A transient increase in total head phosphotyrosine levels is observed upon the emergence of Aedes aegypti from the pupal stage

Jablonka, Willy; Senna, Raquel; Nahu, Thaisa; Ventura, Guilherme; Menezes, Lidiane; Silva-Neto, Mário A.C.

doi:10.1590/s0074-02762011000500005

Cited by 5 publications

(6 citation statements)

References 32 publications

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“…In contrast, AAEL005492 had very low concentration in all tissues. Curiously, AAEL008528 is significantly expressed in the mosquito head, concomitant with a transient increase in phosphotyrosine phosphorylation that may involve fluctuations in the expression levels of AAEL008528 [24]. AAEL008528 is orthologous to Drosophila corkscrew, a PTP that was discovered in mutations related to defects in embryonic development [25], [26].…”

Section: Resultsmentioning

confidence: 99%

“…To ensure that our observations can be interpreted as the enzymatic behavior of PTPs, appropriate controls were performed including enzyme activity initially using pNPP, a generic substrate for phosphatases [24], [39]–[46]. Assays were performed in the presence or absence of micromolar levels of orthovanadate, a classical PTP inhibitor.…”

Section: Discussionmentioning

confidence: 99%

“…In some experiments, we included 0.1 mM of PTP 1B substrate II (Glu-Leu-Glu-Phe-pTyr-Met-Asp-Tyr-Asp-Tyr-Glu) (Calbiochem) in addition to pNPP. Further conditions were as described previously [24], [49].…”

Section: Methodsmentioning

confidence: 99%

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Molecular Analysis of Aedes aegypti Classical Protein Tyrosine Phosphatases Uncovers an Ortholog of Mammalian PTP-1B Implicated in the Control of Egg Production in Mosquitoes

et al. 2014

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BackgroundProtein Tyrosine Phosphatases (PTPs) are enzymes that catalyze phosphotyrosine dephosphorylation and modulate cell differentiation, growth and metabolism. In mammals, PTPs play a key role in the modulation of canonical pathways involved in metabolism and immunity. PTP1B is the prototype member of classical PTPs and a major target for treating human diseases, such as cancer, obesity and diabetes. These signaling enzymes are, hence, targets of a wide array of inhibitors. Anautogenous mosquitoes rely on blood meals to lay eggs and are vectors of the most prevalent human diseases. Identifying the mosquito ortholog of PTP1B and determining its involvement in egg production is, therefore, important in the search for a novel and crucial target for vector control.Methodology/Principal FindingsWe conducted an analysis to identify the ortholog of mammalian PTP1B in the Aedes aegypti genome. We identified eight genes coding for classical PTPs. In silico structural and functional analyses of proteins coded by such genes revealed that four of these code for catalytically active enzymes. Among the four genes coding for active PTPs, AAEL001919 exhibits the greatest degree of homology with the mammalian PTP1B. Next, we evaluated the role of this enzyme in egg formation. Blood feeding largely affects AAEL001919 expression, especially in the fat body and ovaries. These tissues are critically involved in the synthesis and storage of vitellogenin, the major yolk protein. Including the classical PTP inhibitor sodium orthovanadate or the PTP substrate DiFMUP in the blood meal decreased vitellogenin synthesis and egg production. Similarly, silencing AAEL001919 using RNA interference (RNAi) assays resulted in 30% suppression of egg production.Conclusions/SignificanceThe data reported herein implicate, for the first time, a gene that codes for a classical PTP in mosquito egg formation. These findings raise the possibility that this class of enzymes may be used as novel targets to block egg formation in mosquitoes.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Molecular Analysis of Aedes aegypti Classical Protein Tyrosine Phosphatases Uncovers an Ortholog of Mammalian PTP-1B Implicated in the Control of Egg Production in Mosquitoes

et al. 2014

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“…It is mediated by a set of three major components: protein tyrosine kinases (PTKs), protein tyrosine phosphatases (PTPs), and Src Homology 2 (SH2) domains. It has been demonstrated previously the role of such a mechanism during tick embryogenesis [80], mosquito early adult development [81] and parasite infection [82]. The analysis of the An.…”

