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

The structural requirements for complement activation by IgG: does it hinge on the hinge?

O H Brekke1, T E Michaelsen, I Sandlie

  • 1Dept of Biology, University of Oslo, Norway.

Immunology Today
|February 1, 1995
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

Human Secretory IgM Antibodies Activate Human Complement and Offer Protection at Mucosal Surface.

Scandinavian journal of immunology·2016
Same author

Human IgG1, IgG3, and IgG3 Hinge-Truncated Mutants Show Different Protection Capabilities against Meningococci Depending on the Target Antigen and Epitope Specificity.

Clinical and vaccine immunology : CVI·2016
Same author

A public T cell receptor recognized by a monoclonal antibody specific for the D-J junction of the β-chain.

Scandinavian journal of immunology·2013
Same author

Pectic polysaccharides isolated from Malian medicinal plants protect against Streptococcus pneumoniae in a mouse pneumococcal infection model.

Scandinavian journal of immunology·2013
Same author

Different glycosylation pattern of human IgG1 and IgG3 antibodies isolated from transiently as well as permanently transfected cell lines.

Scandinavian journal of immunology·2013
Same author

Chemical and biological characterization of polysaccharides from wild and cultivated roots of Vernonia kotschyana.

Journal of ethnopharmacology·2011

Antibody hinge flexibility is not essential for complement activation. The presence of inter-heavy-chain disulfide bonds in the antibody hinge region is the sole requirement for this immune response. Structural differences in CH2 domains dictate effector functions.

Area of Science:

  • Immunology
  • Molecular Biology
  • Structural Biology

Background:

  • Antibody flexibility, primarily attributed to the hinge region, has been considered crucial for complement activation.
  • Recent research challenges the necessity of hinge flexibility for IgG-mediated complement activation.

Purpose of the Study:

  • To investigate the essential structural requirements of the antibody hinge region for complement activation.
  • To identify the structural basis for functional differences among IgG subclasses.

Main Methods:

  • The study likely involved structural analysis and functional assays of engineered antibody variants.
  • Investigating the role of inter-heavy-chain disulfide bonds and CH2 domains in antibody effector functions.

Main Results:

Related Experiment Videos

  • The presence of inter-heavy-chain disulfide bonds, not hinge flexibility, is the critical factor for complement activation.
  • The CH2 domain of the immunoglobulin molecule harbors the structural determinants for variations in IgG effector functions.

Conclusions:

  • The established link between IgG hinge flexibility and complement activation is re-evaluated, highlighting disulfide bonds as the key element.
  • The CH2 domain is identified as the primary determinant of distinct effector functions across different IgG subclasses.