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1.
Eur Rev Med Pharmacol Sci ; 26(22): 8620-8630, 2022 11.
Artigo em Inglês | MEDLINE | ID: mdl-36459045

RESUMO

In May 2022, cases of monkeypox were reported in non-monkeypox endemic countries such as Europe and the United States. As of 26 May, a cumulative total of 257 laboratory-confirmed cases and approximately 120 suspected cases had been reported to WHO from non-monkeypox endemic countries. This event immediately caused great concern and alarm to the WHO and national virologists. This paper aims to summarize the epidemiological and clinical features of previous monkeypox virus infections and the current local outbreaks in non-monkeypox endemic countries and propose countermeasures to control the current localized infections in non-monkeypox endemic areas as soon as possible. We reviewed the literature and websites related to monkeypox. We searched Google Scholar, PubMed, Web of Science, Embase, and African Journals Online using the medical subject terms "monkeypox", "monkeypox virus", "monkeypox outbreak", "non-monkeypox endemic areas", "clinical features", "epidemiology", "transmission", and "infection". We found that monkeypox is a zoonotic disease of forest animals that has occurred mainly in West and Central Africa since the first case was reported in the Congo in 1970, with occasional cases spreading to countries such as the United States and Europe. It is common among students, housekeepers, hunters, farmers and housewives. It is more common in males than females, occurs below middle age, and is more common in children under 10. The incubation period is 5 to 21 days, and the rash usually appears within 1 to 3 days after the onset of fever. Clinical manifestations include fever, rash, swollen lymph nodes, headache, muscle pain and unusual weakness. Most patients have mild symptoms that last from 2 to 4 weeks. The source of the sudden outbreak in Europe and the United States is currently unknown and occurs mostly in homosexuals who have sex with men (MSM). Outbreaks of monkeypox virus infection in non-monkeypox endemic areas have received widespread attention and focus. We believe that a scientific response to the transmission route of monkeypox virus and, where necessary, vaccination of high-risk groups against the monkeypox smallpox will control infection in non-monkeypox endemic areas.


Assuntos
Exantema , Minorias Sexuais e de Gênero , Animais , Feminino , Masculino , Humanos , Homossexualidade Masculina , Europa (Continente)/epidemiologia , Surtos de Doenças , Febre
2.
Insect Mol Biol ; 18(1): 97-110, 2009 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-19196350

RESUMO

The insect digestive system is the first line of defence protecting cells and tissues of the body from a broad spectrum of toxins and antinutritional factors in its food. To gain insight into the nature and breadth of genes involved in adaptation to dietary challenge, a collection of 20 352 cDNAs was prepared from the midgut tissue of cowpea bruchid larvae (Callosobruchus maculatus) fed on regular diet and diets containing antinutritional compounds. Transcript responses of the larvae to dietary soybean cystatin (scN) were analysed using cDNA microarrays, followed by quantitative real-time PCR (RT-PCR) confirmation with selected genes. The midgut transcript profile of insects fed a sustained sublethal scN dose over the larval life was compared with that of insects treated with an acute high dose of scN for 24 h. A total of 1756 scN-responsive cDNAs was sequenced; these clustered into 967 contigs, of which 653 were singletons. Many contigs (451) did not show homology with known genes, or had homology only with genes of unknown function in a Blast search. The identified differentially regulated sequences encoded proteins presumptively involved in metabolism, structure, development, signalling, defence and stress response. Expression patterns of some scN-responsive genes were consistent in each larval stage, whereas others exhibited developmental stage-specificity. Acute (24 h), high level exposure to dietary scN caused altered expression of a set of genes partially overlapping with the transcript profile seen under chronic lower level exposure. Protein and carbohydrate hydrolases were generally up-regulated by scN whereas structural, defence and stress-related genes were largely down-regulated. These results show that insects actively mobilize genomic resources in the alimentary tract to mitigate the impact of a digestive protease inhibitor. The enhanced or restored digestibility that may result is possibly crucial for insect survival, yet may be bought at the cost of weakened response to other stresses.


Assuntos
Cistatinas/toxicidade , Sistema Digestório/metabolismo , Regulação da Expressão Gênica/efeitos dos fármacos , Glycine max/química , Gorgulhos/metabolismo , Animais , Perfilação da Expressão Gênica , Genes de Insetos/genética , Dados de Sequência Molecular , Extratos Vegetais/toxicidade , Gorgulhos/genética
3.
Insect Mol Biol ; 17(3): 235-45, 2008 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-18397276

