ArticleThe Journal of biological chemistry2008
Interaction of human complement with Sbi, a staphylococcal immunoglobulin-binding protein: indications of a novel mechanism of complement evasion by Staphylococcus aureus.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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Who cites it
73 citing papers in PubMed, 145 citations in OpenAlex.
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- A Scorecard for Information Synthesis in Multiple Experimental Conditions: Application to Bacterial Biofilm Matrix Transcriptomics.Current microbiology · 2025Article
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- Prevalence of Selected Immune Evasion Genes and Clonal Diversity in Methicillin-SusceptibleAntibiotics (Basel, Switzerland) · 2024Article
- Virulence attributes of successful methicillin-resistantClinical microbiology reviews · 2023Review
- Novel method for detecting complement C3 deposition on Staphylococcus aureus.Scientific reports · 2022Article
- Invariant surface glycoprotein 65 of Trypanosoma brucei is a complement C3 receptor.Nature communications · 2022Article
- The C-Terminal Domain ofPathogens (Basel, Switzerland) · 2022Article
- Complement component C3: A structural perspective and potential therapeutic implications.Seminars in immunology · 2022Review
- Staphylococcal Complement Evasion Protein Sbi Stabilises C3d Dimers by Inducing an N-Terminal Helix Swap.Frontiers in immunology · 2022Article
- Lipoteichoic Acid fromMicroorganisms · 2021Article
- Review
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- Out-Smarting the Host: Bacteria Maneuvering the Immune Response to Favor Their Survival.Frontiers in immunology · 2020Review
- Development of a vaccine against Staphylococcus aureus invasive infections: Evidence based on human immunity, genetics and bacterial evasion mechanisms.FEMS microbiology reviews · 2020Review
- Interaction of host and Staphylococcus aureus protease-system regulates virulence and pathogenicity.Medical microbiology and immunology · 2019Review
- The good side of inflammation: Staphylococcus aureus proteins SpA and Sbi contribute to proper abscess formation and wound healing during skin and soft tissue infections.Biochimica et biophysica acta. Molecular basis of disease · 2019Article
- Ensilication Improves the Thermal Stability of the Tuberculosis Antigen Ag85b and an Sbi-Ag85b Vaccine Conjugate.Scientific reports · 2019Article
- Surface Proteins ofMicrobiology spectrum · 2019Review
13 more citing papers are in PubMed but not listed here.
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Authors and funding
11 authors at 6 institutions in 5 countries.
Funding
Abstract
Staphylococcal immunoglobulin-binding protein, Sbi, is a 436-residue protein produced by many strains of Staphylococcus aureus. It was previously characterized as being cell surface-associated and having binding capacity for human IgG and beta(2)-glycoprotein I. Here we show using small angle x-ray scattering that the proposed extracellular region of Sbi (Sbi-E) is an elongated molecule consisting of four globular domains, two immunoglobulin-binding domains (I and II) and two novel domains (III and IV). We further show that together domains III and IV (Sbi-III-IV), as well as domain IV on its own (Sbi-IV), bind complement component C3 via contacts involving both the C3dg fragment and the C3a anaphylatoxin domain. Preincubation of human serum with either Sbi-E or Sbi-III-IV is inhibitory to all complement pathways, whereas domain IV specifically inhibits the alternative pathway. Monitoring C3 activation in serum incubated with Sbi fragments reveals that Sbi-E and Sbi-III-IV both activate the alternative pathway, leading to consumption of C3. By contrast, inhibition of this pathway by Sbi-IV does not involve C3 consumption. The observation that Sbi-E activates the alternative pathway is counterintuitive to intact Sbi being cell wall-associated, as recruiting complement to the surface of S. aureus would be deleterious to the bacterium. Upon re-examination of this issue, we found that Sbi was not associated with the cell wall fraction, but rather was found in the growth medium, consistent with it being an excreted protein. As such, our data suggest that Sbi helps mediate bacterial evasion of complement via a novel mechanism, namely futile fluid-phase consumption.
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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.