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1.
Arch Virol ; 165(12): 2945-2951, 2020 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-33030572

RESUMO

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.


Assuntos
Doenças do Cão/virologia , Cães/virologia , Infecções por Parvoviridae/veterinária , Parvovirus Canino/isolamento & purificação , