ArticleProtein & cell2013
Structures of SdrD from Staphylococcus aureus reveal the molecular mechanism of how the cell surface receptors recognize their ligands.
Article in Protein & cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 47 citations in OpenAlex.
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- In Silico Genome-Scale Analysis of Molecular Mechanisms Contributing to the Development of a Persistent Infection with Methicillin-ResistantInternational journal of molecular sciences · 2022Article
- Structural insights into the intermolecular interaction of the adhesin SdrC in the pathogenicity of Staphylococcus aureus.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Identification of Three Clf-Sdr Subfamily Proteins inFrontiers in microbiology · 2021Article
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- Surface Proteins ofMicrobiology spectrum · 2019Review
- Adhesive Interactions Between Lactic Acid Bacteria and β-Lactoglobulin: Specificity and Impact on Bacterial Location in Whey Protein Isolate.Frontiers in microbiology · 2019Article
- Calcium stabilizes the strongest protein fold.Nature communications · 2018Article
- Genetic variability in the sdrD gene in Staphylococcus aureus from healthy nasal carriers.BMC microbiology · 2018Article
- Septic arthritis caused by an emerging ST121 methicillin-susceptible, PVL-negativeNew microbes and new infections · 2017Article
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- The rising young scientist stars in China.Protein & cell · 2016Article
- Mechanical Strength and Inhibition of the Staphylococcus aureus Collagen-Binding Protein Cna.mBio · 2016Article
- Bacillus anthracis S-layer protein BslA binds to extracellular matrix by interacting with laminin.BMC microbiology · 2016Article
- Isopeptide bond in collagen- and fibrinogen-binding MSCRAMMs.Biophysical reviews · 2016Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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