Antigenic determination fragments of alpha-momorcharin
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AbstractAlpha momorcharin is a protein isolated from the bitter gourd. It has a number of biological activities including induction of abortion, inhibition of tumor growth and anti-HIV. All these activities may be related to the ribosome-inhibiting activity of the protein. Repeated use of alpha MMC can elicit an antigenic response which may neutralize its biological activity. To overcome this problem, we need to know which part of the molecule is the antigenic determinant. In this study, we constructed a random fragment expression library from the alpha MMC cDNA and screened it with three anti-alpha MMC sera. A total of 9 positive clones were picked and sequenced. Based on the sequence information obtained, we were able to deduce three regions at which antibodies raised against native alpha MMC seem to interact. These regions are residues 1-14, residues 71-136 and residues 195-222. Mapping of these regions against a 3D model of alpha MMC indicates that they all are located on the surface of the molecule. As residues 71-136 are found to be in close proximity to the active site involved in ribosome inactivation, treatment with a monoclonal antibody directed to this area was shown to be effective in inactivating the inhibitory effect of alpha MMC on in vitro protein synthesis. (C) 1997 Elsevier Science B.V.
All Author(s) ListLeung KC, Meng ZQ, Ho WKK
Journal nameBBA - General Subjects
Year1997
Month10
Day20
Volume Number1336
Issue Number3
PublisherELSEVIER SCIENCE BV
Pages419 - 424
ISSN0304-4165
eISSN1872-8006
LanguagesEnglish-United Kingdom
Keywordsalpha-momorcharin; antigenicity; protein structure; random fragment; ribosome-inactivating protein; trichosanthin
Web of Science Subject CategoriesBiochemistry & Molecular Biology; BIOCHEMISTRY & MOLECULAR BIOLOGY; Biophysics; BIOPHYSICS

Last updated on 2020-22-10 at 00:53