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Resistance to a Bacterial Toxin Is Mediated by Removal of a Conserved Glycosylation Pathway Required for
 

Summary: Resistance to a Bacterial Toxin Is Mediated by Removal of a
Conserved Glycosylation Pathway Required for
Toxin-Host Interactions*
Received for publication, July 25, 2003, and in revised form, August 22, 2003
Published, JBC Papers in Press, August 27, 2003, DOI 10.1074/jbc.M308142200
Joel S. Griffitts, Danielle L. Huffman, Johanna L. Whitacre, Brad D. Barrows,
Lisa D. Marroquin, Reto Mu¨ ller§, Jillian R. Brown¶, Thierry Hennet§, Jeffrey D. Esko¶,
and Raffi V. Aroian
From the Section of Cell and Developmental Biology, University of California, San Diego,
La Jolla, California 92093, §Institute of Physiology, University of Zu¨rich, Winterhurerstrasse 190,
8057 Zu¨rich, Switzerland, and ¶Department of Cellular and Molecular Medicine, Glycobiology Research
and Training Center, University of California, San Diego, La Jolla, California 92093
Crystal (Cry) proteins made by the bacterium Bacillus
thuringiensis are pore-forming toxins that specifically
target insects and nematodes and are used around the
world to kill insect pests. To better understand how
pore-forming toxins interact with their host, we have
screened for Caenorhabditis elegans mutants that resist
Cry protein intoxication. We find that Cry toxin resist-
ance involves the loss of two glycosyltransferase genes,

  

Source: Aroian, Raffi V. - Division of Biological Sciences, University of California at San Diego

 

Collections: Biology and Medicine