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1.
Vaccines (Basel) ; 11(7)2023 Jun 21.
Artículo en Inglés | MEDLINE | ID: mdl-37514945

RESUMEN

Leishmaniasis is a wide-spectrum disease caused by parasites from Leishmania genus. A well-modulated immune response that is established after the long-lasting clinical cure of leishmaniasis can represent a standard requirement for a vaccine. Previous studies demonstrated that Leishmania (Viannia) naiffi causes benign disease and its antigens induce well-modulated immune responses in vitro. In this work we aimed to identify the immunodominant proteins present in the soluble extract of L. naiffi (sLnAg) as candidates for composing a pan-specific anti-leishmaniasis vaccine. After immunoblotting using cured patients of cutaneous leishmaniasis sera and proteomics approaches, we identified a group of antigenic proteins from the sLnAg. In silico analyses allowed us to select mildly similar proteins to the host; in addition, we evaluated the binding potential and degree of promiscuity of the protein epitopes to HLA molecules and to B-cell receptors. We selected 24 immunodominant proteins from a sub-proteome with 328 proteins. Homology analysis allowed the identification of 13 proteins with the most orthologues among seven Leishmania species. This work demonstrated the potential of these proteins as promising vaccine targets capable of inducing humoral and cellular pan-specific immune responses in humans, which may in the future contribute to the control of leishmaniasis.

2.
Artículo en Inglés | MEDLINE | ID: mdl-37365421

RESUMEN

The emergence of resistant microorganisms has reduced the effectiveness of currently available antimicrobials, necessitating the development of new strategies. Plant antimicrobial peptides (AMPs) are promising candidates for novel drug development. In this study, we aimed to isolate, characterize, and evaluate the antimicrobial activities of AMPs isolated from Capsicum annuum. The antifungal potential was tested against Candida species. Three AMPs from C. annuum leaves were isolated and characterized: a protease inhibitor, a defensin-like protein, and a lipid transporter protein, respectively named CaCPin-II, CaCDef-like, and CaCLTP2. All three peptides had a molecular mass between 3.5 and 6.5 kDa and caused morphological and physiological changes in four different species of the genus Candida, such as pseudohyphae formation, cell swelling and agglutination, growth inhibition, reduced cell viability, oxidative stress, membrane permeabilization, and metacaspase activation. Except for CaCPin-II, the peptides showed low or no hemolytic activity at the concentrations used in the yeast assays. CaCPin-II inhibited α-amylase activity. Together, these results suggest that these peptides have the potential as antimicrobial agents against species of the genus Candida and can serve as scaffolds for the development of synthetic peptides for this purpose.

3.
Zootaxa ; 5235(1): 1-81, 2023 Feb 03.
Artículo en Inglés | MEDLINE | ID: mdl-37045120

RESUMEN

Cerambycidae is one of the largest families of Coleoptera, with approximately 38,000 species described. Knowledge of Cerambycidae fauna in Brazil has increased in the last 50 years, but some regions, such as the Brazilian semi-arid region, remain relatively unexplored. An updated checklist of Cerambycidae from that region, based on previously published works, checklists, and catalogs, and the study of 331 specimens of 72 species, 58 genera, 26 tribes, and three subfamilies deposited in the collection of the Zoology Museum of the Universidade Estadual de Feira de Santana is provided. This list has 633 species, 303 genera, 58 tribes, of four subfamilies of Cerambycidae from 75 municipalities in nine states in the Brazilian semi-arid region. A map illustrating the distribution of the Cerambycidae species in the semi-arid region is also provided. Four new species are described: Eburodacrys boteroi sp. nov. and Coccoderus costae sp. nov. (Cerambycinae); and Aerenicopsis joseferreirai sp. nov. and Pseudomecas mourai sp. nov. (Lamiinae). The new species are included in an identification key to the respective genus. Furthermore, Antodice kyra Martins & Galileo, 1998 is new record from the Bahia State; Chevrolatella tripunctata (Chevrolat, 1862) is a new record to Brazilian semi-arid region; Colobothea rubroornata Zajciw, 1962 is a new record from Bahia State and Brazilian semi-arid region, and Odontocera bilobata Zajciw, 1965 is a new record from the Bahia State and Brazilian semi-arid region. It is evident that some regions in the Brazilian semi-arid region are poorly sampled and new inventory studies must be carried out.


