Mapping the Larval Midgut Lumen Proteome of Helicoverpa armigera, a Generalist Herbivorous Insect

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 bollw...

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Bibliographic Details
Published in:Journal of proteome research 2008-04, Vol.7 (4), p.1629-1639
Main Authors: Pauchet, Yannick, Muck, Alexander, Svatoš, Aleš, Heckel, David G, Preiss, Susanne
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Arginine Kinase - analysis
Arginine Kinase - genetics
Carrier Proteins - analysis
Carrier Proteins - genetics
Digestive System - metabolism
Electrophoresis, Gel, Two-Dimensional - methods
Hydrolases - analysis
Hydrolases - genetics
Insect Proteins - analysis
Insect Proteins - genetics
Larva - genetics
Larva - metabolism
Lepidoptera - genetics
Lepidoptera - metabolism
Lipocalins - analysis
Lipocalins - genetics
Molecular Sequence Data
Peptide Mapping - methods
Proteome - analysis
Proteome - genetics
Proteomics - methods
Sequence Alignment
Sequence Homology, Amino Acid
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods
Tandem Mass Spectrometry - methods
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Summary: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.
ISSN:1535-3893
1535-3907
DOI:10.1021/pr7006208