Proteomic characterization of the released/secreted proteins of Leishmania (Viannia) braziliensis promastigotes

Cuervo, Patrícia; Jesus, José Batista de; Sabóia-Vahia, Leonardo; Mendonça-Lima, Leila; Domont, Gilberto B.; Cupolillo, Elisa

doi:10.1016/j.jprot.2009.08.006

Cited by 85 publications

(66 citation statements)

References 78 publications

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“…Proteomic studies have been previously performed with L. braziliensis with the purpose to identify excreted factors, as well as proteins showing variations of expression in different L. braziliensis strains producing diverse clinical forms of the disease (28,29). The present study is complementary to those performed, since promastigote extracts, as well as amastigote-like-stage proteins, were employed for the identification of the most antigenic proteins of L. braziliensis.…”

Section: Discussionmentioning

confidence: 99%

“…In addition, the identification of proteins able to predict the success of a given treatment will help the follow-up of patients after treatment. Only a few reports that applied proteomic methods for the identification of L. braziliensis-excreted proteins or those related to the development of different clinical forms of TL have been published so far (28,29). In this context, the present study applied for the first time an immunoproteomic approach to the stationary-phase promastigote and amastigote-like stages of L. braziliensis using sera from TL patients.…”

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confidence: 99%

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Proteins Selected in Leishmania (Viannia) braziliensis by an Immunoproteomic Approach with Potential Serodiagnosis Applications for Tegumentary Leishmaniasis

Duarte

Pimenta

Menezes‐Souza

et al. 2015

Clin Vaccine Immunol

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The serodiagnosis of human tegumentary leishmaniasis (TL) presents some problems, such as the low level of antileishmanial antibodies found in most of the patients, as well as the cross-reactivity in subjects infected by other trypanosomatids. In the present study, an immunoproteomic approach was performed aimed at identification of antigens in total extracts of stationaryphase promastigote and amastigote-like forms of Leishmania (Viannia) braziliensis using sera from TL patients. With the purpose of reducing the cross-reactivity of the identified proteins, spots recognized by sera from TL patients, as well as those recognized by antibodies present in sera from noninfected patients living in areas where TL is endemic and sera from Chagas disease patients, were discarded. Two Leishmania hypothetical proteins and 18 proteins with known functions were identified as antigenic. The study was extended with some of them to validate the results of the immunoscreening. The coding regions of five of the characterized antigens (enolase, tryparedoxin peroxidase, eukaryotic initiation factor 5a, ␤-tubulin, and one of the hypothetical proteins) were cloned in a prokaryotic expression vector, and the corresponding recombinant proteins were purified and evaluated for the serodiagnosis of TL. The antigens presented sensitivity and specificity values ranging from 95.4 to 100% and 82.5 to 100%, respectively. As a comparative antigen, a preparation of Leishmania extract showed sensitivity and specificity values of 65.1 and 57.5%, respectively. The present study has enabled the identification of proteins able to be employed for the serodiagnosis of TL. L eishmaniasis consists of a spectrum of diseases caused by protozoan parasites of the genus Leishmania, which present high morbidity and mortality throughout the world (1). Approximately 350 million people in 98 countries are at risk of contracting the infection, while nearly 1.0 to 1.5 million cases of tegumentary leishmaniasis (TL) and 0.2 to 0.5 million cases of visceral leishmaniasis (VL) are registered annually (2). Although TL is not a fatal disease, it is endemic in more than 70 countries, and 90% of the cases have occurred in Afghanistan, Algeria, Brazil, Pakistan, Peru, Saudi Arabia, and Syria (3). The disease exhibits distinct clinical manifestations, such as cutaneous leishmaniasis (CL), diffuse cutaneous leishmaniasis (DCL), and mucosal leishmaniasis (ML) (4, 5). In Brazil, TL is caused mainly by infection with the species Leishmania (Viannia) braziliensis, Leishmania (V.) guyanensis, and Leishmania (Leishmania) amazonensis, although parasitological and molecular evidence has shown that L. braziliensis is the most important etiological agent of the disease (6, 7).At present, there is no gold standard test for TL diagnosis, and a combination of diagnostic methods is frequently needed to obtain more precise results (8). Parasitological diagnosis is definitive and consists of the microscopic examination of Giemsa-stained biopsy specimen smears, of histopathological examinati...