Asunto(s)
Escarabajos , Animales , Brasil , Zoología , Museos , Manejo de Especímenes
4.
Neotrop Entomol ; 51(3): 458-473, 2022 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-35590008

RESUMEN

Two new species of the Pelidnota liturella species group are described from Brazil, Pelidnota everardoi sp. nov. and P. luciae sp. nov. The new species are included on the Pelidnota key proposed previously in the literature and an identification key is provided for the Pelidnota liturella species group. Diagnostic characters of the new species, illustrations of male genitalia, and photographs of type material are provided. Furthermore, notes about the Pelidnota liturella species group distribution and new Brazilian state records for two species are also provided: P. flavovittata (Perty, 1830) from Goiás, Rio de Janeiro and São Paulo; and P. liturella liturella (Kirby, 1819) from Ceará. Finally, distributional maps for all the P. liturella species group are provided.


Asunto(s)
Escarabajos , Animales , Brasil , Genitales Masculinos , Masculino
5.
Zootaxa ; 4728(4): zootaxa.4728.4.10, 2020 Jan 24.
Artículo en Inglés | MEDLINE | ID: mdl-32229890

RESUMEN

This contribution is an update catalogue of the type specimens of Insecta deposited in the entomological collection Prof. Johann Becker of the Museum of Zoology of Universidade Estadual de Feira de Santana, Bahia, Brazil. A list of 206 holtypes and 1,430 paratypes of 23 families, 73 genera, and 244 species allocated in 12 orders. Lectotype and paralectotypes of Bitoma palmarum Bondar, 1940 were designated. Diptera present the highest number of types on the collection, with 161 holotypes and 1,324 paratypes.


Asunto(s)
Entomología , Insectos , Museos , Animales , Brasil , Zoología
6.
J Pept Sci ; 24(11): e3129, 2018 Nov.
Artículo en Inglés | MEDLINE | ID: mdl-30325566

RESUMEN

Eight molecules, four peptides (SPs) and four lipopeptides (LPs) derived by rational design from surfactin, a well-known secreted biosurfactant from Bacillus subtilis, were produced employing Fmoc-based solid-phase synthesis. These new peptides were tested to evaluate their potential biosurfactant and biological activities, aiming at possible applications in industrial, biological, pharmaceutical, and medical use. Five molecules (SP1, SP2, SP4, LP5, and LP8) presented potential for medical uses, mainly due to their drug delivery properties as suggested by their synergistic activity with the antibiotic vancomycin against Staphylococcus aureus. All synthetic peptides showed low toxicity against Vero cell cultures, in assays of hemolysis, and in different cytotoxicity assays. In addition, we found that three peptides (SP1, LP6, and LP7) had potential technological and industrial use because of their emulsifying capacity, low toxicity, and ability to physically stabilize solutions. These novel molecules retained some properties of the parental molecule (surfactin, which was originally obtained through nonribosomal synthesis in Bacillus subtilis) but have the advantage of being linear peptides, which can be produced at large scales through the use of conventional heterologous protein expression protocols.


Asunto(s)
Bacillus subtilis/metabolismo , Lipopéptidos/síntesis química , Péptidos Cíclicos/química , Péptidos/síntesis química , Técnicas de Síntesis en Fase Sólida/métodos , Animales , Bacillus subtilis/química , Proteínas Bacterianas/química , Chlorocebus aethiops , Portadores de Fármacos/síntesis química , Portadores de Fármacos/química , Portadores de Fármacos/farmacología , Sinergismo Farmacológico , Emulsionantes/síntesis química , Emulsionantes/química , Emulsionantes/farmacología , Humanos , Lipopéptidos/química , Lipopéptidos/farmacología , Péptidos/química , Péptidos/farmacología , Staphylococcus aureus/efectos de los fármacos , Vancomicina/farmacología , Células Vero
7.
Protein Pept Lett ; 19(5): 520-9, 2012 May.
Artículo en Inglés | MEDLINE | ID: mdl-22486647

