Thermodynamic and kinetic aspects of antibody evolution during the immune response to hapten

We determined thermodynamic and kinetic parameters for the antigen–antibody interaction using a group of anti-(4-hydroxy-3-nitrophenyl)acetyl monoclonal antibodies whose differences in amino acid sequences had arisen only from somatic hypermutation. These monoclonal antibodies were considered to hav...

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Bibliographic Details
Published in:Molecular immunology 2003-03, Vol.39 (13), p.801-808
Main Authors: Sagawa, Takuma, Oda, Masayuki, Ishimura, Miyuki, Furukawa, Koji, Azuma, Takachika
Format: Article
Language:English
Subjects:
Affinity maturation
Amino Acid Sequence
Animals
Antibodies, Monoclonal - genetics
Antibodies, Monoclonal - immunology
Antibodies, Monoclonal - metabolism
Antigen-Antibody Reactions - genetics
Antigen-Antibody Reactions - immunology
Antigen-Antibody Reactions - physiology
Antigen–antibody interaction
Binding kinetics
Binding thermodynamics
Circular Dichroism
Clonally related antibodies
Evolution, Molecular
Haptens - immunology
Kinetics
Mice
Models, Immunological
Molecular Sequence Data
Nitrophenols - immunology
Phenylacetates
Sequence Homology, Amino Acid
Somatic Hypermutation, Immunoglobulin
Surface Plasmon Resonance
Thermodynamics
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Summary:We determined thermodynamic and kinetic parameters for the antigen–antibody interaction using a group of anti-(4-hydroxy-3-nitrophenyl)acetyl monoclonal antibodies whose differences in amino acid sequences had arisen only from somatic hypermutation. These monoclonal antibodies were considered to have originated from a common ancestor clone and to represent progression along the affinity maturation pathway. The kinetic measurements showed that both association and dissociation rate constants of the antigen–antibody interaction decreased during maturation. Thermodynamic measurements revealed that an increase in affinity was obtained by an increase in entropy without any significant change in enthalpy. These results suggested that the mechanism for the antigen–antibody interaction shifted from a “zipper” type to a “lock-and-key” type during antibody evolution.
ISSN:0161-5890
1872-9142
DOI:10.1016/S0161-5890(02)00282-1