title: Mapping the larval midgut lumen proteome of Helicoverpa armigera, a generalist herbivorous insect.
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.
authors.affiliation: Department of Entomology and Mass Spectrometry Research Group, Max Planck Institute for Chemical Ecology, Hans-Knöll-Str. 8, D-07745 Jena, Germany.
authors.forename: Yannick
authors.initials: Y
authors.lastname: Pauchet
authors.forename: Alexander
authors.initials: A
authors.lastname: Muck
authors.forename: Ales
authors.initials: A
authors.lastname: Svatos
authors.forename: David G
authors.initials: DG
authors.lastname: Heckel
authors.forename: Susanne
authors.initials: S
authors.lastname: Preiss
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001122:Arginine Kinase / Q000032:analysis / Q000235:genetics; D002352:Carrier Proteins / Q000032:analysis / Q000235:genetics; D004064:Digestive System / Q000378:metabolism*; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods; D006867:Hydrolases / Q000032:analysis / Q000235:genetics; D019476:Insect Proteins / Q000032:analysis* / Q000235:genetics; D007814:Larva / Q000235:genetics / Q000378:metabolism; D007915:Lepidoptera / Q000235:genetics / Q000378:metabolism*; D054834:Lipocalins / Q000032:analysis / Q000235:genetics; D008969:Molecular Sequence Data; D010449:Peptide Mapping / Q000379:methods; D020543:Proteome / Q000032:analysis* / Q000235:genetics; D040901:Proteomics / Q000379:methods; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods; D053719:Tandem Mass Spectrometry / Q000379:methods
chemical_list: D002352:Carrier Proteins; D019476:Insect Proteins; D054834:Lipocalins; D020543:Proteome; C405332:beta-1,3-glucan recognition protein, insect; D001122:Arginine Kinase; D006867:Hydrolases