Primary structure of three distinct isoabrins determined by cDNA sequencing. Conservation and significance

J Mol Biol. 1993 Jan 5;229(1):263-7. doi: 10.1006/jmbi.1993.1029.

Abstract

A family of toxic proteins, the isoabrins, which possess N-glycosylase activity toward eukaryotic 28 S r-RNA, may have potential use in cancer chemotherapy. By polymerase chain reaction techniques, cDNA clones of three isoabrins, carrying A and B-chain sequences, were isolated and their nucleotide sequences were determined. The isoabrins consist of an A-chain comprised of 250 of 251 amino acids, followed by a 10 amino acid linker and a B-chain of 267 amino acids. There is substantial conservation in the B-chain of the three isoabrins, with less than six amino acid substitutions, whereas as many as 46 amino acid substitutions occur in the A-chains. Based on the relationships between the biological activities and the putative amino acid sequences of the isoabrins, three isoabrins, abrin-a, -b and -d, could be identified and the potential epitope of immunological response of these isoabrins could be assigned.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Abrin / chemistry*
  • Abrin / genetics
  • Abrin / immunology
  • Amino Acid Sequence
  • Base Sequence
  • Cross Reactions
  • Molecular Sequence Data
  • Sequence Homology, Amino Acid

Substances

  • Abrin

Associated data

  • GENBANK/M98344
  • GENBANK/M98345
  • GENBANK/M98346