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

Human IgG2 can form covalent dimers.

Esther M Yoo1, Letitia A Wims, Lisa A Chan

  • 1Department of Microbiology, Immunology, and Molecular Genetics and Molecular Biology Institute, University of California, Los Angeles, CA 90095,USA.

Journal of Immunology (Baltimore, Md. : 1950)
|March 11, 2003
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

An Anti-CD138-Targeted Interferon-Alpha Has Broad Efficacy in Solid Tumors Through Direct Tumor Cell Killing and Intratumoral Immune Modulation.

Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research·2024
Same author

Genetically engineered antibodies and their application to brain delivery.

Advanced drug delivery reviews·2022
Same author

89Zr-ImmunoPET Shows Therapeutic Efficacy of Anti-CD20-IFNα Fusion Protein in a Murine B-cell Lymphoma Model.

Molecular cancer therapeutics·2022
Same author

Plasma Cells Are Obligate Effectors of Enhanced Myelopoiesis in Aging Bone Marrow.

Immunity·2019
Same author

Elastomeric sensor surfaces for high-throughput single-cell force cytometry.

Nature biomedical engineering·2019
Same author

Publisher Correction: Elastomeric sensor surfaces for high-throughput single-cell force cytometry.

Nature biomedical engineering·2019
Same journal

Optineurin restrains IL-17-associated neuroinflammation in trigeminal ganglia to preserve sensory function after ocular HSV-1 infection.

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

Crystal structure and immune single-cell atlas provide insights into the functional divergence of type I IFNs in fish.

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

Complement C3 deficiency increases the effector and cytotoxic functions of NK cells and suppresses tumor growth.

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

Increased Nur77 is disconnected from TCR affinity in insulin-specific Tregs.

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

FTR85 negatively regulates type I IFN antiviral signaling pathway by promoting K48-linked polyubiquitination of IRF3.

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

An MR1-specific nanobody capable of blocking MR1T cell activation.

Journal of immunology (Baltimore, Md. : 1950)·2026
See all related articles

Researchers discovered covalent dimers in human immunoglobulin G2 (IgG2) antibodies, unlike previously observed noncovalent interactions. This finding suggests a novel mechanism for IgG2 antibody function in immune responses.

Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • Immunoglobulin A (IgA) and Immunoglobulin M (IgM) are known to form covalent polymers.
  • Murine IgG3 antibodies have been observed to polymerize via noncovalent interactions in the presence of specific antigens.
  • Covalent polymerization of human IgG subclasses, particularly IgG2, has not been previously established.

Purpose of the Study:

  • To investigate the potential for covalent polymerization in human IgG antibodies.
  • To characterize the nature and presence of IgG2 dimers in human samples.

Main Methods:

  • Production and analysis of recombinant human IgG2 antibodies in myeloma cells.
  • Analysis of pooled human gamma globulin and normal human sera.
  • Cyanogen bromide cleavage analysis to identify involved residues.

Related Experiment Videos

Main Results:

  • Detection of covalent dimers in three different recombinant human IgG2 antibody preparations.
  • Confirmation of IgG2 dimers in pooled human gamma globulin and normal sera.
  • Distinction of these covalent IgG2 dimers from noncovalent dimers arising from idiotype/anti-idiotype interactions.
  • Cyanogen bromide cleavage suggests involvement of cysteine residues in the IgG2 hinge region in dimer formation.

Conclusions:

  • Human IgG2 antibodies can form covalent dimers, a previously unrecognized form of IgG polymerization.
  • These covalent IgG2 dimers are distinct from noncovalent interactions.
  • The findings suggest a potential role for IgG2 covalent dimers in immunity, particularly against carbohydrate antigens.