAMM(Microbial Surface Components Recognizing Adhesive Matrix Molecules)family surface protein,plays an important role in S.aureus adhesion and pathogenesis,while its binding target and molecular mechanism remain largely unknown.Here we solved the crystal structures of SdrD N2-N3 domain and N2-N3-B1 domain.Through structural analysis and comparisons,we characterized the ligand binding site of SdrD,and proposed a featured sequence motif of its potential ligands.In addition,the structures revealed for the first time the interactions between B1 domain and N2-N3 domain among B domain-containing MSCRAMMs.Our results may help in understanding the roles SdrD plays in S.aureus adhesion and shed light on the development of novel antibiotics.展开更多
基金supported by the National Basic Research Program(973 Program)(Nos.2011CB910502 and 2012CB911101)National Natural Science Foundation of China(Grant Nos.31030020 and 31170679).
文摘Staphylococcus aureus is the most important Gram-positive colonizer of human skin and nasal passage,causing high morbidity and mortality.SD-repeat containing protein D(SdrD),an MSCRAMM(Microbial Surface Components Recognizing Adhesive Matrix Molecules)family surface protein,plays an important role in S.aureus adhesion and pathogenesis,while its binding target and molecular mechanism remain largely unknown.Here we solved the crystal structures of SdrD N2-N3 domain and N2-N3-B1 domain.Through structural analysis and comparisons,we characterized the ligand binding site of SdrD,and proposed a featured sequence motif of its potential ligands.In addition,the structures revealed for the first time the interactions between B1 domain and N2-N3 domain among B domain-containing MSCRAMMs.Our results may help in understanding the roles SdrD plays in S.aureus adhesion and shed light on the development of novel antibiotics.
