Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 4 de 4
Filtrar
Mais filtros








Base de dados
Intervalo de ano de publicação
1.
J Infect Dis ; 228(2): 149-159, 2023 07 14.
Artigo em Inglês | MEDLINE | ID: mdl-36861215

RESUMO

Omicron and its subvariants have steadily gained greater capability of immune escape compared to other variants of concern, resulting in an increased incidence of reinfections even among vaccinated individuals. We evaluated the antibody response to Omicron BA.1, BA.2, and BA.4/5 in US military members vaccinated with the primary 2-dose series of Moderna mRNA-1273 in a cross-sectional study. While nearly all vaccinated participants had sustained spike (S) IgG and neutralizing antibodies (ND50) to the ancestral strain, only 7.7% participants had detectable ND50 to Omicron BA.1 at 8 months postvaccination. The neutralizing antibody response to BA.2 and BA.5 was similarly reduced. The reduced antibody neutralization of Omicron correlated with the decreased antibody binding to the receptor-binding domain. The participants' seropositivity to the nuclear protein positively correlated with ND50. Our data emphasizes the need for continuous vigilance in monitoring for emerging variants and the need to identify potential alternative targets for vaccine design.


Assuntos
COVID-19 , Militares , Humanos , Vacina de mRNA-1273 contra 2019-nCoV , Formação de Anticorpos , Estudos Transversais , SARS-CoV-2/genética , Anticorpos Neutralizantes , Anticorpos Antivirais
2.
Microbiol Spectr ; 11(1): e0228622, 2023 02 14.
Artigo em Inglês | MEDLINE | ID: mdl-36519888

RESUMO

Rapid coronavirus disease 2019 (COVID-19) antigen tests can be used to aid in quickly identifying positive cases, which can help mitigate the spread of COVID-19 infection. Using previously characterized Omicron-positive severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), non-Omicron-positive SARS-CoV-2, and negative samples, we evaluated five brands of at-home rapid COVID-19 antigen tests (On/Go at-home COVID-19 rapid antigen self-test, iHealth COVID-19 antigen rapid test, QuickVue SARS antigen test, Abbott BinaxNOW COVID-19 card home test, and InBios SCoV-2 Ag detect rapid self-test). Our results showed that these rapid tests had similar levels of sensitivity to Omicron and non-Omicron variants (On/Go, 76.4% and 71.0%; iHealth, 73.0% and 71.0%; QuickVue, 84.3% and 74.3%; BinaxNOW, 69.7% and 71.0%; and InBios, 66.3% and 64.5%, respectively). In conclusion, rapid COVID-19 antigen tests can continue to be used as part of public health measures to combat the spread of the Omicron variant, as their sensitivity was not significantly affected. IMPORTANCE The emergence of the Omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is due to mutations as part of the virus evolution process. These mutations might affect the sensitivity of diagnostic tests that are currently being used to detect the virus. Because rapid coronavirus disease 2019 (COVID-19) antigen tests are commonly used in the general population, it is important to assess their performance in detecting the Omicron variant. Here, we compared the performance of five brands of rapid tests against Omicron and non-Omicron variants using nasopharyngeal swab samples in viral transport media. Our result found no difference in their performance, suggesting no reduction in sensitivity when used to detect the Omicron variant.


Assuntos
COVID-19 , Humanos , COVID-19/diagnóstico , SARS-CoV-2/genética , Mutação , Saúde Pública
3.
J Agric Food Chem ; 63(42): 9315-22, 2015 Oct 28.
Artigo em Inglês | MEDLINE | ID: mdl-26395320

RESUMO

This study was to create an ω-3 (n-3) fatty-acid-enriched chicken product using defatted green microalgae (DGA, Nannochloropsis oceanica) biomass out of biofuel research. Hatching Ross broiler chicks were fed a corn-soybean meal diet containing 0 (control), 2, 4, 8, or 16% DGA for 6 weeks (n = 6 cages/diet). The DGA inclusion resulted in a linear (p < 0.001) increase in total n-3 fatty acids, eicosapentaenoic acid (EPA), and docosahexaenoic acid (DHA) in plasma, liver, breast, and thigh at weeks 3 and 6. The increase in the breast EPA + DHA by the 16% DGA diet reached 60-fold (p < 0.0001) over the control. The 8 and 4% DGA diets elevated (p < 0.05) liver mRNA levels of Δ-9 (88%) and Δ-6 (96) desaturases. In conclusion, 8-16% of the DGA can be added in diets for broilers to produce a n-3 fatty-acid-enriched chicken meat.


Assuntos
Galinhas/metabolismo , Ácidos Graxos Ômega-3/metabolismo , Carne/análise , Microalgas/química , Ração Animal/análise , Animais , Ácidos Graxos Ômega-3/análise , Fígado/metabolismo , Microalgas/metabolismo
4.
Nutr Res ; 31(7): 544-54, 2011 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-21840471

RESUMO

The activity of lysine α-ketoglutarate reductase (LKR), the initial enzyme in the principal pathway of lysine catabolism, is a primary determinant of whole-body lysine status. Past research indicated that LKR activity was predominantly hepatic; recent in vivo data suggest that other tissues can also catabolize lysine. The hypothesis of this investigation was that lysine catabolism takes place in extrahepatic tissues in pigs and that the enzymes involved may be subject to inhibition or activation. Using mitochondria from various tissues of market-age pigs, the activities of LKR and saccharopine dehydrogenase were measured. Liver mitochondria had the highest LKR activity, and the enzyme was subject to substrate inhibition. Mitochondria from the muscle, kidney, heart, and intestinal epithelial cells all had measurable LKR activity. The LKR activity was significantly inhibited by a variety of compounds including saccharopine, α-aminoadipate, α-ketoadipate, 5-hydroxy-l-lysine, and several metals. Oxidation of (14)C-lysine to (14)CO(2) was demonstrated in mitochondria isolated from the liver, muscle, and intestinal epithelial cells. Western blotting confirmed the presence of the α-aminoadipate δ-semialdehyde synthase protein in some extrahepatic tissues. These data show a significant capacity for lysine degradation in these extrahepatic tissues, most notably in cells of the intestine and muscle. These tissues should be considered important contributors to whole-body lysine catabolism.


Assuntos
Mucosa Intestinal/enzimologia , Cetona Oxirredutases/metabolismo , Rim/enzimologia , Fígado/enzimologia , Lisina/metabolismo , Músculo Esquelético/enzimologia , Animais , Western Blotting , Inibidores Enzimáticos/farmacologia , Cetona Oxirredutases/antagonistas & inibidores , Mitocôndrias/enzimologia , Miocárdio/enzimologia , Oxirredução , Sacaropina Desidrogenases/metabolismo , Suínos
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA