Kinetics of expression of the salivary apyrases in Triatoma infestans

Faudry, Eric; Rocha, Priscila S.; Vernet, Thierry; Lozzi, Silene P.; Teixeira, Antônio R. L.

doi:10.1016/j.ibmb.2004.06.016

Cited by 16 publications

(15 citation statements)

References 32 publications

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“…In the saliva of blood sucking arthropods, apyrases function to hydrolyze ADP in a Ca 2+ -dependent manner and inhibit ADP-induced platelet aggregation to facilitate blood feeding (Ribeiro and Francischetti, 2003; Faudry et al, 2004). Apyrases identified in sand fly saliva belong to the Cimex apyrase family (Valenzuela et al, 2001; Hamasaki et al, 2009).…”

Section: Resultsmentioning

confidence: 99%

Analysis of salivary gland transcripts of the sand fly Lutzomyia ayacuchensis, a vector of Andean-type cutaneous leishmaniasis

Kato¹,

Jochim²,

Gómez³

et al. 2013

Infection, Genetics and Evolution

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The saliva of blood sucking insects contains potent pharmacologically active components that assist them in counteracting the host hemostatic and inflammatory systems during blood feeding. In addition, sand fly salivary proteins affect host immunity and have the potential to be a vaccine against Leishmania infection. In the present study, the salivary gland transcripts of Lutzomyia ayacuchensis, a vector of cutaneous leishmaniasis in Ecuadorian and Peruvian Andes, were analyzed by sequencing randomly selected clones of the salivary gland cDNA library of this sand fly. This resulted in the identification of the most abundant transcripts coding for secreted proteins. These proteins were homologous to the salivary molecules present in other sand flies including the RGD-containing peptide, PpSP15/SL1 family protein, yellow-related protein, putative apyrase, antigen 5-related protein, D7 family protein, and 27 kDa salivary protein. Of note, homologues of maxadilan, an active vasodilator abundantly present in saliva of Lutzomyia longipalpis, were not identified. This analysis is the first description of salivary proteins from a sand fly of the subgenus Helcocyrtomyia and from vector of cutaneous leishmaniasis in the New World. The present analysis will provide further insights into the evolution of salivary components in blood sucking arthropods.

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Section: Resultsmentioning

confidence: 99%

Analysis of salivary gland transcripts of the sand fly Lutzomyia ayacuchensis, a vector of Andean-type cutaneous leishmaniasis

Kato¹,

Jochim²,

Gómez³

et al. 2013

Infection, Genetics and Evolution

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“…. Furthermore, Ti saliva would have a multigene apyrase family with at least three to five forms and N -glycosylation 62. In 2DE-based-proteomic analysis, five Ti apyrase forms displayed a typical pattern of isoforms for each form 19.…”

Section: Resultsmentioning

confidence: 99%

Insight into the Salivary Transcriptome and Proteome of Dipetalogaster maxima

et al. 2011

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Dipetalogaster maximais a blood-sucking Hemiptera that inhabits sylvatic areas in Mexico. It usually takes its blood meal from lizards, but following human population growth, it invaded suburban areas, feeding also on humans and domestic animals. Hematophagous insect salivary glands produce potent pharmacologic compounds that counteract host hemostasis, including anticlotting, antiplatelet, and vasodilatory molecules. To obtain further insight into the salivary biochemical and pharmacologic complexity of this insect, a cDNA library from its salivary glands was randomly sequenced. Salivary proteins were also submitted to one- and two-dimensional gel electrophoresis (1DE and 2DE) followed by mass spectrometry analysis. We present the analysis of a set of 2728 cDNA sequences, 1375 of which coded for proteins of a putative secretory nature. The saliva 2DE proteome displayed approximately 150 spots. The mass spectrometry analysis revealed mainly lipocalins, pallidipins, antigen 5-like proteins, and apyrases. The redundancy of sequence identification of saliva-secreted proteins suggests that proteins are present in multiple isoforms or derive from gene duplications. Supplemental files can be downloaded from http://exon.niaid.nih.gov/transcriptome/D_maxima/Dm-S1-web.xls and http://exon.niaid.nih.gov/transcriptome/D_maxima/Dm-S2-web.xls.

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“…The high expression of the PmSgP1‐encoding gene in salivary glands D1/D2 and the 7.5‐fold increase of the expression rate after blood ingestion indicate the importance of this enzyme in the saliva. The expression of an apyrase‐encoding gene was only increased about 3.5‐fold 24 h after feeding (Faudry et al ., 2004). The de novo protein synthesis is necessary because the triatomines inject relatively high volumes of saliva during blood ingestion.…”

Section: Discussionmentioning

confidence: 99%

“…In Tri. infestans about 50% of the pool of apyrase from the salivary glands is injected (Faudry et al ., 2004). In P. megistus a similar reduction seems to occur, because after feeding the volume of released saliva was reduced by about 45%.…”

Section: Discussionmentioning

confidence: 99%

A salivary serine protease of the haematophagous reduviid Panstrongylus megistus: sequence characterization, expression pattern and characterization of proteolytic activity

Meiser

Piechura

Meyer

et al. 2010

Insect Molecular Biology

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A cDNA encoding a trypsin-like protease from the salivary glands of the haematophagous reduviid Panstrongylus megistus was cloned and sequenced. The deduced protein sequence showed similarities to serine proteases of other hemipterans but with substitutions in the catalytic triad and the substrate binding site. The expression of the gene increased more than sixfold after feeding. Saliva showed the highest proteolytic activity at neutral to slightly basic pH. Substrate and inhibitor profiles and zymography indicated the presence of a trypsin-like protease with preference for Arg and Lys at P1. Using chromatography, a fibrinolytic enzyme was purified whose sequence was identified by tandem mass spectrometry as that encoded by the cDNA.

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Kinetics of expression of the salivary apyrases in Triatoma infestans

Cited by 16 publications

References 32 publications

Analysis of salivary gland transcripts of the sand fly Lutzomyia ayacuchensis, a vector of Andean-type cutaneous leishmaniasis

Analysis of salivary gland transcripts of the sand fly Lutzomyia ayacuchensis, a vector of Andean-type cutaneous leishmaniasis

Insight into the Salivary Transcriptome and Proteome of Dipetalogaster maxima

A salivary serine protease of the haematophagous reduviid Panstrongylus megistus: sequence characterization, expression pattern and characterization of proteolytic activity

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