Isolation of high-affinity human IgE and IgG antibodies recognising Bet v 1 and Humicola lanuginosa lipase from combinatorial phage libraries.
Allergen-specific Fab fragments isolated from combinatorial IgE and IgG libraries are useful tools for studying allergen-antibody interactions. To characterise the interaction between different allergens and antibodies we have created recombinant human phage antibody libraries in the Fab format. Human IgE and IgG libraries have been created from patients allergic to birch pollen or lipase. These libraries have been used to select binders recognising the major birch pollen allergen Bet v 1 and Humicola lanuginosa lipase. A panel of allergen-specific IgE and IgG antibodies were identified; these were further characterised by allergen binding studies using Biacore and competition studies using human sera and antibodies purified from human sera. Affinities in the nM range were recorded and a competition with human sera for allergen binding was observed.
Department of Molecular Biology, Aarhus University, Gustav Wieds Vej, Aarhus C, Denmark.
Charlotte G
CG
Jakobsen
Uffe
U
Bodtger
Peter
P
Kristensen
Lars K
LK
Poulsen
Erwin L
EL
Roggen
D000485:Allergens / Q000276:immunology*; D000595:Amino Acid Sequence; D052179:Antigens, Plant; D001402:B-Lymphocytes / Q000276:immunology; D001483:Base Sequence; D006801:Humans; D007073:Immunoglobulin E / Q000097:blood / Q000276:immunology / Q000302:isolation & purification*; D007074:Immunoglobulin G / Q000097:blood / Q000276:immunology / Q000302:isolation & purification*; D008049:Lipase / Q000276:immunology*; D008969:Molecular Sequence Data; D019151:Peptide Library
D000485:Allergens; D052179:Antigens, Plant; D007074:Immunoglobulin G; D019151:Peptide Library; D007073:Immunoglobulin E; D008049:Lipase