Mannose-specific lectin activity of parasporal proteins from a lepidoptera-specific bacillus thuringiensis strain

Naoya Wasano, Akira Ohgushi, Michio Ohba

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)

Abstract

Lectin activity, agglutinating sheep erythrocytes, was associated with parasporal inclusion proteins from a Lepidoptera-specific isolate of Bacillus thuringiensis serovar galleriae (H5ab). The activity was generated when parasporal inclusions were solubilized in an alkaline condition. Proteolytic processing was not required for generation of the lectin activity; the activity level was not affected by the presence/absence of the three proteases (trypsin, chymotrypsin, and proteinase K). SDS-PAGE analysis revealed that (1) alkali -solubilized parasporal inclusion proteins consisted of two major components of 130 kDa and 65 kDa, and (2) proteinase K treatment of alkali-solubilized proteins yielded a single major protein of 60 kDa. Lectin activity of our isolate was strongly inhibited by preincubation with D-mannose, but not with the six other monosaccharides: D-galactose, D-glucose, L-fucose, N-acetyl-D-glucosamine, N-acetyl-D-galactosamine, and N-acetylneuraminic acid. In contrast, D-mannose did not inhibit the in vivo larvicidal activity of the proteins against the silkworm, Bombyx mori.

Original languageEnglish
Pages (from-to)43-46
Number of pages4
JournalCurrent Microbiology
Volume46
Issue number1
DOIs
Publication statusPublished - Jan 2003

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Applied Microbiology and Biotechnology

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