title: Protein N-glycosylation and N-glycan trimming are required for postembryonic development of the pest beetle Tribolium castaneum.
abstract: In holometabolous insects the transition from larva to adult requires a complete body reorganization and relies on N-glycosylated proteins. N-glycosylation is an important posttranslational modification that influences protein activity but its impact on the metamorphosis has not been studied yet. Here we used the red flour beetle, Tribolium castaneum, to perform a first comprehensive study on the involvement of the protein N-glycosylation pathway in metamorphosis. The transcript levels for genes encoding N-glycan processing enzymes increased during later developmental stages and, in turn, transition from larva to adult coincided with an enrichment of more extensively modified paucimannose glycans, including fucosylated ones. Blockage of N-glycan attachment resulted in larval mortality, while RNAi of α-glucosidases involved in early N-glycan trimming and quality control disrupted the larva to pupa transition. Additionally, simultaneous knockdown of multiple genes responsible for N-glycan processing towards paucimannose structures revealed their novel roles in pupal appendage formation and adult eclosion. Our findings revealed that, next to hormonal control, insect post-embryonic development and metamorphosis depend on protein N-glycan attachment and efficient N-glycan processing. Consequently, disruption of these processes could be an effective new approach for insect control.
authors.affiliation: Laboratory of Agrozoology, Department of Crop Protection, Faculty of Bioscience Engineering, Ghent University, Ghent, Belgium.|Laboratory of Biochemistry and Glycobiology, Department of Molecular Biotechnology, Faculty of Bioscience Engineering, Ghent University, Ghent, Belgium.
authors.forename: Tomasz
authors.initials: T
authors.lastname: Walski
authors.affiliation: Laboratory of Biochemistry and Glycobiology, Department of Molecular Biotechnology, Faculty of Bioscience Engineering, Ghent University, Ghent, Belgium.
authors.forename: Els J M
authors.initials: EJ
authors.lastname: Van Damme
authors.affiliation: Mass Spectrometry Laboratory, GIGA-Research, University of Liege, Liege, Belgium.
authors.forename: Nicolas
authors.initials: N
authors.lastname: Smargiasso
authors.affiliation: Laboratory of Agrozoology, Department of Crop Protection, Faculty of Bioscience Engineering, Ghent University, Ghent, Belgium.
authors.forename: Olivier
authors.initials: O
authors.lastname: Christiaens
authors.affiliation: Mass Spectrometry Laboratory, GIGA-Research, University of Liege, Liege, Belgium.
authors.forename: Edwin
authors.initials: E
authors.lastname: De Pauw
authors.affiliation: Laboratory of Agrozoology, Department of Crop Protection, Faculty of Bioscience Engineering, Ghent University, Ghent, Belgium.
authors.forename: Guy
authors.initials: G
authors.lastname: Smagghe
mesh_terms: D000818:Animals; D002240:Carbohydrate Sequence; D029721:Drosophila Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D004331:Drosophila melanogaster / Q000235:genetics / Q000254:growth & development / Q000378:metabolism; D018507:Gene Expression Regulation, Developmental; D055785:Gene Knockdown Techniques; D017344:Genes, Insect; D006023:Glycoproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006031:Glycosylation; D019476:Insect Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008675:Metamorphosis, Biological / Q000235:genetics / Q000502:physiology; D010802:Phylogeny; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D034622:RNA Interference; D014231:Tribolium / Q000235:genetics / Q000254:growth & development* / Q000378:metabolism*
chemical_list: D029721:Drosophila Proteins; D006023:Glycoproteins; D019476:Insect Proteins; D011134:Polysaccharides