Basic structure of antibodies (Ab’s): Antibodies are heterodimers
MLRS 242 Immunology Pat Reed Antibodies
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Transcript of MLRS 242 Immunology Pat Reed Antibodies
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MLRS 242Immunology
Pat ReedAntibodies
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Serum proteins
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General antibody structure
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Enzyme digestion fragments
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Protein structure of immunoglobulins
• Early amino acid sequence experiments were unsuccessful—too much variation
• Multiple myeloma serum is 95% same antibody• Bence-jones protein found in urine of myeloma
patients is excess light chain• 110 amino acids highly variable, rest are quite
constant• 5 different isotypes identified: based on type of
heavy chain: G,D,E,M,A• Human light chains: 60% kappa (K) chains, 40%
lambda (L) chains
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Ribbon model of antibody
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Detailed structure of antibody
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Ribbon model of variable region
• Variable region contains highly variable connecting regions called complementarity-determining regions or CDRs
• These regions are also shown to be the antigen binding sites
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Model of antibody
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Amino acid diversity of variable domains – complementarity- determining regions (CDRs)
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Antigen – antibody interaction
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Space filling model
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Hiv protease and Fab fragmentConformational change in Fab
domain
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General structures of different antibody classes
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Subclasses of IgG
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Secretory IgA
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Receptor bound IgE
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• Isotype – different species
• Allotype – same species, different alleles
• Idiotype – same species, different VH and VL domains
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Isotypic determinants – different species variation within the
constant region
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Allotypic determinants – different constant regions within the same
species – different alleles
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Idiotypic determinants – variations in the variable region within the
same antibody type
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B Cell Receptor - BCR
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Fc receptors – bind Fc portion of antibody molecules
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Immunoglobulin superfamily of cell receptors – evolved from common
ancestor gene
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More members of the Ig superfamily
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Monoclonal antibodies
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Many uses for monoclonal antibodies
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Antibodies can deliver drugs to specific targets