RESUMO

Insects are capable of readjusting their digestive regimes in response to dietary challenge. Cowpea bruchids (Callosobruchus maculatus) strongly induce C. maculatus cathepsin B-like cysteine protease 1 (CmCatB1) transcripts when fed diet containing a soybean cysteine protease inhibitor soyacystatin N (scN). CmCatB1 shares significant sequence similarity with cathepsin B-like cysteine proteases. In this study, we isolated another cDNA, namely CmCatB2 that encodes a protein sequence otherwise identical to CmCatB1, but lacking a 70-amino-acid internal section. CmCatB1 and CmCatB2 probably resulted from alternate splicing events. Only the CmCatB1 transcript, however, exhibited differential expression in response to dietary scN. Further, this expression was only detectable in larvae, which is the developmental stage associated with food ingestion. The scN-activated and developmentally regulated CmCatB1 expression pattern suggests it may have a unique function in insect counter-defence against antinutritional factors. Heterologously expressed recombinant CmCatB1 protein exhibited enzymatic activity in a pH-dependent manner. Activity of the protein was inhibited by both the cysteine protease inhibitor E-64 and the cathepsin B-specific inhibitor CA-074, verifying its cathepsin B-like cysteine protease nature. Interestingly, the enzymatic activity was unaffected by the presence of scN. Together, we have provided functional evidence suggesting that CmCatB1 confers inhibitor-insensitive enzymatic activity to cowpea bruchids, which is crucial for insect survival when challenged by dietary protease inhibitors.


Assuntos
Catepsina B/metabolismo , Proteínas de Insetos/metabolismo , Insetos/enzimologia , Insetos/imunologia , Processamento Alternativo/efeitos dos fármacos , Sequência de Aminoácidos , Animais , Sequência de Bases , Catepsina B/química , Catepsina B/genética , Sequência Conservada , Cistatinas/farmacologia , Regulação da Expressão Gênica no Desenvolvimento/efeitos dos fármacos , Glicosilação/efeitos dos fármacos , Concentração de Íons de Hidrogênio/efeitos dos fármacos , Proteínas de Insetos/química , Proteínas de Insetos/genética , Insetos/genética , Isoenzimas/química , Isoenzimas/genética , Isoenzimas/metabolismo , Dados de Sequência Molecular , Proteínas Recombinantes/biossíntese , Proteínas de Soja/farmacologia , Especificidade por Substrato/efeitos dos fármacos
4.
Oncogene ; 25(15): 2137-47, 2006 Apr 06.
Artigo em Inglês | MEDLINE | ID: mdl-16288203

RESUMO

The spindle assembly checkpoint (SAC) guards against chromosomal mis-segregation and the emergence of aneuploidy. SAC in higher eukaryotes includes at least 10 proteins including MAD1-3, BUB1-3, and Msp1. A long-standing observation has been that rodent cells are more tolerant of microtubule toxins than primate cells indicating that SAC function is more relaxed in the former than the latter. Here, we report on an unexpected functional difference between the rodent and human MAD1 component of the respective SAC. Ectopic expression of human MAD1 in mouse and hamster cells corrected a relaxed SAC to a more stringent form. Our findings posit MAD1 as a species-specific determinant which influences the stringency of cellular response to microtubule depolymerization and spindle damage.


Assuntos
Proteínas de Ciclo Celular/metabolismo , Microtúbulos/metabolismo , Mitose , Proteínas Nucleares/metabolismo , Fuso Acromático , Sequência de Aminoácidos , Animais , Antineoplásicos/farmacologia , Células CHO/efeitos dos fármacos , Células CHO/metabolismo , Proteínas de Ciclo Celular/genética , Cricetinae , Células HeLa/efeitos dos fármacos , Células HeLa/metabolismo , Humanos , Neoplasias Pulmonares/metabolismo , Neoplasias Pulmonares/patologia , Camundongos , Microtúbulos/efeitos dos fármacos , Dados de Sequência Molecular , Células NIH 3T3/efeitos dos fármacos , Células NIH 3T3/metabolismo , Nocodazol/farmacologia , Proteínas Nucleares/genética , Ratos , Homologia de Sequência de Aminoácidos , Especificidade da Espécie
5.
Guang Pu Xue Yu Guang Pu Fen Xi ; 21(6): 814-8, 2001 Dec.
Artigo em Chinês | MEDLINE | ID: mdl-12958903

RESUMO

The interaction of deoxyribonucleic acid (DNA) and 3-amino-6-dimethylamino-2-methlphenazine hydrochloride (ZR) was investigated by UV spectrophotometric method in solution (pH 7.4). When DNA was added into ZR solution, the red color was observed, which indicated formation of the DNA-ZR complex. The maximum absorption of the complex was 520 nm with the apparent molar absorptivity of epsilon = 1.5 x 10(6) mol-1.L.cm-1. The maximum absorption of the complex was shifted 70 nm than with ZR. The maximum binding number is n = 303. The basic reaction conditions were investigated. It is found that sodium chloride concentration of the solution has significant effect on the sensitivity of DNA-ZR complex. The Scatchard model is appropriate in the treatment of data obtained here.