Section: Resultsmentioning

confidence: 95%

Transcriptome Sequencing and Developmental Regulation of Gene Expression in Anopheles aquasalis

et al. 2014

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Background Anopheles aquasalis is a major malaria vector in coastal areas of South and Central America where it breeds preferentially in brackish water. This species is very susceptible to Plasmodium vivax and it has been already incriminated as responsible vector in malaria outbreaks. There has been no high-throughput investigation into the sequencing of An. aquasalis genes, transcripts and proteins despite its epidemiological relevance. Here we describe the sequencing, assembly and annotation of the An. aquasalis transcriptome.Methodology/Principal FindingsA total of 419 thousand cDNA sequence reads, encompassing 164 million nucleotides, were assembled in 7544 contigs of ≥2 sequences, and 1999 singletons. The majority of the An. aquasalis transcripts encode proteins with their closest counterparts in another neotropical malaria vector, An. darlingi. Several analyses in different protein databases were used to annotate and predict the putative functions of the deduced An. aquasalis proteins. Larval and adult-specific transcripts were represented by 121 and 424 contig sequences, respectively. Fifty-one transcripts were only detected in blood-fed females. The data also reveal a list of transcripts up- or down-regulated in adult females after a blood meal. Transcripts associated with immunity, signaling networks and blood feeding and digestion are discussed.Conclusions/SignificanceThis study represents the first large-scale effort to sequence the transcriptome of An. aquasalis. It provides valuable information that will facilitate studies on the biology of this species and may lead to novel strategies to reduce malaria transmission on the South American continent. The An. aquasalis transcriptome is accessible at http://exon.niaid.nih.gov/transcriptome/An_aquasalis/Anaquexcel.xlsx.

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“…Figure 8C shows that total PTP activity increased during the refilling cycle, being the highest at 30 days, the time for maximal loading with NO (as demonstrated in Figure 1 for NOS). Salivary gland PTP activity is highly inhibited by sodium orthovanadate (SO), which is a classical inhibitor of PTPs [29], [30], [31], [32], [33]. Furthermore, injection of the insects with Tc GIPL decreased PTP activity in glands (Figure 8D).…”

Section: Resultsmentioning

confidence: 99%

Glycoinositolphospholipids from Trypanosomatids Subvert Nitric Oxide Production in Rhodnius prolixus Salivary Glands

et al. 2012

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Background Rhodnius prolixus is a blood-sucking bug vector of Trypanosoma cruzi and T. rangeli. T. cruzi is transmitted by vector feces deposited close to the wound produced by insect mouthparts, whereas T. rangeli invades salivary glands and is inoculated into the host skin. Bug saliva contains a set of nitric oxide-binding proteins, called nitrophorins, which deliver NO to host vessels and ensure vasodilation and blood feeding. NO is generated by nitric oxide synthases (NOS) present in the epithelium of bug salivary glands. Thus, T. rangeli is in close contact with NO while in the salivary glands.Methodology/Principal FindingsHere we show by immunohistochemical, biochemical and molecular techniques that inositolphosphate-containing glycolipids from trypanosomatids downregulate NO synthesis in the salivary glands of R. prolixus. Injecting insects with T. rangeli-derived glycoinositolphospholipids (Tr GIPL) or T. cruzi-derived glycoinositolphospholipids (Tc GIPL) specifically decreased NO production. Salivary gland treatment with Tc GIPL blocks NO production without greatly affecting NOS mRNA levels. NOS protein is virtually absent from either Tr GIPL- or Tc GIPL-treated salivary glands. Evaluation of NO synthesis by using a fluorescent NO probe showed that T. rangeli-infected or Tc GIPL-treated glands do not show extensive labeling. The same effect is readily obtained by treatment of salivary glands with the classical protein tyrosine phosphatase (PTP) inhibitor, sodium orthovanadate (SO). This suggests that parasite GIPLs induce the inhibition of a salivary gland PTP. GIPLs specifically suppressed NO production and did not affect other anti-hemostatic properties of saliva, such as the anti-clotting and anti-platelet activities.Conclusions/SignificanceTaken together, these data suggest that trypanosomatids have overcome NO generation using their surface GIPLs. Therefore, these molecules ensure parasite survival and may ultimately enhance parasite transmission.

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A transient increase in total head phosphotyrosine levels is observed upon the emergence of Aedes aegypti from the pupal stage

Cited by 5 publications

References 32 publications

Molecular Analysis of Aedes aegypti Classical Protein Tyrosine Phosphatases Uncovers an Ortholog of Mammalian PTP-1B Implicated in the Control of Egg Production in Mosquitoes

Molecular Analysis of Aedes aegypti Classical Protein Tyrosine Phosphatases Uncovers an Ortholog of Mammalian PTP-1B Implicated in the Control of Egg Production in Mosquitoes

Transcriptome Sequencing and Developmental Regulation of Gene Expression in Anopheles aquasalis

Glycoinositolphospholipids from Trypanosomatids Subvert Nitric Oxide Production in Rhodnius prolixus Salivary Glands

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