| Literature DB >> 18314941 |
Yannick Pauchet1, Alexander Muck, Ales Svatos, David G Heckel, Susanne Preiss.
Abstract
The gut lumen is the primary site of digestion and detoxification and thus presents conditions hostile to most proteins. We used 2D-gel electrophoresis and MS/MS de novo peptide sequencing to identify the major proteins stable enough to persist in the midgut lumen of caterpillars of the cotton bollworm Helicoverpa armigera, a generalist herbivorous insect and a major crop pest worldwide. As expected, we found several enzymes responsible for digestion of carbohydrates, proteins, and lipids. In addition, we identified nondigestive proteins such as a multidomain lipocalin, a protein with pathogen recognition domains, an arginine kinase related to a class of major human allergens, and abundant proteins of unknown function. Identification of the set of proteins that are secreted into the lumen will enable us to further characterize the nutritional and defensive functions of this important intraorganismal space.Entities:
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Year: 2008 PMID: 18314941 DOI: 10.1021/pr7006208
Source DB: PubMed Journal: J Proteome Res ISSN: 1535-3893 Impact factor: 4.466