Studies on enzymes in the salivary glands of Lygus rugulipennis (Hemiptera, miridae)

Laurema, Seppo; Varis, Anna-Liisa; Miettinen, Harri

doi:10.1016/0020-1790(85)90010-1

Cited by 63 publications

(33 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Our analyses confirm the presence of PGs in L. rugulipennis (Laurema et al, 1985;D'Ovidio et al, 2004) andA. lineolatus (D'Ovidio et al, 2004) (L.) and C. norwegicus.…”

Section: Discussionsupporting

confidence: 85%

“…These enzymes are associated with feeding in both piercing-sucking (Adams & McAllan, 1956;Laurema & Nuorteva, 1961;Strong & Kruitwagen, 1968;Strong, 1970;Miles, 1972;Laurema et al, 1985;Ma et al, 1990;Agblor et al, 1994;Cohen & Wheeler, 1998;Miles, 1999;Agusti & Cohen, 2000;Cherqui & Tjallingii, 2000;Boyd et al, 2002;Shen et al, 2003;D'Ovidio et al, 2004;Shackel et al, 2005) and chewing species (Shen et al, 1996;Doostdar et al, 1997;Girard & Jouanin, 1999;Shen et al, 2003), and appear to play an important role in insect-plant interactions. PGs are present in species belonging to different insect taxa, but especially common in mirid bugs (Heteroptera: Miridae) (Laurema & Nuorteva, 1961;Strong & Kruitwagen, 1968;Strong, 1970;Laurema et al, 1985;Agblor et al, 1994;Agusti & Cohen, 2000;Boyd et al, 2002;D'Ovidio et al, 2004;Shackel et al, 2005;reviewed by Wheeler, 2001). In nematodes, an exo-PG was cloned from the plant parasitic nematode Meloidogyne incognita (Kofoid & White) (Jaubert et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Activity of endo-polygalacturonases in mirid bugs (Heteroptera: Miridae) and their inhibition by plant cell wall proteins (PGIPs)

Frati¹,

Galletti²,

Lorenzo³

et al. 2006

Eur. J. Entomol.

View full text Add to dashboard Cite

Abstract. Endo-polygalacturonases (PGs) are hydrolytic enzymes involved in the degradation of pectin, one of the major components of plant cell wall. While PGs from fungi, bacteria and plants have been extensively studied, PGs from insects are much less known, although they are likely to play an important role in insect-plant interactions. Presence of PGs has been reported for both piercing-sucking and chewing insect species, and possibly more commonly in mirid bugs (Heteroptera: Miridae). A screening of some common mirid species and other insects, belonging to different orders and families, was conducted using agarose diffusion assays run at different pHs. All the mirid species tested [Lygus rugulipennis Popp., L. pratensis (L.), Orthops kalmi (L.), Adelphocoris lineolatus (Goeze) and Closterotomus norwegicus (Gmelin)] showed PG activity, mainly at pH 7-8, whereas no activity was recorded for the other insect species, except Sitophilus sp. (Coleoptera: Curculionidae). PG activity in females of L. pratensis was significantly higher than in males, whereas there were no differences between the sexes in the other species. In all these species, PGs were present both in the salivary glands and the gut, with a higher activity in the salivary glands, confirming the role of these enzymes in the feeding behaviour of mirid bugs. Inhibition of mirid PGs by polygalacturonase-inhibiting proteins (PGIPs) from different plant sources was analysed at pH 7. PGIPs are extracellular plant proteins known for their ability to inhibit fungal PGs and restrict fungal colonization. Two PGIPs from Phaseolus vulgaris (PvPGIP3 and PvPGIP4) inhibited PGs of all the mirid bugs tested. This information may be helpful for the development of innovative insect-resistant plant varieties, for use in low-impact IPM.

show abstract

“…Our analyses confirm the presence of PGs in L. rugulipennis (Laurema et al, 1985;D'Ovidio et al, 2004) andA. lineolatus (D'Ovidio et al, 2004) (L.) and C. norwegicus.…”

Section: Discussionsupporting

confidence: 85%

Section: Introductionmentioning

confidence: 99%

Activity of endo-polygalacturonases in mirid bugs (Heteroptera: Miridae) and their inhibition by plant cell wall proteins (PGIPs)

Frati¹,

Galletti²,

Lorenzo³

et al. 2006

Eur. J. Entomol.

