A proteomic analysis of salivary glands of femaleAnopheles gambiae mosquito

Kalume, Dário Eluan; Okulate, Mobolaji; Zhong, Jun; Reddy, Raghunath; Suresh, Shubha; Deshpande, Nandan P.; Kumar, Nirbhay; Pandey, Akhilesh

doi:10.1002/pmic.200401210

Cited by 67 publications

(46 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Differences between the identified proteins obtained from different preparative samples are often reported, e.g. [24], highlighting the importance of adopting multiple approaches to characterise and identify novel sets of proteins, as used here. The failure to match MS/ MS reads against proteins deposited in the NCBI nr database indicates that the proteins reported during this study were of aphid origin and were not derived from microbial contamination.…”

Section: Discussionmentioning

confidence: 99%

The secreted salivary proteome of the pea aphid Acyrthosiphon pisum characterised by mass spectrometry

et al. 2009

View full text Add to dashboard Cite

Nine proteins secreted in the saliva of the pea aphid Acyrthosiphon pisum were identified by a proteomics approach using GE-LC-MS/MS and LC-MS/MS, with reference to EST and genomic sequence data for A. pisum. Four proteins were identified by their sequences: a homolog of angiotensin-converting enzyme (an M2 metalloprotease), an M1 zinc-dependant metalloprotease, a glucose-methanol-choline (GMC)-oxidoreductase and a homolog to regucalcin (also known as senescence marker protein 30). The other five proteins are not homologous to any previously described sequence and included an abundant salivary protein (represented by ACYPI009881), with a predicted length of 1161 amino acids and high serine, tyrosine and cysteine content. A. pisum feeds on plant phloem sap and the metalloproteases and regucalcin (a putative calcium-binding protein) are predicted determinants of sustained feeding, by inactivation of plant protein defences and inhibition of calcium-mediated occlusion of phloem sieve elements, respectively. The amino acid composition of ACYPI009881 suggests a role in the aphid salivary sheath that protects the aphid mouthparts from plant defences, and the oxidoreductase may promote gelling of the sheath protein or mediate oxidative detoxification of plant allelochemicals. Further salivary proteins are expected to be identified as more sensitive MS technologies are developed.

show abstract

Section: Discussionmentioning

confidence: 99%

The secreted salivary proteome of the pea aphid Acyrthosiphon pisum characterised by mass spectrometry

et al. 2009

View full text Add to dashboard Cite

show abstract

“…Among these housekeeping proteins, protein disulfide isomerase, Hsp70, tubulin b-chain, calreticulin, ATP synthase b-subunit, enolase, ribosomal protein, arginine kinase and aldolase have been previously identified in the salivary glands of female individuals of the hematophagous insect species A. gambiae mosquito (Kalume et al, 2005) and of other hematophagous arthropods (Ribeiro et al, 2004(Ribeiro et al, , 2007Oleaga et al, 2007) by proteomic analysis. Further, the ribosomal protein, Hsp60, protein disulfide isomerase, ATP synthase b-subunit, ATP synthase D chain, ATP synthase d-chain, enolase, tubulin a-and b-chain, actin, myosin light chain, and porin have been identified in the salivary glands of a phytophagous gall midge, Mayetiola destructor (Chen et al, 2008).…”

Section: Discussionmentioning

confidence: 99%

Proteomic analysis of the salivary glands of the rice brown planthopper, Nilaparvata lugens (Stål) (Homoptera: Delphacidae)

Konishi

Noda

Tamura

et al. 2009

Appl. Entomol. Zool.

View full text Add to dashboard Cite

The rice brown planthopper, Nilaparvata lugens is a phloem-feeding insect pest of the rice plant Oryza sativa. To understand the role of saliva in its feeding process, we analyzed salivary gland proteins using two-dimensional polyacrylamide gel electrophoresis followed by Edman degradation of proteins. Of the 52 major spots analyzed, 25 N-terminal sequences were determined. The internal amino acid sequences of the remaining 27 proteins were determined by the Cleveland peptide mapping method. We identified 22 of the 25 proteins whose N-terminal regions were sequenced and 13 of the 27 proteins that were internally sequenced after searching them against the entries in the expressed sequence tag (EST) database of N. lugens. Through a homology search using public nonredundant protein databases, we identified EST-unmatched proteins. As a result, many housekeeping proteins responsible for energy metabolism, protein synthesis, folding and modification were identified, of which actins, tubulins, heat-shock proteins, protein disulfide isomerases and ATP synthases were in common with proteins identified from the salivary glands of hematophagous arthropods such as Anopheles gambiae, and a phytophagous gall midge Mayetiola destructor. However, we could not identify the glucosidases and phenoloxidases previously detected in the salivary glands of N. lugens. In contrast, novel proteins with an EF-hand domain were found in relatively high abundance in salivary gland homogenates derived from N. lugens; their corresponding ESTs were specifically derived from the salivary glands. Their calcium-binding properties suggest their importance of phloem feeding by the planthopper.

show abstract

“…A proteomic analysis of salivary glands from female A. gambiae mosquitoes was carried out [32]. Salivary gland extracts were hydrolyzed with trypsin using a 1-DE in-gel and an in solution digestion and analyzed by LC-MS/MS.…”

Section: Wwwintechopencommentioning

confidence: 99%