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Appl Environ Microbiol. 1993 August; 59(8): 2666-2672
Copyright © 1993, American Society for Microbiology. All Rights Reserved.

Nonenzymatic Glycosylation of Lepidopteran-Active Bacillus thuringiensis Protein Crystals

Meenakshi Bhattacharya, Bradley A. Plantz, Jane D. Swanson-Kobler{dagger} and Kenneth W. Nickerson*

School of Biological Sciences, University of Nebraska, Lincoln, Nebraska 68588-0343

ABSTRACT

We used high-pH anion-exchange chromatography with pulsed amperometric detection to quantify the monosaccharides covalently attached to Bacillus thuringiensis HD-1 (Dipel) crystals. The crystals contained 0.54% sugars, including, in decreasing order of prevalence, glucose, fucose, arabinose/rhamnose, galactose, galactosamine, glucosamine, xylose, and mannose. Three lines of evidence indicated that these sugars arose from nonenzymatic glycosylation: (i) the sugars could not be removed by N- or O-glycanases; (ii) the sugars attached were influenced both by the medium in which the bacteria had been grown and by the time at which the crystals were harvested; and (iii) the chemical identity and stoichiometry of the sugars detected did not fit any known glycoprotein models. Thus, the sugars detected were the product of fermentation conditions rather than bacterial genetics. The implications of these findings are discussed in terms of crystal chemistry, fermentation technology, and the efficacy of B. thuringiensis as a microbial insecticide.

FOOTNOTES

* Corresponding author.

{dagger} Present address: U.S. Army Corps of Engineers, Missouri River Division, Omaha, NE 68144.

Appl Environ Microbiol. 1993 August; 59(8): 2666-2672
Copyright © 1993, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Mironova, R., Niwa, T., Dimitrova, R., Boyanova, M., Ivanov, I. (2003). Glycation and Post-translational Processing of Human Interferon-{gamma} Expressed in Escherichia coli. J. Biol. Chem. 278: 51068-51074 [Abstract] [Full Text]  


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