RESUMEN

In this study, the antifungal activity of peptides extracted from Adenanthera pavonina seeds was assessed. Peptides were extracted and fractionated by DEAE-Sepharose chromatography. The non-retained D1 fraction efficiently inhibited the growth of the pathogenic fungi. This fraction was later further fractionated by reversed-phase chromatography, resulting in 23 sub-fractions. All separation processes were monitored by tricine-SDS-PAGE. Fractions H11 and H22 strongly inhibited the growth of Saccharomyces cerevisiae and Candida albicans. Fraction H11 caused 100% death in S. cerevisiae in an antimicrobial assay. The complete amino acid sequence of the peptide in fraction P2 was determined, revealing homology to plant defensins, which was named ApDef1. Peptides from fraction H22 were also sequenced.


Asunto(s)
Antifúngicos/farmacología , Péptidos Catiónicos Antimicrobianos/farmacología , Fabaceae/química , Hongos/efectos de los fármacos , Extractos Vegetales/farmacología , Semillas/química , Secuencia de Aminoácidos , Antifúngicos/química , Péptidos Catiónicos Antimicrobianos/química , Cromatografía Liquida , Pruebas de Sensibilidad Microbiana , Viabilidad Microbiana/efectos de los fármacos , Datos de Secuencia Molecular , Extractos Vegetales/química , Alineación de Secuencia
8.
Circ J ; 76(6): 1476-85, 2012.
Artículo en Inglés | MEDLINE | ID: mdl-22453000

RESUMEN

BACKGROUND: Epsilon-protein kinase C (εPKC) protects the heart from ischemic injury. However, the mechanism(s) of εPKC cardioprotection is still unclear. Identification of the εPKC targets may aid in elucidating the εPKC-mediated cardioprotective mechanisms. Previous studies, using εPKC transgenic mice and difference in gel electrophoresis, identified proteins involved in glucose metabolism, the expression of which was modified by εPKC. Those studies were accompanied by metabolomic analysis, suggesting that increased glucose oxidation may be responsible for the cardioprotective effect of εPKC. Whether these εPKC-mediated alterations were because of differences in protein expression or phosphorylation was not determined. METHODS AND RESULTS: In the present study, we used an εPKC -specific activator peptide, ψεRACK, combined with phosphoproteomics, to find εPKC targets, and identified that the proteins whose phosphorylation was altered by selective activation of εPKC were mostly mitochondrial proteins. Analysis of the mitochondrial phosphoproteome led to the identification of 55 spots, corresponding to 37 individual proteins, exclusively phosphorylated, in the presence of ψεRACK. The majority of the proteins identified were involved in glucose and lipid metabolism, components of the respiratory chain as well as mitochondrial heat shock proteins. CONCLUSIONS: The protective effect of εPKC during ischemia involves phosphorylation of several mitochondrial proteins involved in glucose and lipid metabolism and oxidative phosphorylation. Regulation of these metabolic pathways by εPKC phosphorylation may lead to εPKC-mediated cardioprotection induced by ψεRACK.


Asunto(s)
Metabolismo Energético , Mitocondrias Cardíacas/enzimología , Isquemia Miocárdica/enzimología , Miocardio/enzimología , Proteína Quinasa C-epsilon/metabolismo , Animales , Citoprotección , Modelos Animales de Enfermedad , Metabolismo Energético/efectos de los fármacos , Activación Enzimática , Activadores de Enzimas/farmacología , Glucosa/metabolismo , Técnicas In Vitro , Metabolismo de los Lípidos , Isquemia Miocárdica/prevención & control , Oligopéptidos/farmacología , Fosforilación Oxidativa , Perfusión , Fosforilación , Proteómica/métodos , Ratas , Ratas Wistar , Transducción de Señal
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