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Related Concept Videos

Protein Families02:47

Protein Families

Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key locations, protein...
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 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...
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...
Exon Recombination02:32

Exon Recombination

The evolution of new genes is critical for speciation. Exon recombination, also known as exon shuffling or domain shuffling, is an important means of new gene formation. It is observed across vertebrates, invertebrates, and in some plants such as potatoes and sunflowers. During exon recombination, exons from the same or different genes recombine and produce new exon-intron combinations, which might evolve into new genes. 
Exon shuffling follows “splice frame rules.” Each exon has three reading...
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.

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Quantification of Circulating Pig-Specific DNA in the Blood of a Xenotransplantation Model
07:34

Quantification of Circulating Pig-Specific DNA in the Blood of a Xenotransplantation Model

Published on: September 22, 2020

Porcine IgG: structure, genetics, and evolution.

J E Butler1, Nancy Wertz, Nicholas Deschacht

  • 1Department of Microbiology and Interdisciplinary Immunology Program, The University of Iowa, Iowa City, IA 52242, USA. john-butler@uiowa.edu

Immunogenetics
|December 3, 2008
PubMed
Summary
This summary is machine-generated.

Researchers identified eleven porcine Cgamma gene sequences, revealing over 20 potential antibody chains. This highlights species-specific antibody functions, cautioning against extrapolating findings between different mammals.

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Area of Science:

  • Immunogenetics
  • Comparative genomics
  • Mammalian immunology

Background:

  • The diversity and evolutionary origins of porcine immunoglobulin G (IgG) subclasses remain incompletely understood.
  • Previous classifications of porcine IgG genes require refinement based on genomic data.

Purpose of the Study:

  • To characterize the genomic sequences of porcine Cgamma genes.
  • To elucidate the evolutionary relationships and functional implications of porcine IgG subclasses.

Main Methods:

  • Genomic sequencing of porcine Cgamma genes.
  • Sequence analysis and comparison with other mammalian IgG genes.
  • Identification of potential functional motifs and interaction sites.

Main Results:

  • Eleven genomic porcine Cgamma gene sequences were identified, representing six putative subclasses.
  • Established that previously described IgG1 and IgG3 genes are allelic variants of IGHG1 and IGHG2.
  • Discovered a unique, evolutionarily conserved porcine IgG3 with an extended hinge and identified potential functional interactions with Fcgamma receptors, FcRn, protein A, and protein G.

Conclusions:

  • Porcine IgG subclasses diversified after speciation, necessitating species-specific functional assessments.
  • The identified porcine IgG subclasses exhibit distinct structural features and potential effector functions.
  • Swine possess the capacity to transcribe over 20 different Cgamma chains, indicating significant antibody repertoire diversity.