ArticleProtein science : a publication of the Protein Society2008
Electrostatic contributions drive the interaction between Staphylococcus aureus protein Efb-C and its complement target C3d.
Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
- An overview of moonlighting proteins in Staphylococcus aureus infection.Archives of microbiology · 2021Review
- A Coarse-Grained Methodology Identifies Intrinsic Mechanisms That Dissociate Interacting Protein Pairs.Frontiers in molecular biosciences · 2020Article
- HawkDock: a web server to predict and analyze the protein-protein complex based on computational docking and MM/GBSA.Nucleic acids research · 2019Article
- The Streptococcus agalactiae complement interfering protein combines multiple complement-inhibitory mechanisms by interacting with both C4 and C3 ligands.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Native State of Complement Protein C3d Analysed via Hydrogen Exchange and Conformational Sampling.International journal of computational biology and drug design · 2018Article
- A rapid method for selecting suitable animal species for studying pathogen interactions with plasma protein ligands in vivo.Microbial biotechnology · 2017Article
- Structural Implications for the Formation and Function of the Complement Effector Protein iC3b.Journal of immunology (Baltimore, Md. : 1950) · 2017Article
- Complement component C3 - The "Swiss Army Knife" of innate immunity and host defense.Immunological reviews · 2016Review
- Complement System Part II: Role in Immunity.Frontiers in immunology · 2015Review
- DENV-2 subunit proteins fused to CR2 receptor-binding domain (P28)-induces specific and neutralizing antibodies to the Dengue virus in mice.Human vaccines & immunotherapeutics · 2013Article
- Manipulating the mediator: modulation of the alternative complement pathway C3 convertase in health, disease and therapy.Immunobiology · 2012Review
- Staphylococcus aureus proteins Sbi and Efb recruit human plasmin to degrade complement C3 and C3b.PloS one · 2012Article
- Advances in understanding the structure, function, and mechanism of the SCIN and Efb families of Staphylococcal immune evasion proteins.Advances in experimental medicine and biology · 2012Review
- Learning probabilistic models of hydrogen bond stability from molecular dynamics simulation trajectories.BMC bioinformatics · 2011Article
- A structural basis for Staphylococcal complement subversion: X-ray structure of the complement-binding domain of Staphylococcus aureus protein Sbi in complex with ligand C3d.Molecular immunology · 2011Article
- Allosteric inhibition of complement function by a staphylococcal immune evasion protein.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Multi-scale characterization of the energy landscape of proteins with application to the C3D/Efb-C complex.Proteins · 2010Article
- A molecular insight into complement evasion by the staphylococcal complement inhibitor protein family.Journal of immunology (Baltimore, Md. : 1950) · 2009Article
- Cutting edge: members of the Staphylococcus aureus extracellular fibrinogen-binding protein family inhibit the interaction of C3d with complement receptor 2.Journal of immunology (Baltimore, Md. : 1950) · 2008Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
The C3-inhibitory domain of Staphylococcus aureus extracellular fibrinogen-binding protein (Efb-C) defines a novel three-helix bundle motif that regulates complement activation. Previous crystallographic studies of Efb-C bound to its cognate subdomain of human C3 (C3d) identified Arg-131 and Asn-138 of Efb-C as key residues for its activity. In order to characterize more completely the physical and chemical driving forces behind this important interaction, we employed in this study a combination of structural, biophysical, and computational methods to analyze the interaction of C3d with Efb-C and the single-point mutants R131A and N138A. Our results show that while these mutations do not drastically affect the structure of the Efb-C/C3d recognition complex, they have significant adverse effects on both the thermodynamic and kinetic profiles of the resulting complexes. We also characterized other key interactions along the Efb-C/C3d binding interface and found an intricate network of salt bridges and hydrogen bonds that anchor Efb-C to C3d, resulting in its potent complement inhibitory properties.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.