Primary structure of hemolytic lectin CEL-III from marine invertebrate Cucumaria echinata and its cDNA: Structural similarity to the B-chain from plant lectin, ricin

Masahiro Nakano, Satoshi Tabata, Ken Sugihara, Yoshiaki Kouzuma, Makoto Kimura, Nobuyuki Yamasaki

Research output: Contribution to journalArticle

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Abstract

CEL-III, a galactose/N-acetylgalactosamine (Gal/GalNAc) specific lectin purified from a marine invertebrate Cucumaria echinata has a strong hemolytic activity especially toward human and rabbit erythrocytes. We determined the primary structure of the CEL-III by examining the amino acid sequences of the protein and the nucleotide sequence of the cDNA. The cDNA encoding CEL-III has 1823 nucleotides and an open reading frame of 1296 nucleotides. CEL-III is composed of 432 amino acid residues with a M(r) of 47 457 and has six internal tandem repeats, each with of 40-50 amino acids, comprising the N- terminal two-thirds of the molecule. Similar repeats are found in the B- chains of cytotoxic plant lectins, such as ricin and abrin, where six repetitive sequences extend throughout the molecules. A hydropathy plot predicts hydrophobic segments in the C-terminal region of CEL-III. These findings suggest that the N-terminal region of CEL-III plays an important role in binding to carbohydrate receptors on the target cell membranes, an event which triggers an intermolecular hydrophobic interaction of the C- terminal region, the result being oligomerization of CEL-III to lead to pore- formation in erythrocyte membrane.

Original languageEnglish
Pages (from-to)167-176
Number of pages10
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume1435
Issue number1-2
DOIs
Publication statusPublished - Nov 16 1999

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Cucumaria
Plant Lectins
Ricin
Invertebrates
Abrin
Nucleotides
Complementary DNA
Acetylgalactosamine
Amino Acids
Tandem Repeat Sequences
Nucleic Acid Repetitive Sequences
Erythrocyte Membrane
Galactose
Hydrophobic and Hydrophilic Interactions
Lectins
Open Reading Frames
Amino Acid Sequence
Oligomerization
Molecules
Erythrocytes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Structural Biology
  • Biophysics

Cite this

Primary structure of hemolytic lectin CEL-III from marine invertebrate Cucumaria echinata and its cDNA : Structural similarity to the B-chain from plant lectin, ricin. / Nakano, Masahiro; Tabata, Satoshi; Sugihara, Ken; Kouzuma, Yoshiaki; Kimura, Makoto; Yamasaki, Nobuyuki.

In: Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, Vol. 1435, No. 1-2, 16.11.1999, p. 167-176.

Research output: Contribution to journalArticle

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