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Related Concept Videos

Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

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...
Transcytosis of IgG01:15

Transcytosis of IgG

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...
Diversity of Antigen Receptors01:28

Diversity of Antigen Receptors

Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...
Antibody Structure01:10

Antibody Structure

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...
Antibody Structure and Classes01:25

Antibody Structure and Classes

Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
Selectins01:25

Selectins

Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain, which...

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Updated: May 22, 2026

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment
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The rs150311303 polymorphism in FcγRIIa enhances IgG binding capacity.

A H Omar1, H Shibata, M Yasunami

  • 1Department of Immunogenetics, Institute of Tropical Medicine (NEKKEN) and Global COE Program, Nagasaki University, Nagasaki, Japan.

Scandinavian Journal of Immunology
|May 1, 2012
PubMed
Summary

Genetic variations in the Fc gamma receptor IIa (FcγRIIa) gene did not significantly impact susceptibility to symptomatic malaria in Ghanaian children. However, specific FcγRIIa haplotype variants showed enhanced binding capabilities to IgG subclasses.

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Area of Science:

  • Immunogenetics
  • Infectious Diseases
  • Human Genetics

Background:

  • Fc gamma receptor (FcγR) is crucial for linking humoral and cellular immunity.
  • FcγRIIa-H131R polymorphism influences IgG subclass binding and malaria susceptibility.
  • Understanding FcγRIIa gene polymorphisms is vital for malaria endemic populations.

Purpose of the Study:

  • To investigate the association between FCGR2A gene polymorphisms and symptomatic malaria risk in Ghanaian children.
  • To analyze the functional impact of FcγRIIa polymorphisms on IgG subclass binding.

Main Methods:

  • Genotyping of 429 Ghanaian children for FCGR2A polymorphisms using direct DNA sequencing.
  • Calculation of attributable and relative risks for symptomatic malaria.
  • Flow cytometric analysis of HEK cells transfected with FcγRIIa variants to assess IgG subclass binding.

Main Results:

  • Two major FCGR2A polymorphisms (rs1801274 and rs150311303) were identified.
  • No significant association was found between these polymorphisms and symptomatic malaria susceptibility.
  • The FcγRIIa(RL) haplotype variant demonstrated the highest binding ability to IgG1, IgG3, and IgG4.

Conclusions:

  • FCGR2A gene polymorphisms rs1801274 and rs150311303 are not significantly associated with symptomatic malaria in this Ghanaian cohort.
  • The FcγRIIa(RL) haplotype variant exhibits enhanced IgG subclass binding, suggesting potential functional implications.
  • Further research may explore the broader immunogenetic landscape of malaria resistance.