Non-linear antigenic regions in epidermal growth factor (EGF) and transforming growth factor alpha (TGF alpha) studied by EGF-TGF alpha chimaeras

With the help of 16 chimaeras between human epidermal growth factor (hEGF) and human transforming growth factor alpha (hTGF alpha), a detailed analysis was performed on the epitope recognized by two polyclonal antibodies raised against hEGF, and one polyclonal antibody raised against hTGF alpha. All...

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Bibliographic Details
Published in:Biochemical journal 2000-07, Vol.349 (Pt 1), p.267-274
Main Authors: van de Poll, M L, van Rotterdam, W, Gadellaa, M M, Stortelers, C, van Vugt, M J, van Zoelen, E J
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Antibodies - metabolism
Antigens - chemistry
Binding Sites
Cell Division
Dose-Response Relationship, Drug
Drosophila
Drosophila Proteins
Epidermal Growth Factor - chemistry
Epidermal Growth Factor - immunology
Epitope Mapping
Epitopes - chemistry
Humans
Membrane Proteins - chemistry
Models, Molecular
Molecular Sequence Data
Protein Conformation
Protein Structure, Secondary
Receptors, Notch
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - metabolism
Sequence Homology, Amino Acid
Transforming Growth Factor alpha - chemistry
Transforming Growth Factor alpha - immunology
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Summary:With the help of 16 chimaeras between human epidermal growth factor (hEGF) and human transforming growth factor alpha (hTGF alpha), a detailed analysis was performed on the epitope recognized by two polyclonal antibodies raised against hEGF, and one polyclonal antibody raised against hTGF alpha. All three antibodies recognized essentially the same antigenic site, a non-linear and conformation-dependent sequence that is located near the second and fourth disulphide-bonded cysteines and that includes the start of the B-loop beta-sheet. The epitope recognized by the anti-hEGF antibodies was further characterized using 8 chimaeras between hEGF and an EGF-repeat from Drosophila Notch and was found to include Met(21), Ala(30) and Asn(32). All three polyclonal antibodies were able to neutralize the biological activity of the respective growth factor when tested on 32D murine haematopoietic progenitor cells transfected with ErbB-1, indicating that the receptor binding domain is shielded upon binding of the antibody.
ISSN:0264-6021
1470-8728
DOI:10.1042/0264-6021:3490267