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1.
Artículo en Inglés | MEDLINE | ID: mdl-20183493

RESUMEN

Two bacteriophages, phi6 and phi8, were investigated as potential surrogates for H5N1 highly pathogenic avian influenza virus in persistence and chlorine inactivation studies in water. In the persistence studies, phi6 and phi8 remained infectious at least as long as the H5N1 viruses at both 17 and 28 degrees C in fresh water, but results varied in salinated water. The bacteriophage phi6 also exhibited a slightly higher chlorine resistance than that of the H5N1 viruses. Based upon these findings, the bacteriophages may have potential for use as surrogates in persistence and inactivation studies in fresh water.


Asunto(s)
Bacteriófago phi 6/efectos de los fármacos , Cloro/toxicidad , Subtipo H5N1 del Virus de la Influenza A , Inactivación de Virus/efectos de los fármacos , Microbiología del Agua , Bacteriófago phi 6/fisiología , Salinidad , Temperatura
2.
J Cell Biol ; 147(3): 671-82, 1999 Nov 01.
Artículo en Inglés | MEDLINE | ID: mdl-10545509

RESUMEN

Studies on the virus-cell interactions have proven valuable in elucidating vital cellular processes. Interestingly, certain virus-host membrane interactions found in eukaryotic systems seem also to operate in prokaryotes (Bamford, D.H., M. Romantschuk, and P. J. Somerharju, 1987. EMBO (Eur. Mol. Biol. Organ.) J. 6:1467-1473; Romantschuk, M., V.M. Olkkonen, and D.H. Bamford. 1988. EMBO (Eur. Mol. Biol. Organ.) J. 7:1821-1829). straight phi6 is an enveloped double-stranded RNA virus infecting a gram-negative bacterium. The viral entry is initiated by fusion between the virus membrane and host outer membrane, followed by delivery of the viral nucleocapsid (RNA polymerase complex covered with a protein shell) into the host cytosol via an endocytic-like route. In this study, we analyze the interaction of the nucleocapsid with the host plasma membrane and demonstrate a novel approach for dissecting the early events of the nucleocapsid entry process. The initial binding of the nucleocapsid to the plasma membrane is independent of membrane voltage (DeltaPsi) and the K(+) and H(+) gradients. However, the following internalization is dependent on plasma membrane voltage (DeltaPsi), but does not require a high ATP level or K(+) and H(+) gradients. Moreover, the nucleocapsid shell protein, P8, is the viral component mediating the membrane-nucleocapsid interaction.


Asunto(s)
Bacteriófago phi 6/metabolismo , Membrana Celular/fisiología , Endocitosis , Nucleocápside/metabolismo , Pseudomonas/virología , Adenosina Trifosfato/metabolismo , Adsorción/efectos de los fármacos , Bacteriófago phi 6/efectos de los fármacos , Bacteriófago phi 6/inmunología , Bacteriófago phi 6/ultraestructura , Membrana Celular/efectos de los fármacos , Membrana Celular/ultraestructura , Transporte de Electrón/efectos de los fármacos , Endocitosis/efectos de los fármacos , Concentración de Iones de Hidrógeno , Potenciales de la Membrana/efectos de los fármacos , Microscopía Electrónica , Pruebas de Neutralización , Nucleocápside/efectos de los fármacos , Nucleocápside/inmunología , Nucleocápside/ultraestructura , Potasio/antagonistas & inhibidores , Potasio/metabolismo , Inhibidores de la Bomba de Protones , Bombas de Protones/metabolismo , Fuerza Protón-Motriz/efectos de los fármacos , Pseudomonas/citología , Pseudomonas/metabolismo , Pseudomonas/ultraestructura , Esferoplastos/citología , Esferoplastos/metabolismo , Esferoplastos/ultraestructura , Esferoplastos/virología , Temperatura , Factores de Tiempo , Desacopladores/farmacología , Proteínas Virales/inmunología , Proteínas Virales/metabolismo
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