Diversity in Protein Glycosylation among Insect Species

Abstract

BackgroundA very common protein modification in multicellular organisms is protein glycosylation or the addition of carbohydrate structures to the peptide backbone. Although the Class of the Insecta is the largest animal taxon on Earth, almost all information concerning glycosylation in insects is derived from studies with only one species, namely the fruit fly Drosophila melanogaster.Methodology/Principal FindingsIn this report, the differences in glycoproteomes between insects belonging to several economically important insect orders were studied. Using GNA (Galanthus nivalis agglutinin) affinity chromatography, different sets of glycoproteins with mannosyl-containing glycan structures were purified from the flour beetle (Tribolium castaneum), the silkworm (Bombyx mori), the honeybee (Apis mellifera), the fruit fly (D. melanogaster) and the pea aphid (Acyrthosiphon pisum). To identify and characterize the purified glycoproteins, LC-MS/MS analysis was performed. For all insect species, it was demonstrated that glycoproteins were related to a broad range of biological processes and molecular functions. Moreover, the majority of glycoproteins retained on the GNA column were unique to one particular insect species and only a few glycoproteins were present in the five different glycoprotein sets. Furthermore, these data support the hypothesis that insect glycoproteins can be decorated with mannosylated O-glycans.Conclusions/SignificanceThe results presented here demonstrate that oligomannose N-glycosylation events are highly specific depending on the insect species. In addition, we also demonstrated that protein O-mannosylation in insect species may occur more frequently than currently believed.

Noctilisin, a Venom Glycopeptide of <I>Sirex noctilio</I> (Hymenoptera: Siricidae), Causes Needle Wilt and Defense Gene Responses in Pines

“…However, in specific mammalian cell types or disease-states, including cancer, this extension process may be lacking or blocked, leaving naked Tn-antigen structures that can serve as easily detected immunological markers (Ju and Cummings 2005). The structural information collected for noctilisin suggests that commercially available reagents for histochemical detection of Tn-antigen may prove useful for future studies of noctilisin mobility and localization in trees, particularly because plants do not produce Tn-antigen structures that might interfere with immunodetection (Vandenborre et al 2011b, Yang et al 2012). …”

A bifunctional α-amylase/trypsin inhibitor from pigeonpea seeds: Purification, biochemical characterization and its bio-efficacy against Helicoverpa armigera

“…A lipid transfer protein from coffee seed is demonstrated to have direct action on intestinal tissues of insect along with α-AI activity[34].The glycan binding activity is evident in PPA[32]. It is also reported in some insect amylases such as A. pisum, A. mellifera, B. mori and T. castaneum along with some proteins which are involved in the number of biological processes and molecular functions[35].…”

Role in Diuresis of a Calcitonin Receptor (GPRCAL1) Expressed in a Distal-Proximal Gradient in Renal Organs of the Mosquito Aedes aegypti (L.)

“…Thus, either the receptor runs as a 51 kDa band or the ∼4 kDa mass difference may result from either post-translational modifications at predicted phosphorylation sites or O-linked glycosylation at Ser/Thr residues (Fig. S1) [37], [40]. The presence of glycosylated and unglycosylated receptor forms in the MT suggests that the subpopulation of glycosylated receptors is structurally suitable for functional interaction with yet unknown proteins analogous to mammalian RAMPs, and that glycosylation may regulate receptor activation.…”