Morphology and Proteome Characterization of the Salivary Glands of the Western Chinch Bug (Hemiptera: Blissidae)

• Published in: Journal of economic entomology 2015-08, Vol.108 (4), p.2055-2064
• Main Authors: Ramm, Crystal, Wayadande, Astri, Baird, Lisa, Nandakumar, Renu, Madayiputhiya, Nandakumar, Amundsen, Keenan, Donze-Reiner, Teresa, Baxendale, Frederick, Sarath, Gautam, Heng-Moss, Tiffany
• Format: Article
• Language: English
• Subjects: Accessory gland; Acyrthosiphon pisum; Amino acid sequence; amino acid sequences; Animals; Batrisodes occiduus; Blissidae; Blissus occiduus; Bouteloua dactyloides; cell structures; Cellular structure; Chemical damage; chinch bug; Feeding; Feeding behavior; Hemiptera; Heteroptera - cytology; Heteroptera - genetics; Heteroptera - ultrastructure; Hydrolase; Insect Proteins - genetics; insects; Liquid chromatography; Mass spectrometry; Mass spectroscopy; Microscopy; Microscopy, Electron, Scanning; Molecular Sequence Data; Morphology; Nucleotide sequence; Peroxidase; pests; PLANT RESISTANCE; proteins; Proteome; Proteomes; Reductase; Reductases; Salivary gland; Salivary glands; Salivary Glands - cytology; Salivary Glands - ultrastructure; salivary proteome; Scanning electron microscopy; Sequences; Structure-function relationships; tandem mass spectrometry
• ISSN: 0022-0493; 1938-291X
• DOI: 10.1093/jee/tov149

The western chinch bug, Blissus occiduus Barber, is a serious pest of buffalograss, Buchloe dactyloides (Nuttall) due to physical and chemical damage caused during the feeding process. Although previous work has investigated the feeding behaviors of chinch bugs in the Blissus complex, no study to date has explored salivary gland morphology and the associated salivary complex of this insect. Whole and sectioned B. occiduus salivary glands were visualized using light and scanning electron microscopy to determine overall structure and cell types of the salivary glands and their individual lobes. Microscopy revealed a pair of trilobed principal glands and a pair of tubular accessory glands of differing cellular types. To link structure with function, the salivary gland proteome was characterized using liquid chromatography tandem mass spectrometry. The salivary proteome analysis resulted in B. occiduus sequences matching 228 nonhomologous protein sequences of the pea aphid, Acyrthosiphon pisum (Harris), with many specific to the proteins present in the salivary proteome of A. pisum. A number of sequences were assigned the molecular function of hydrolase and oxido-reductase activity, with one specific protein sequence revealing a peroxidase-like function. This is the first study to characterize the salivary proteome of B. occiduus and the first of any species in the family Blissidae.