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1.
Sci Rep ; 9(1): 12616, 2019 08 30.
Artigo em Inglês | MEDLINE | ID: mdl-31471549

RESUMO

Antimicrobial resistance (AMR) is now a major global problem largely resulting from the overuse of antibiotics in humans and livestock. In some AMR bacteria, resistance is encoded by conjugative plasmids expressing sex-pili that can readily spread resistance through bacterial populations. The aim of this study was to use sex pilus-specific (SPS) phage to reduce the carriage of AMR plasmids. Here, we demonstrate that SPS phage can kill AMR Escherichia coli and select for AMR plasmid loss in vitro. For the first time, we also demonstrate that SPS phage can both prevent the spread of AMR Salmonella Enteritidis infection in chickens and shift the bacterial population towards antibiotic sensitivity.


Assuntos
Infecções Bacterianas/genética , Bacteriófagos/genética , Infecções por Escherichia coli/virologia , Doenças das Aves Domésticas/virologia , Animais , Antibacterianos/farmacologia , Infecções Bacterianas/tratamento farmacológico , Infecções Bacterianas/microbiologia , Infecções Bacterianas/virologia , Bacteriófagos/crescimento & desenvolvimento , Galinhas/microbiologia , Farmacorresistência Bacteriana Múltipla/genética , Escherichia coli/efeitos dos fármacos , Escherichia coli/patogenicidade , Infecções por Escherichia coli/tratamento farmacológico , Infecções por Escherichia coli/genética , Infecções por Escherichia coli/microbiologia , Pili Sexual/efeitos dos fármacos , Pili Sexual/genética , Plasmídeos/genética , Doenças das Aves Domésticas/tratamento farmacológico , Doenças das Aves Domésticas/genética , Doenças das Aves Domésticas/microbiologia , Salmonella enteritidis/efeitos dos fármacos , Salmonella enteritidis/patogenicidade
2.
Gene ; 529(2): 345-50, 2013 Oct 25.
Artigo em Inglês | MEDLINE | ID: mdl-23954254

RESUMO

Prion diseases are a group of human and animal neurodegenerative disorders caused by the deposition of an abnormal isoform prion protein (PrP(Sc)) encoded by a single copy prion protein gene (PRNP). Prion disease has been reported in many herbivores but not in Equus and the species barrier might be playing a role in resistance of these species to the disease. Therefore, analysis of genotype of prion protein (PrP) in these species may help understand the transmission of the disease. Xiji donkey is a rare species of Equus not widely reared in Ningxia, China, for service, food and medicine, but its PRNP has not been studied. Based on the reported PrP sequence in GenBank we designed primers and amplified, cloned and sequenced the PRNP of Xiji donkey. The sequence analysis showed that the Xiji donkey PRNP was consisted of an open reading frame of 768 nucleotides encoding 256 amino acids. Amino acid residues unique to donkey as compared with some Equus animals, mink, cow, sheep, human, dog, sika deer, rabbit and hamster were identified. The results showed that the amino acid sequence of Xiji donkey PrP starts with the consensus sequence MVKSH, with almost identical amino acid sequence to the PrP of other Equus species in this study. Amino acid sequence analysis showed high identity within species and close relation to the PRNP of sika deer, sheep, dog, camel, cow, mink, rabbit and hamster with 83.1-99.7% identity. The results provided the PRNP data for an additional Equus species, which should be useful to the study of the prion disease pathogenesis, resistance and cross species transmission.


Assuntos
Equidae/genética , Príons/genética , Motivos de Aminoácidos , Sequência de Aminoácidos , Animais , China , Clonagem Molecular , Dados de Sequência Molecular , Filogenia , Príons/química , Análise de Sequência de DNA
3.
J Mol Neurosci ; 51(1): 219-24, 2013 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-23715697

RESUMO

Prion diseases characterize a category of fatal neurodegenerative diseases. Although reports have increasingly shown that oxidative stress plays an important role in the progression of prion diseases, little is known about whether oxidative stress is a cause or a consequence of a prion disease. The mechanism of prion disease development also remains unclear. The purpose of this study was to investigate three things: the possible mechanisms of neuron cell damage, the conformation of anti-protease K (PK) PrP(Sc), and the role of oxidative stress in the progression of prion diseases. The study results demonstrated that normal PrP(C) transformed into a PK-resistant protein under oxidative stress in the presence of PrP106-126. Further, the protein misfolding cyclic amplification procedure may have accelerated this process. Mitochondrial damage and dysfunction in prion disease progression were also observed in this study. Our results suggested that neuron cell damage, and particularly mitochondrial damage, was induced by oxidative stress. This damage may be the initial cause of a given prion disease.


Assuntos
Endopeptidase K/metabolismo , Mitocôndrias/metabolismo , Neurônios/metabolismo , Estresse Oxidativo , Fragmentos de Peptídeos/metabolismo , Doenças Priônicas/metabolismo , Príons/metabolismo , Linhagem Celular Tumoral , Humanos , Ferro/farmacologia , Mitocôndrias/ultraestrutura , Neurônios/efeitos dos fármacos , Fragmentos de Peptídeos/farmacologia , Príons/farmacologia , Dobramento de Proteína
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