Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 2 de 2
Filtrar
Más filtros











Base de datos
Intervalo de año de publicación
1.
Arch Virol ; 165(12): 2945-2951, 2020 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-33030572

RESUMEN

Minute virus of canines (MVC) belongs to the family Parvoviridae, genus Bocaparvovirus, and has been mainly described during enteritis episodes in young dogs. This study reports the characterization of four divergent MVC strains detected between 2012 and 2018, three of which were from dogs illegally imported into Italy, most probably from Eastern Europe, that cluster together phylogenetically but share low genetic similarity with the fourth MVC from an autochthonous dog and other available MVC sequences. Our data indicate that the introduction of genetically distinct MVC strains occurred through the illegal movement of dogs from a geographic area where a distinct MVC lineage was most likely circulating. Enforced surveillance of MVC in the dog population of Eastern Europe and its neighboring countries may shed light on, and eventually trace back to, illegal animal movements.


Asunto(s)
Enfermedades de los Perros/virología , Perros/virología , Infecciones por Parvoviridae/veterinaria , Parvovirus Canino/aislamiento & purificación , Animales , ADN Viral/química , ADN Viral/genética , Europa Oriental , Italia , Infecciones por Parvoviridae/virología , Parvovirus Canino/genética , Filogenia , Viaje
2.
J Mol Biol ; 210(1): 91-111, 1989 Nov 05.
Artículo en Inglés | MEDLINE | ID: mdl-2555523

RESUMEN

The structure of human rhinovirus 1A (HRV1A) has been determined to 3.2 A resolution using phase refinement and extension by symmetry averaging starting with phases at 5 A resolution calculated from the known human rhinovirus 14 (HRV14) structure. The polypeptide backbone structures of HRV1A and HRV14 are similar, but the exposed surfaces are rather different. Differential charge distribution of amino acid residues in the "canyon", the putative receptor binding site, provides a possible explanation for the difference in minor versus major receptor group specificities, represented by HRV1A and HRV14, respectively. The hydrophobic pocket in VP1, into which antiviral compounds bind, is in an "open" conformation similar to that observed in drug-bound HRV14. Drug binding in HRV1A does not induce extensive conformational changes, in contrast to the case of HRV14.


Asunto(s)
Rhinovirus/ultraestructura , Secuencia de Aminoácidos , Antivirales/metabolismo , Cápside , Cristalización , Humanos , Modelos Biológicos , Datos de Secuencia Molecular , Estructura Molecular , Receptores de Droga/metabolismo , Receptores de Droga/ultraestructura , Rhinovirus/inmunología , Serotipificación
SELECCIÓN DE REFERENCIAS
DETALLE DE LA BÚSQUEDA