View full text Add to dashboard Cite

show abstract

“…Orius, Nabis, etc). Salivary lipases and phospholipases are found in both infraorders, but hyaluronidases have been reported only in the saliva of cimicomorphs (Edwards, 1961;Laurema et al, 1985;Cohen, 1998b). Dissections of prey 15-30 min after feeding provide visual evidence of differences in the relative digestive ability of cimicomorphan and pentatomomorphan saliva.…”

Section: Hemipteran Salivary Enzymes and Handling Timementioning

confidence: 99%

“…On the other hand, transgenic plants may impose a problem in the future for predatory hemipterans that switch between animals and plants (Ashouri et al, 1998;Bell et al, 2003). Pectinase is a distinguishing enzyme for phytophagy showing that species secreting this enzyme are very well equipped for macromolecular destruction of plant cells via the salivary apparatus (Laurema et al, 1985;Agusti and Cohen, 2000;Hori, 2000). In contrast, the presence of amylase activity in the salivary glands of zoophages is suggestive of their ability to feed on plant and acquires nutrients if necessary.…”

Section: Implications Conclusion and Future Needsmentioning

confidence: 99%

Zoophytophagy in predatory Hemiptera

Torres

Boyd²

2009

Braz. arch. biol. technol.

View full text Add to dashboard Cite

show abstract

“…Predators such as Zelus renardii (Reduviidae) have high levels of proteolytic activity in the salivary glands as well as in the entire midgut (Cohen, 1993). Salivary protease activity was detected in the mirids Lygus rugulipennis (Miridae) (Laurema et al, 1985) and Creontiades dilutus (Miridae) (Colebatch et al, 2001). In Zelus renardii and both Lygus hesperus and Lygus lineolaris (Miridae), salivary gland protease activity is predominantly trypsin-like (Cohen, 1993;Agusti and Cohen, 2000), but in Creontiades dilutus, chymotrypsin-like pro-tease activity appears to predominate in the salivary glands (Colebatch et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Molecular Cloning, Gene Structure, Expression, and Enzyme Activity of a Serine Protease from Water Scorpion, Laccotrephes japonensis (Hemiptera: Nepidae)

Park¹,

Choi²,

Nam³

et al. 2012

International Journal of Industrial Entomology

View full text Add to dashboard Cite

Serine proteases are major insect enzymes involved in the digestion of dietary proteins and in the process of blood meal digestion. In this study, cDNA was constructed using the whole body of Laccotrephes japonensis. The flanking sequences of the 5-and 3-end of this gene were characterized by RACE-PCR. Sequence analysis showed that this gene contained a 963-bp ORF encoding 320 amino acids. The deduced amino acid sequence showed 62% identity with the Creontiades dilutus serine protease, 58% with the Lygus lineolaris trypsin precursor, and 54% with the Triatoma infestans salivary trypsin. To assess the expression of the L. japonensis serine protease (JGsp), the JGsp gene was cloned into a baculovirus transfer vector, pBac-1, and expressed in Sf9 cells (Spodoptera frugiperda). SDS-PAGE and western blot analysis have shown that the JGsp recombinant protein was a monomer with a molecular weight of about 32 kDa. Recombinant JGsp has shown activity in the protease enzyme assay using gelatin as a substrate.

show abstract

Studies on enzymes in the salivary glands of Lygus rugulipennis (Hemiptera, miridae)

Cited by 63 publications

References 42 publications

Activity of endo-polygalacturonases in mirid bugs (Heteroptera: Miridae) and their inhibition by plant cell wall proteins (PGIPs)

Activity of endo-polygalacturonases in mirid bugs (Heteroptera: Miridae) and their inhibition by plant cell wall proteins (PGIPs)

Zoophytophagy in predatory Hemiptera

Molecular Cloning, Gene Structure, Expression, and Enzyme Activity of a Serine Protease from Water Scorpion, Laccotrephes japonensis (Hemiptera: Nepidae)

Contact Info

Product

Resources

About