KEITY SOUZA SANTOS
Projetos de Pesquisa
Unidades Organizacionais
Departamento de Clínica Médica, Faculdade de Medicina - Docente
LIM/19 - Laboratório de Histocompatibilidade e Imunidade Celular, Hospital das Clínicas, Faculdade de Medicina - Líder
LIM/19 - Laboratório de Histocompatibilidade e Imunidade Celular, Hospital das Clínicas, Faculdade de Medicina - Líder
22 resultados
Resultados de Busca
Agora exibindo 1 - 10 de 22
conferenceObject Immune Responses Of CVID Patients To COVID-19 Vaccines(2023) MEDEIROS, Giuliana Xavier de; FERREIRA, Loisi de Carvalho Pereira; MAGAWA, Jhosiene Yukari; KURAMOTO, Andreia; SASAHARA, Greyce Luri; FERREIRA, Marcelo; BARROS, Myrthes Maragna Toledo; KALIL, Jorge; MARINHO, Ana Karolina Barreto Berselli; CUNHA-NETO, Edecio; SANTOS, Keity Souza; KOKRON, CristinabookPart Laboratório em alergia(2022) KOKRON, Cristina Maria; SANTOS, Keity SouzabookPart Medicina de precisão em alergia(2022) SANTOS, Keity Souza; LIMA, Karine de Amicis; CASTRO, Fábio Fernandes Morato; KALIL, Jorge- Is age associated with the development of antibodies against botulinum toxin?(2013) AUN, M. V.; CHUNG, T. M.; SANTOS, K. S.; BATTISTELLA, L. M. R.; RIZZO, L. V.; KALIL, J.; GIAVINA-BIANCHI, P.
- 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.
- Proteomic Analysis of Urine in Rats Chronically Exposed to Fluoride(2011) KOBAYASHI, Claudia Ayumi Nakai; LEITE, Aline de Lima; SILVA, Thelma Lopes da; SANTOS, Lucilene Delazari dos; NOGUEIRA, Fabio Cesar Sousa; SANTOS, Keity Souza; OLIVEIRA, Rodrigo Cardoso de; PALMA, Mario Sergio; DOMONT, Gilberto Barbosa; BUZALAF, Marilia Afonso RabeloUrine is an ideal source of materials to search for potential disease-related biomarkers as it is produced by the affected tissues and can be easily obtained by noninvasive methods. 2-DE-based proteomic approach was used to better understand the molecular mechanisms of injury induced by fluoride (F-) and define potential biomarkers of dental fluorosis. Three groups of weanling male Wistar rats were treated with drinking water containing 0 (control), 5, or 50 ppm F- for 60 days (n = 15/group). During the experimental period, the animals were kept individually in metabolic cages, to analyze the water and food consumption, as well as fecal and urinary F excretion. Urinary proteome profiles were examined using 2-DE and Colloidal Coomassie Brilliant Blue staining. A dose-response regarding F- intake and excretion was detected. Quantitative intensity analysis revealed 8, 11, and 8 significantly altered proteins between control vs. 5 ppm F-, control vs. 50 ppm F- and 5 ppm F- vs. 50 ppm F- groups, respectively. Two proteins regulated by androgens (androgen-regulated 20-KDa protein and 0c-2,1-globulin) and one related to detoxification (aflatoxin-Bl-aldehyde-reductase) were identified by MALDI-TOF-TOF MS/MS. Thus, proteomic analysis can help to better understand the mechanisms underlying F- toxicity, even in low doses. 2010 Wiley Periodicals, Inc. J Biochem Mol Toxicol 25:8-14, 2011; View this article online at wileyonlinelibrary.com. DOI 10:1002/jbt.20353
- Follow-up of young adult monozygotic twins after simultaneous critical coronavirus disease 2019: a case report (vol 9, 1008585, 2022)(2023) CASTRO, Mateus V. de; SILVA, Monize V. R.; SOARES, Flavia B.; CORIA, Vivian R.; NASLAVSKY, Michel S.; SCLIAR, Marilia O.; CASTELLI, Erick C.; OLIVEIRA, Jamile R. de; MEDEIROS, Giuliana X. de; SASAHARA, Greyce L.; SANTOS, Keity S.; CUNHA-NETO, Edecio; KALIL, Jorge; ZATZ, Mayana
- Proteomic characterization of the multiple forms of the PLAs from the venom of the social wasp Polybia paulista(2011) SANTOS, Lucilene Delazari dos; MENEGASSO, Anally Ribeiro da Silva; PINTO, Jose Roberto Aparecido dos Santos; SANTOS, Keity Souza; CASTRO, Fabio Morato; KALIL, Jorge Elias; PALMA, Mario SergioThe phospholipases A(1) (PLA(1)s) from the venom of the social wasp Polybia paulista occur as a mixture of different molecular forms. To characterize the molecular origin of these structural differences, an experimental strategy was planned combining the isolation of the pool of PLAs from the wasp venom with proteomic approaches by using 2-D, MALDI-TOF-TOF MS and classical protocols of protein chemistry, which included N- and C-terminal sequencing. The existence of an intact form of PLA(1) and seven truncated forms was identified, apparently originating from controlled proteolysis of the intact protein; in addition to this, four of these truncated forms also presented carbohydrates attached to their molecules. Some of these forms are immunoreactive to specific-IgE, while others are not. These observations permit to raise the hypothesis that naturally occurring proteolysis of PLA(1), combined with protein glycosylation may create a series of different molecular forms of these proteins, with different levels of allergenicity. Two forms of PLA(2)s, apparently related to each other, were also identified; however, it was not possible to determine the molecular origin of the differences between both forms, except that one of them was glycosylated. None of these forms were immunoreactive to human specific IgE.
- Reactions to Shrimp Including Severe Anaphylaxis in Mite- and Cockroach-Allergic Patients Who Have Never Eaten Shrimp: Clinical Significance of IgE Cross-Reactivity to Tropomyosins From Different Sources(2019) MARTINS, T. F.; MENDONCA, T. N.; MELO, J. M. L.; MORENO, A. S.; JANUARIO, Y. C.; DASILVA, L. L. P.; DIAS, M. M.; MEIRELES, P. R.; SANTOS, K. S.; YANG, A. C.; ARRUDA, L. K.
- Modification of the brain proteome of Africanized honeybees (Apis mellifera) exposed to a subaEurolethal doses of the insecticide fipronil(2014) ROAT, T. C.; SANTOS-PINTO, J. R. A. dos; SANTOS, L. D. dos; SANTOS, K. S.; MALASPINA, O.; PALMA, M. S.Fipronil is a phenylpyrazole insecticide that is widely used in Brazilian agriculture for pest control. Although honeybees are not targets of fipronil, studies indicate that this pesticide can be harmful to honeybees. To assess the effects of fipronil in the brain of Africanized Apis mellifera workers, this study focused on the toxico-proteome profiling of the brain of newly emerged and aged honeybee workers that were exposed to a sub-lethal dose (10 pg fipronil per day. i.e. (1)/(100) of LD50/bee/day during 5 days) of the insecticide. Proteomic analysis identified 25 proteins that were differentially up-regulated or down-regulated when the fipronil-exposed and non-exposed groups were compared. These proteins are potentially related to pathogen susceptibility, neuronal chemical stress, neuronal protein misfolding, and occurrence of apoptosis, ischemia, visual impairment, damaged synapse formation, brain degeneration, memory and learning impairment. The exposure of honeybees to a very low dose of fipronil, even for a short period of time (5 days), was sufficient to cause a series of important neuroproteomic changes in the brains of honeybees.
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