Jove
Visualize
Contact Us

Related Concept Videos

Transcytosis of IgG01:15

Transcytosis of IgG

3.0K
Transcytosis is the process in which molecules are internalized by endocytosis, transported across the cell, and released through exocytosis from the opposite end of the cell. Molecules such as insulin, immunoglobulins, and certain nutrients are transferred through the recycling endosomes by recycling and transcytosis.
IgG molecules from a mother undergo transcytosis starting around 13 weeks of gestation. The amount of IgG transferred and entering the fetal blood circulation increases with...
3.0K
Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled Receptors

2.8K
G Protein–Coupled Receptors (GPCRs) are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to various stimuli. GPCRs regulate critical physiological pathways and are excellent drug targets for treating diseases such as diabetes, cancer, obesity, depression, or Alzheimer's. Nearly 35% of approved drugs implement their therapeutic effects by selectively interacting with specific GPCRs.
GPCRs are also called heptahelical,...
2.8K
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

3.5K
Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
3.5K
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

13.9K
G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
13.9K
Antibody Structure01:10

Antibody Structure

61.6K
Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
61.6K

You might also read

Related Articles

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

Sort by
Same author

Allotypes matter: Evaluation of twelve commercially available antihuman IgG2 antibodies for subclass specificity.

Journal of immunological methods·2026
Same author

Fc-fucosylation of Plasmodium falciparum-specific IgG varies with antigen and immunization.

The Journal of infectious diseases·2026
Same author

Clinical implications of natalizumab Fab-arm exchange in patients with multiple sclerosis.

Frontiers in immunology·2026
Same author

Structural promiscuity in the human circulatory IgA1 clonal repertoire.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Maternal anti-HPA-1a antibodies block αIIbβ3 and αvβ3 integrin activation which correlates with FNAIT disease severity.

Blood·2026
Same author

Antigen-specific IgG glycosylation profiles in hamsters and macaques following COVID-19 vaccination.

iScience·2026
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 Video

Updated: Oct 7, 2025

Assessment of Human Natural Killer Cell Events Driven by FcγRIIIa Engagement in the Presence of Therapeutic Antibodies
09:54

Assessment of Human Natural Killer Cell Events Driven by FcγRIIIa Engagement in the Presence of Therapeutic Antibodies

Published on: May 22, 2020

3.7K

Human IgE does not bind to human FcRn.

Maximilian Brinkhaus1, Elvera J van der Kooi1, Arthur E H Bentlage1

  • 1Department of Experimental Immunohematology, Sanquin Research and Landsteiner Laboratory, Amsterdam UMC, University of Amsterdam, Plesmanlaan 125, 1066 CX, Amsterdam, The Netherlands.

Scientific Reports
|January 8, 2022
PubMed
Summary
This summary is machine-generated.

The neonatal Fc receptor (FcRn) does not directly bind to IgE antibodies. This suggests that IgE may transfer from mother to fetus indirectly, potentially passing on allergies.

More Related Videos

Development of an in vitro model system for studying the interaction of Equus caballus IgE with its high-affinity receptor FcεRI
07:31

Development of an in vitro model system for studying the interaction of Equus caballus IgE with its high-affinity receptor FcεRI

Published on: November 1, 2014

12.5K
Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells
14:02

Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells

Published on: April 9, 2018

8.6K

Related Experiment Videos

Last Updated: Oct 7, 2025

Assessment of Human Natural Killer Cell Events Driven by FcγRIIIa Engagement in the Presence of Therapeutic Antibodies
09:54

Assessment of Human Natural Killer Cell Events Driven by FcγRIIIa Engagement in the Presence of Therapeutic Antibodies

Published on: May 22, 2020

3.7K
Development of an in vitro model system for studying the interaction of Equus caballus IgE with its high-affinity receptor FcεRI
07:31

Development of an in vitro model system for studying the interaction of Equus caballus IgE with its high-affinity receptor FcεRI

Published on: November 1, 2014

12.5K
Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells
14:02

Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells

Published on: April 9, 2018

8.6K

Area of Science:

  • Immunology
  • Perinatal Medicine
  • Molecular Biology

Background:

  • The neonatal Fc receptor (FcRn) facilitates IgG transfer from mother to fetus, crucial for passive immunity.
  • Immunoglobulin E (IgE) is primarily involved in allergic reactions and defense against parasites.
  • Emerging evidence indicates FcRn might be involved in IgE transplacental passage, but direct interaction is unconfirmed.

Purpose of the Study:

  • To investigate the direct binding interaction between human IgE and the neonatal Fc receptor (FcRn).
  • To compare the binding affinities of IgE and IgG to FcRn under physiological and endosomal conditions.

Main Methods:

  • Utilized surface plasmon resonance (SPR) to analyze binding kinetics.
  • Employed recombinant soluble human FcRn complexed with β2-microglobulin (sFcRn).
  • Tested binding interactions of human IgE and IgG variants at pH 7.4 and pH 6.0.

Main Results:

  • No direct binding interaction was detected between human IgE and human sFcRn at either tested pH.
  • This contrasts with the known interaction of IgG with FcRn, which is pH-dependent.

Conclusions:

  • FcRn does not directly bind IgE, indicating that FcRn-mediated IgE transfer across the placenta is likely indirect.
  • The indirect transfer mechanism may have implications for the transmission of maternal allergic sensitization to the fetus.