Related Experiment Video
Updated: May 29, 2026

Double Labeling Immunofluorescence using Antibodies from the Same Species to Study Host-Pathogen Interactions
Published on: July 10, 2021
A conserved host and pathogen recognition site on immunoglobulins: structural and functional aspects
Bruce D Wines1, Halina M Trist, William Farrugia
1Centre for Immunology, Burnet Institute, Melbourne, VIC 3004, Australia. bwines@burnet.edu.au
Pathogen proteins target a common site on immunoglobulin Fc regions, crucial for host immunity and pathogen evasion. Understanding these interactions reveals potential virulence mechanisms affecting innate and adaptive immunity.
Area of Science:
- Immunology
- Structural Biology
- Molecular Recognition
Background:
- A conserved region in the constant (Fc) part of immunoglobulins serves as a binding site for host receptors and is targeted by pathogen proteins.
- This site, located at the junction of antibody heavy chain constant domains (CH2 and CH3 in IgG/IgA, CH3 and CH4 in IgM), forms a shallow cavity.
Purpose of the Study:
- To review the structural and functional aspects of molecular recognition at the common Fc site by host and pathogen molecules.
- To explore how pathogen interactions with this site may influence host immunity and virulence.
Main Methods:
- Analysis of crystal structures of immunoglobulin Fc complexes with various ligands.
- Review of existing literature on host-pathogen interactions at the Fc region.
Main Results:
- Structural data exists for IgG-Fc and IgA-Fc complexes with diverse host, pathogen, and in vitro selected ligands.
- Pathogen proteins may evade host immunity by directly blocking Fc interactions.
- Pathogen molecules likely interact with other host factors for their biological functions.
Conclusions:
- Pathogen proteins exploit a common molecular site on immunoglobulin Fc regions for immune evasion.
- These interactions may promote pathogen virulence by modulating the bridge between innate and adaptive immunity.
Related Concept Videos
Antibody Structure
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
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 Classes
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.
Immunoglobulin-like Cell Adhesion Molecules
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Antigens Involved in Adaptive Immunity
Complete Antigens
Complete antigens possess both immunogenicity and reactivity.