Assuntos
DNA/química , Fenazinas/química , Quelantes/química , Interações Medicamentosas , Humanos , Sondas Moleculares , Cloreto de Sódio/química , Espectrofotometria Ultravioleta
6.
FEBS Lett ; 486(2): 103-6, 2000 Dec 08.
Artigo em Inglês | MEDLINE | ID: mdl-11113447

RESUMO

Possible functions that have been proposed for the plant 1Cys-peroxiredoxin, include activity as a dormancy regulator and as an antioxidant. The transcript level of rice 1Cys-peroxiredoxin (R1C-Prx) rapidly decreased after imbibition of rice seeds, but the protein was detected for 15 days after imbibition. To investigate the function of this protein, we generated transgenic tobacco plants constitutively expressing the R1C-Prx gene. The transgenic R1C-Prx plants showed a germination frequency similar to control plants. However, the transgenic lines exhibited higher resistance against oxidative stress, suggesting that antioxidant activity may be its primary function.


Assuntos
Antioxidantes , Oryza/enzimologia , Peroxidases/fisiologia , Animais , Expressão Gênica , Germinação/fisiologia , Oryza/genética , Oryza/fisiologia , Estresse Oxidativo , Peroxidases/genética , Peroxirredoxinas , Plantas Geneticamente Modificadas , Plantas Tóxicas , Coelhos , Sementes/fisiologia , Nicotiana
7.
Plant Mol Biol ; 40(5): 825-34, 1999 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-10487217

RESUMO

A cDNA (C2C-Prx) corresponding to a 2Cys-peroxiredoxin (2Cys-Prx) was isolated from a leaf cDNA library of Chinese cabbage. The predicted amino acid sequence of C2C-Prx has 2 conserved cysteines and several peptide domains present in most of the 2Cys-Prx subfamily members. It shows the highest sequence homology to the 2Cys-Prx enzymes of spinach (88%) and Arabidopsis (86%). Southern analysis using the cDNA insert of C2C-Prx revealed that it consists of a small multigene family in Chinese cabbage genome. RNA blot analysis showed that the gene was predominantly expressed in the leaf tissue of Chinese cabbage seedlings, but the mRNA was generally expressed in most tissues of mature plant, except roots. The expression of C2C-Prx was slightly induced by treatment with H2O2 (100 microM) or Fe3+/O2/DTT oxidation system, but not by ABA (50 microM) or GA3 (10 microM). The C2C-Prx is encoded as a preprotein of 273 amino acids containing a putative chloroplast-targeting signal of 65 amino acids at its N-terminus. The N-terminally truncated recombinant protein (deltaC2C-Prx) migrates as a dimer in a non-reducing SDS-polyacrylamide gel and as a monomer in a reducing condition. The deltaC2C-Prx shows no immuno cross-reactivity to antiserum of the yeast thiol-specific antioxidant protein, and vice versa. The deltaC2C-Prx prevents the inactivation of glutamine synthetase and the DNA cleavage in the metal-catalyzed oxidation system. In the yeast thioredoxin system containing thioredoxin reductase, thioredoxin, and NADPH, the deltaC2C-Prx exhibits peroxidase activity on H2O2.


Assuntos
Brassica/enzimologia , Brassica/genética , Peroxidases/genética , Sequência de Aminoácidos , Animais , Arabidopsis/genética , Sequência de Bases , Clonagem Molecular , Sequência Conservada , Cisteína , Regulação da Expressão Gênica de Plantas , Glutamato-Amônia Ligase/metabolismo , Humanos , Cinética , Dados de Sequência Molecular , Oligodesoxirribonucleotídeos , Peroxidases/biossíntese , Peroxidases/química , Peroxirredoxinas , Alinhamento de Sequência , Homologia de Sequência de Aminoácidos , Spinacia oleracea/enzimologia
8.
Biochem Biophys Res Commun ; 258(3): 768-71, 1999 May 19.
Artigo em Inglês | MEDLINE | ID: mdl-10329461

RESUMO

A cDNA encoding a newly identified isotype of peroxiredoxin (Prx) was isolated from a Chinese cabbage flower bud cDNA library and designated CPrxII. Database searches using the predicted CPrxII amino acid sequence revealed no substantial homology to other proteins with the exception of the yeast type II Prx with which CPrxII shares 27.8% sequence identity. Recombinant CPrxII expressed in Escherichia coli was able to protect glutamine synthetase from inactivation in a metal-catalyzed oxidation system and to reduce H2O2 with electrons provided by thioredoxin. This specific antioxidant activity of CPrxII was about 6-fold higher than that of 2Cys-Prx of the same plant. In contrast to 2Cys-Prx, which is predominantly expressed in leaf tissue of cabbage seedlings, CPrxII is highly expressed in root tissue as revealed by Northern and Western blot analyses. The CPrxII gene exists as a small multigene family in the cabbage genome.


Assuntos
Brassica/genética , Isoenzimas/genética , Peroxidases/genética , Sequência de Aminoácidos , Brassica/enzimologia , Clonagem Molecular , DNA Complementar , Escherichia coli/genética , Isoenzimas/química , Isoenzimas/metabolismo , Dados de Sequência Molecular , Família Multigênica , Peroxidases/química , Peroxidases/metabolismo , Peroxirredoxinas , Proteínas Recombinantes/química , Proteínas Recombinantes/genética , Proteínas Recombinantes/metabolismo , Homologia de Sequência de Aminoácidos
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