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Proteins Selected in Leishmania (Viannia) braziliensis by an Immunoproteomic Approach with Potential Serodiagnosis Applications for Tegumentary Leishmaniasis

Duarte

Pimenta

Menezes‐Souza

et al. 2015

Clin Vaccine Immunol

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“…Some extracellular proteins are known to be transported via a non-conventional secretion pathway which does not require the presence of a signal peptide (Nickel and Rabouille, 2009). In fact, for some kinetoplastid pathogens, the majority of extracellular proteins do not possess a signal peptide and are released by a micro-vesicle based secretion system (Silverman et al, 2008;Cuervo et al, 2009;Geiger et al, 2010). SecretomeP software (Bendtsen et al, 2004a) was used to determine whether some of the QPX proteins, which were found to be extracellular by LC/MS analysis but did not contain an N-terminal signal peptide, were secreted via a non-classical pathway (Geiger et al, 2010).…”

Section: Discussionmentioning

confidence: 99%

Characterisation of the secretome of the clam parasite, QPX

Rubin

Espinosa

Koller

et al. 2015

International Journal for Parasitology

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“…However, exceptions to this rule have been found in increasing number and recent proteomic studies of animal cells suggest that 16% of the secreted proteins lack a signal sequence (40). Surprisingly, over half of the proteins secreted by Leishmania braziliensis follow non-classical secretion mechanisms (41). Over 20 mammalian proteins have now been well characterized as being secreted through one of the multiple unconventional secretion mechanisms (37).…”

Section: Discussionmentioning

confidence: 99%

Pregnenolone Sulfate and Cortisol Induce Secretion of Acyl-CoA-binding Protein and Its Conversion into Endozepines from Astrocytes

Loomis

Behrens

Williams

et al. 2010

Journal of Biological Chemistry

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Acyl-CoA-binding protein (ACBP) functions both intracellularly as part of fatty acid metabolism and extracellularly as diazepam binding inhibitor, the precursor of endozepine peptides. Two of these peptides, ODN and TTN, bind to the GABA A receptor and modulate its sensitivity to ␥-aminobutyric acid (GABA). We have found that depolarization of mouse primary astrocytes induces the rapid release and processing of ACBP to the active peptides. We previously showed that ODN can trigger the rapid sporulation of the social amoeba Dictyostelium. Using this bioassay, we now show that astrocytes release the endozepine peptides within 10 min of exposure to the steroids cortisol, pregnenolone, pregnenolone sulfate, or progesterone. ACBP lacks a signal sequence for secretion through the endoplasmic reticulum/Golgi pathway and its secretion is not affected by addition of brefeldin A, a well known inhibitor of the classical secretion pathway, suggesting that it follows an unconventional pathway for secretion. Moreover, induction of autophagy by addition of rapamycin also resulted in rapid release of ACBP indicating that this protein uses components of the autophagy pathway for secretion. Following secretion, ACBP is proteolytically cleaved to the active neuropeptides by protease activity on the surface of astrocytes. Neurosteroids, such as pregnenolone sulfate, were previously shown to modulate the excitatory/inhibitory balance in brain through increased release of glutamate and decreased release of GABA. These effects of steroids in neurons will be reinforced by the release of endozepines from astrocytes shown here, and suggest an orchestrated astrocyte-neuron cross-talk that can affect a broad spectrum of behavioral functions.

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Proteomic characterization of the released/secreted proteins of Leishmania (Viannia) braziliensis promastigotes

Cited by 85 publications

References 78 publications

Proteins Selected in Leishmania (Viannia) braziliensis by an Immunoproteomic Approach with Potential Serodiagnosis Applications for Tegumentary Leishmaniasis

Proteins Selected in Leishmania (Viannia) braziliensis by an Immunoproteomic Approach with Potential Serodiagnosis Applications for Tegumentary Leishmaniasis

Characterisation of the secretome of the clam parasite, QPX

Pregnenolone Sulfate and Cortisol Induce Secretion of Acyl-CoA-binding Protein and Its Conversion into Endozepines from Astrocytes

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