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Printable Handouts
Navigable Slide Index
- Introduction
- Introduction to antibody function
- Antibody classes have different valancies
- Valency increases avidity
- Valency allows for co-operative binding
- The antibody is an adapter molecule
- Fc Receptors
- Human antibody isotype Fc effector functions
- Human IgG subclasses are similar in sequence but have different functional properties
- Human IgG Fc Receptors
- Cell distribution and modulation of expression of leukocyte FcR
- Cell signalling by immune complexes
- The neonatal receptor FcRn (Brambell receptor)
- The IgG receptor FcRn
- FcRn protection function
- IgG1 allotypes
- A role for human IgG allotypes?
- Binding of human IgG to cells infected with HSV-1
- Binding of human IgG1 allotype variants to cells infected with HSV-1
- Thank you for listening
Topics Covered
- The significance of valency in antigen recognition
- Functional properties of antibodies
- The role of different classes and subclasses of antibodies in immune functions
- Immune complexes
- Fc Receptors
- Allotypes
Links
Series:
Categories:
Therapeutic Areas:
Talk Citation
Clark, M. (2021, February 28). Antibody structure and function: antibody function [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved December 3, 2024, from https://doi.org/10.69645/PZEZ2498.Export Citation (RIS)
Publication History
Financial Disclosures
- Requested.
Antibody structure and function: antibody function
Published on February 28, 2021
42 min
Other Talks in the Series: The Immune System - Key Concepts and Questions
Transcript
Please wait while the transcript is being prepared...
0:00
Hello, my name is Dr. Mike Clark.
I was formerly Reader in therapeutic and
molecular immunology in the Department of Pathology, Cambridge University.
This is part of the lecture on antibody structure and function,
this is the second part of that lecture dealing with the functions of antibodies.
0:16
In this lecture, we're going to deal with
the structure of the different classes and subclasses of antibody.
In particular, we're going to deal with
the significance of valency in antigen recognition,
and also the role of different classes and
subclasses of antibodies in their immune functions.
0:32
Let's return now to something that we were discussing earlier,
the valency of the antibodies for binding antigen.
Essentially lining up these structures, IgG,
IgA, and IgM to use as examples.
As I mentioned before, we've got a monomeric type structure for the IgG,
where we have two antigen-binding sites.
We've got a dimeric structure for the IgA dimer,
where we have four antigen-binding sites.
We've got that pentameric structure
(five repeated subunits) for the IgM,
where we've got 10 binding sites.
We can discuss the valency of IgG as being bivalent,
we can discuss the valency of IgA as being
tetravalent, and we discuss the valency of IgM as being decavalent,
so two valencies, four valencies, ten valencies.
That's the maximum number of antigens that each of these molecules could
bind simultaneously through the Fab arms that are available in individual molecule.
That becomes crucial to an understanding of how these molecules interact with antigen.
What I want to do is to discuss how the valency of the antibody (that