HELEN ANDRADE ARCURI
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- Coagulation Factor XII Gene Mutation in Brazilian Families with Hereditary Angioedema with Normal C1 Inhibitor(2015) MORENO, Adriana S.; VALLE, Solange O. R.; LEVY, Soloni; FRANCA, Alfeu T.; SERPA, Faradiba S.; ARCURI, Helen A.; PALMA, Mario S.; CAMPOS, Wagner N.; DIAS, Marina M.; PONARD, Denise; MONNIER, Nicole; LUNARDI, Joel; BORK, Konrad; SILVA JR., Wilson Araujo; ARRUDA, L. KarlaBackground: Hereditary angioedema (HAE) with normal C1 inhibitor (C1-INH) is a rare disorder. Mutations of the gene encoding coagulation factor XII have been identified in a subset of patients with this condition. Our aim was to investigate mutations in the F12 gene in patients with HAE with normal C1-INH from Brazil. Methods: We studied 5 Brazilian families with index female patients who presented with recurrent angioedema with normal C1-INH and C4 levels. Genomic DNA was isolated from whole blood and PCR was performed. Mutations were detected by the sequencing of exon 9 of the F12 gene and allelic discrimination. Results: The c.983C>A (p.Thr328Lys) mutation was identified in 16 subjects, from 4 of the 5 families studied, including 8 patients with symptoms of HAE with normal C1-INH (87.5% women) and 8 subjects asymptomatic for HAE (25% women). Mean age at onset of symptoms among the FXII-HAE patients was 13.8 years (range 6-25 years). Recurrent abdominal pain (100%) and subcutaneous angioedema (87.5%) were the most frequent clinical presentations. Two patients presented with associated laryngeal edema. In keeping with previous observations in patients with both C1-INH-HAE and HAE with normal C1-INH, all 7 women with FXII-HAE reported triggering or worsening of symptoms upon intake of estrogen-containing oral contraceptives and/or pregnancy. Conclusions: We report for the first time in Brazil a mutation in the F12 gene as a likely cause of HAE with normal C1-INH in patients with recurrent attacks of angioedema and/or abdominal pain. A higher frequency of abdominal pain attacks and onset of symptoms at a younger age were observed among Brazilian patients when compared to those from other parts of the world. (C) 2015 S. Karger AG, Basel
- Novel allergens from ancient foods: Man e 5 from manioc (Manihot esculenta Crantz) cross reacts with Hev b 5 from latex(2013) SANTOS, Keity Souza; GADERMAIER, Gabriele; VEJVAR, Eva; ARCURI, Helen Andrade; GALVAO, Clovis Eduardo; YANG, Ariana Campos; RESENDE, Virginia Maria Ferreira; MARTINS, Carlo de Oliveira; HIMLY, Martin; MARI, Adriano; LISO, Marina; POMPONI, Debora; BREITENEDER, Heimo; WAGNER, Stefan; KALIL, Jorge; FERREIRA, Fatima; CASTRO, Fabio Fernandes MoratoScope Manioc (Manihot esculenta) is a tuber mainly consumed in the Southern Hemisphere and used worldwide by food and chemistry industry. We aimed to recombinantly produce and characterize the first manioc allergen and evaluate its IgE reactivity in sera of Brazilian and Italian patients. Methods and results The molecule, termed Man e5, was expressed in E. coli, characterized by amino acid analysis, mass spectrometry, circular dichroism, HPLC, and dynamic light scattering. A tertiary structural model of the protein was produced using bioinformatics and susceptibility to pepsin digestion was analyzed in vitro. Based on its high content of charged residues, heat stability, flexibility and lack of secondary structure elements, the allergen was determined a member of the intrinsically disordered protein family. Brazilian patients were selected based on manioc allergy and Italians based on latex allergy and sensitization to Hev b 5.71% of Brazilians and 40% of Italians were in vitro IgE positive to Man e5. Cross-inhibition assays suggest a possible involvement of this allergen in the latex-fruit syndrome. Conclusion Man e5, the first purified allergen from manioc demonstrates IgE cross-reactivity with Hev b 5. Data suggest Hev b 5 might act as primary sensitizer and could therefore lead to allergic manifestations upon manioc consumption without prior exposition.
article 15 Citação(ões) na Scopus Understanding the Structure, Activity and Inhibition of Chorismate Synthase from Mycobacterium tuberculosis(2011) ARCURI, H. A.; PALMA, M. S.Tuberculosis is considered a worldwide health problem mainly due to co-infection with HIV and proliferation of multi-drug-resistant strains. The enzymes of the shikimate pathway are potential targets for the development of new therapies because they are essential for bacteria, but absent from mammals. The last step in this pathway is performed by chorismate synthase (CS), which catalyzes the conversion of 5-enolpyruvylshikimate-3-phosphate (EPSP) to chorismate. The aim of this article is to review the available information on chorismate synthase from Mycobacterium tuberculosis.- Analysis of the coverage capacity of the StreptInCor candidate vaccine against Streptococcus pyogenes(2014) AMICIS, Karine M. De; BARROS, Samar Freschi de; ALENCAR, Raquel E.; POSTOL, Edilberto; MARTINS, Carlo de Oliveira; ARCURI, Helen Andrade; GOULART, Cibelly; KALIL, Jorge; GUILHERME, LuizaStreptococcus pyogenes is responsible for infections as pharyngitis, sepsis, necrotizing fasciitis and streptococcal toxic shock syndrome. The M protein is the major bacterial antigen and consists of both polymorphic N-terminal portion and a conserved region. In the present study, we analyzed the in vitro ability of StreptInCor a C-terminal candidate vaccine against S. pyogenes to induce antibodies to neutralize/opsonize the most common S. pyogenes strains in Sao Paulo by examining the recognition by sera from StreptInCor immunized mice. We also evaluated the presence of cross-reactive antibodies against human heart valve tissue. Anti-StreptInCor antibodies were able to neutralize/opsonize at least 5 strains, showing that immunization with StreptInCor is effective against several S. pyogenes strains and can prevent infection and subsequent sequelae without causing autoimmune reactions.
