Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

A structural basis for complement inhibition by Staphylococcus aureus.

Michal Hammel1, Georgia Sfyroera, Daniel Ricklin

  • 1Division of Cell Biology and Biophysics, School of Biological Sciences, University of Missouri at Kansas City, Kansas City, Missouri 64110, USA.

Nature Immunology
|March 14, 2007
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Bacterial targeting of the neutrophil inhibitory receptor LILRB3 to evade antibody immunity.

Nature communications·2026
Same author

Production and characterization of gigastasin, a leech-derived inhibitor of complement and coagulation pathways.

Scientific reports·2026
Same author

New Analogs of the Compstatin Family of Clinical Complement Inhibitors with Low Picomolar Target Affinity.

Journal of medicinal chemistry·2026
Same author

Targeting Cancer-Associated PCNA with AOH1996 Induces Mitotic Catastrophe and Enhances Cisplatin Therapy in Cervical Cancer.

Cancer research communications·2026
Same author

Response to comment on "the C-terminal domain of Staphylococcus aureus Efb recruits FHR-2 to C3b, synergistically inhibiting the terminal complement pathway".

Journal of immunology (Baltimore, Md. : 1950)·2026
Same author

The C-terminal domain of Staphylococcus aureus Efb recruits FHR-2 to C3b, synergistically inhibiting the terminal complement pathway.

Journal of immunology (Baltimore, Md. : 1950)·2025
Same journal

Editorial Expression of Concern: Recognition of the nonclassical MHC class I molecule H2-M3 by the receptor Ly49A regulates the licensing and activation of NK cells.

Nature immunology·2026
Same journal

Inflammatory immune modulators of AML lung infiltration and respiratory failure.

Nature immunology·2026
Same journal

The neuroimmune system and cognition.

Nature immunology·2026
Same journal

Critical connections.

Nature immunology·2026
Same journal

Innate immune signaling and functions in astrocytes.

Nature immunology·2026
Same journal

Epigenetic mechanisms of inflammatory memory in the central nervous system.

Nature immunology·2026
See all related articles

Staphylococcus aureus uses its extracellular fibrinogen-binding protein (Efb-C) to inhibit the complement system. This bacterial protein binds to human C3, altering its shape and blocking immune responses.

Area of Science:

  • Immunology
  • Microbiology
  • Structural Biology

Background:

  • The complement system is crucial for innate immunity, identifying and eliminating pathogens.
  • Bacteria have evolved mechanisms to evade complement-mediated destruction.
  • Staphylococcus aureus employs virulence factors to subvert host immune responses.

Purpose of the Study:

  • To elucidate the structural basis of complement inhibition by Staphylococcus aureus extracellular fibrinogen-binding protein (Efb-C).
  • To understand how Efb-C interacts with complement component C3 to evade immune detection.

Main Methods:

  • X-ray crystallography was used to determine the structures of Efb-C free and bound to human C3d.
  • Structure-function studies were performed to analyze the inhibitory mechanism.

Related Experiment Videos

Main Results:

  • The structure of Efb-C revealed a helical motif critical for complement regulation.
  • The structure of Efb-C bound to C3d provided insights into pathogen recognition of complement proteins.
  • Efb-C was shown to bind native C3, altering its conformation and preventing downstream complement activation.

Conclusions:

  • Efb-C represents a novel mechanism for bacterial complement evasion.
  • Understanding Efb-C's interaction with C3 can inform strategies to enhance complement-mediated immunity against S. aureus.