From transcriptome to immunome: Identification of DTH inducing proteins from a Phlebotomus ariasi salivary gland cDNA library

Oliveira, Fabiano; Kamhawi, Shaden; Seitz, Amy E.; Pham, Van My; Guigal, Pierre M.; Fischer, Laurent; Ward, J; Valenzuela, Jesús G.

doi:10.1016/j.vaccine.2005.07.085

Cited by 107 publications

(153 citation statements)

References 28 publications

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“…aegypti), and an endonuclease (2 EST in 1 cluster). All these types of transcripts were previously found in all mosquito sialotranscriptomes done to date, except for the endonuclease, which was found only on in those of Culex pipiens quinquefasciatus (Ribeiro et al, 2004b), where the secreted recombinant enzyme was studied (Calvo and Ribeiro, 2006), and Phlebotomines (Anderson et al, 2006;Oliveira et al, 2006). Transcripts coding for the other enzymes are most probably associated with sugar feeding and antimicrobial activity.…”

Section: Putative Secreted Proteins Belonging To Ubiquitous Protein Fmentioning

confidence: 92%

An insight into the sialotranscriptome of the non-blood feeding Toxorhynchites amboinensis mosquito

Calvo

Pham

Ribeiro

2008

Insect Biochemistry and Molecular Biology

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All adult mosquitoes take sugar meals, and most adult females also take blood meals to develop eggs. Salivary glands (SG) of males are thus much smaller and do not contain many of the antihemostatic and antiinflammatory compounds found in females. In the past 5 years, transcriptome analyses have identified nearly 70 different genes expressed in adult female SG. For most of these, no function can be assigned in either blood or sugar feeding. Exceptionally, Toxorhynchites mosquitoes are unusual in that they never feed on blood, and the SG of adults are identical in both sexes. Transcriptome analysis of the adult SG of this mosquito was performed to increase knowledge of the evolution of blood feeding-and to identify polypeptide families associated with sugar feeding-in mosquitoes.

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Section: Putative Secreted Proteins Belonging To Ubiquitous Protein Fmentioning

confidence: 92%

An insight into the sialotranscriptome of the non-blood feeding Toxorhynchites amboinensis mosquito

Calvo

Pham

Ribeiro

2008

Insect Biochemistry and Molecular Biology

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“…Sixteen DNA plasmids coding for Lu. longipalpis salivary proteins were cloned into the VR2001-TOPO vector and purified as described (8). Two-month-old hamsters were immunized i.d.…”

Section: Construction Of Dna Plasmids Coding For Lu Longipalpis Salimentioning

confidence: 99%

“…Saliva contains a variety of potent and pharmacologically active components that favorably change the environment at the feeding site (4-7). Exposure to sand fly bites or salivary proteins results in strong cellular and/or humoral immunity specific to these components (8)(9)(10)(11). In animal models of CL, mice immunized with Phlebotomus papatasi salivary gland homogenate (SGH) or preexposed to uninfected sand fly bites were protected against Leishmania major infection delivered via needle inoculation (2) or by infected sand flies (12).…”

mentioning

confidence: 99%

Immunity to a salivary protein of a sand fly vector protects against the fatal outcome of visceral leishmaniasis in a hamster model

Gomes

Teixeira

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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209

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Visceral leishmaniasis (VL) is a fatal disease for humans, and no vaccine is currently available. Sand fly salivary proteins have been associated with protection against cutaneous leishmaniasis. To test whether vector salivary proteins can protect against VL, a hamster model was developed involving intradermal inoculation in the ears of 100,000 Leishmania infantum chagasi parasites together with Lutzomyia longipalpis saliva to mimic natural transmission by sand flies. Hamsters developed classical signs of VL rapidly, culminating in a fatal outcome 5-6 months postinfection. Saliva had no effect on the course of infection in this model. Immunization with 16 DNA plasmids coding for salivary proteins of Lu. longipalpis resulted in the identification of LJM19, a novel 11-kDa protein, that protected hamsters against the fatal outcome of VL. LJM19-immunized hamsters maintained a low parasite load that correlated with an overall high IFN-␥/TGF-␤ ratio and inducible NOS expression in the spleen and liver up to 5 months postinfection. Importantly, a delayed-type hypersensitivity response with high expression of IFN-␥ was also noted in the skin of LJM19-immunized hamsters 48 h after exposure to uninfected sand fly bites. Induction of IFN-␥ at the site of bite could partly explain the protection observed in the viscera of LJM19-immunized hamsters through direct parasite killing and/or priming of anti-Leishmania immunity. We have shown that immunity to a defined salivary protein (LJM19) confers powerful protection against the fatal outcome of a parasitic disease, which reinforces the concept of using components of arthropod saliva in vaccine strategies against vector-borne diseases.antisaliva immunity ͉ Leishmania ͉ sand fly saliva ͉ vector-based vaccine

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“…arabicus, and P. orientalis [12][13][14][15][16][17] and 3 Lutzomyia species; Lutzomyia (Lu. ) longipalpis, Lu.…”

Section: Phlebotomus (P) Papatasi P Ariasi P Perniciosus P Argmentioning

confidence: 99%

Ayadualin, a novel RGD peptide with dual antihemostatic activities from the sand fly Lutzomyia ayacuchensis, a vector of Andean-type cutaneous leishmaniasis

et al. 2015

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Sequence analysis of the Lutzomyia (Lu.) ayacuchensis salivary gland cDNA library identified a short peptide containing an RGD (Arg-Gly-Asp) sequence flanked by two cysteine residues in the C-terminal end as the most abundant transcript. In the present study, a recombinant protein of the RGD-containing peptide, designated ayadualin, was expressed in Escherichia colt and its activity was characterized. Ayadualin inhibited both collagen and ADP-induced platelet aggregations by interfering with the binding of integrin alpha(IIb)beta(3) to fibrinogen. The RGD sequence and cysteine residues located on both sides of the RGD sequence were essential for the inhibitory action. Moreover, ayadualin efficiently inhibited the intrinsic blood coagulation pathway irrespective of the RGD sequence. Measuring the enzymatic activity of coagulation factors using chromogenic substrates revealed that ayadualin efficiently inhibited factor XIIa (FXIIa) activity in a dose-dependent manner. In addition, pre-incubation of ayadualin with FXII inhibited FXIIa activity, while activated FXIIa was not affected by ayadualin, indicating that ayadualin inhibits the activation of FXII, but not enzymatic activity of FXIIa. These results indicated that ayadualin plays an important role in the blood feeding of Lu. ayacuchensis by inhibiting host hemostasis via dual mechanisms. (C) 2015 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved

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From transcriptome to immunome: Identification of DTH inducing proteins from a Phlebotomus ariasi salivary gland cDNA library

Cited by 107 publications

References 28 publications

An insight into the sialotranscriptome of the non-blood feeding Toxorhynchites amboinensis mosquito

An insight into the sialotranscriptome of the non-blood feeding Toxorhynchites amboinensis mosquito

Immunity to a salivary protein of a sand fly vector protects against the fatal outcome of visceral leishmaniasis in a hamster model

Ayadualin, a novel RGD peptide with dual antihemostatic activities from the sand fly Lutzomyia ayacuchensis, a vector of Andean-type cutaneous leishmaniasis

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