- B-cell linear epitopes mapping of antigen-5 allergen from Polybia paulista wasp venom(2015) SANTOS-PINTO, Jose Roberto Aparecido dos; SANTOS, Lucilene Delazari dos; ARCURI, Helen Andrade; MENEGASSO, Anally Ribeiro da Silva; PEGO, Paloma Napoleao; SANTOS, Keity Souza; CASTRO, Fabio Morato; KALIL, Jorge Elias; DE-SIMONE, Salvatore Giovanni; PALMA, Mario Sergio
- Using Proteomic Strategies for Sequencing and Post-Translational Modifications Assignment of Antigen-5, a Major Allergen from the Venom of the Social Wasp Polybia paulista(2014) SANTOS-PINTO, Jose Roberto Aparecido dos; SANTOS, Lucilene Delazari dos; ARCURI, Helen Andrade; CASTRO, Fabio Morato; KALIL, Jorge Elias; PALMA, Mario SergioAntigen-5 is one of the major allergens identified in wasp venoms, and despite the fact that its biological function is still unknown, many studies have demonstrated its allergenicity. In this study, the biochemical and structural characterization of antigen-5 from the venom of the social wasp Polybia paulista are reported. A gel-based mass spectrometry strategy with CID fragmentation methods and classical protocols of protein chemistry, which included N- and C-terminal sequencing, were used to assign the complete sequence and determine the presence/location of the post-translational modifications (PTMs) of this protein. Six different isoforms of antigen-5 were identified in the crude venom of P. paulista; the most abundant, which corresponds to the intact form of this protein, was recognized by the pool of human specific-IgE. This protein was extensively sequenced through CID mass spectrometry, and a series of PTMs were observed such as hydroxylation, phosphorylation, and glycosylation. Sequence data revealed that this protein has 59.3-93.7% identity with antigen-5 proteins from other known vespid venoms. The molecular model of P. paulista antigen-5 shows that this protein has three alpha-helices, one 3(10), helix, and four beta-sheets covering 28 and 17.9% of the sequence, respectively. The identification and characterization of allergenic compounds is essential for the development of advanced component-resolved allergy diagnostics and treatment.
- Proteomic Characterization of the Hyaluronidase (EC 3.2.1.35) from the Venom of the Social Wasp Polybia paulista(2012) PINTO, Jose Roberto Aparecido dos Santos; SANTOS, Lucilene Delazari dos; ARCURI, Helen Andrade; DIAS, Nathalia Baptista; PALMA, Mario SergioPolybia paulista wasp venom possesses three major allergens: phospholipase A(1), hyaluronidase and antigen-5. To the best of our knowledge, no hyaluronidase from the venom of Neotropical social wasps was structurally characterized up to this moment, mainly due to its reduced amount in the venom of the tropical wasp species (about 0.5% of crude venom). Four different glycoproteic forms of this enzyme were detected in the venom of the wasp Polybia paulista. In the present investigation, an innovative experimental approach was developed combining 2-D SDS-PAGE with in-gel protein digestion by different proteolytic enzymes, followed by mass spectrometry analysis under collision-induced dissociation CID) conditions for the complete assignment of the protein sequencing. Thus, the most abundant form of this enzyme in P. paulista venom, the hyaluronidase-III, was sequenced, revealing that the first 47 amino acid residues from the N-terminal region, common to other Hymenoptera venom hyaluronidases, are missing. The molecular modeling revealed that hyaluronidase-III has a single polypeptide chain, folded into a tertiary structure, presenting a central (beta/alpha)(5) core with alternation of beta-strands and alpha-helices; the tertiary structure stabilized by a single disulfide bridge between the residues Cys(189) and Cys(201). The structural pattern reported for P. paulista venom hyaluronidase-III is compatible with the classification of the enzyme as member of the family 56 of glycosidase hydrolases. Moreover, its structural characterization will encourage the use of this protein as a model for future development of ""component-resolved diagnosis"".
- Structural and Molecular Changes Caused By Mutations Thr328Lys and Thr328Arg In FXII Associated With Hereditary Angioedema With Normal C1 Inhibitor(2014) MORENO, Adriana S.; ARCURI, Helen; PALMA, Mario; ARRUDA, Luisa Karla P.
conferenceObject Mutation in factor XII gene in Brazilian families associated with hereditary angioedema with normal C1 inhibitor(2013) MORENO, A. S.; VALLE, S. O.; FRANCA, A. T.; LEVY, S. A.; SERPA, F. S.; MONNIER, N.; PONARD, D.; LUNARDI, J.; MENDONCA, M. D.; CAMPOS, W. A.; ARCURI, H.; PALMA, M. S.; SILVA JUNIOR, W. A. da; ARRUDA, L. K.