title: Salivary proteins of plant-feeding hemipteroids - implication in phytophagy.
abstract: Many hemipteroids are major pests and vectors of microbial pathogens, infecting crops. Saliva of the hemipteroids is critical in enabling them to be voracious feeders on plants, including the economically important ones. A plethora of hemipteroid salivary enzymes is known to inflict stress in plants, either by degrading the plant tissue or by affecting their normal metabolism. Hemipteroids utilize one of the following three strategies of feeding behaviour: salivary sheath feeding, osmotic-pump feeding and cell-rupture feeding. The last strategy also includes several different tactics such as lacerate-and-flush, lacerate-and-sip and macerate-and-flush. Understanding hemipteroid feeding mechanisms is critical, since feeding behaviour directs salivary composition. Saliva of the Heteroptera that are specialized as fruit and seed feeders, includes cell-degrading enzymes, auchenorrhynchan salivary composition also predominantly consists of cell-degrading enzymes such as amylase and protease, whereas that of the Sternorhyncha includes a variety of allelochemical-detoxifying enzymes. Little is known about the salivary composition of the Thysanoptera. Cell-degrading proteins such as amylase, pectinase, cellulase and pectinesterase enable stylet entry into the plant tissue. In contrast, enzymes such as glutathione peroxidase, laccase and trehalase detoxify plant chemicals, enabling the circumvention of plant-defence mechanisms. Salivary enzymes such as M1-zinc metalloprotease and CLIP-domain serine protease as in Acyrthosiphon pisum (Aphididae), and non-enzymatic proteins such as apolipophorin, ficolin-3-like protein and 'lava-lamp' protein as in Diuraphis noxia (Aphididae) have the capacity to alter host-plant-defence mechanisms. A majority of the hemipteroids feed on phloem, hence Ca++-binding proteins such as C002 protein, calreticulin-like isoform 1 and calmodulin (critical for preventing sieve-plate occlusion) are increasingly being recognized in hemipteroid-plant interactions. Determination of a staggering variety of proteins shows the complexity of hemipteroid saliva: effector proteins localized in hemipteran saliva suggest a similarity to the physiology of pathogen-plant interactions.
authors.affiliation: School of Agricultural & Wine Sciences, Charles Sturt University, PO Box 883, Orange, NSW 2800, Australia.
authors.forename: A
authors.initials: A
authors.lastname: Sharma
authors.affiliation: School of Agricultural & Wine Sciences, Charles Sturt University, PO Box 883, Orange, NSW 2800, Australia.
authors.forename: A N
authors.initials: AN
authors.lastname: Khan
authors.affiliation: School of Agricultural & Wine Sciences, Charles Sturt University, PO Box 883, Orange, NSW 2800, Australia.
authors.forename: S
authors.initials: S
authors.lastname: Subrahmanyam
authors.affiliation: School of Agricultural & Wine Sciences, Charles Sturt University, PO Box 883, Orange, NSW 2800, Australia.
authors.forename: A
authors.initials: A
authors.lastname: Raman
authors.affiliation: Australian Centre for Evolutionary Biology and Biodiversity, and School of Earth and Environmental Sciences, University of Adelaide, SA 5005, Australia.
authors.forename: G S
authors.initials: GS
authors.lastname: Taylor
authors.affiliation: Orange Agricultural Institute, NSW Department of Primary Industries, Forest Road, Orange, NSW 2800, Australia.
authors.forename: M J
authors.initials: MJ
authors.lastname: Fletcher
mesh_terms: D000818:Animals; D005247:Feeding Behavior; D006430:Hemiptera / Q000201:enzymology*; D012471:Salivary Proteins and Peptides / Q000378:metabolism*
chemical_list: D012471:Salivary Proteins and Peptides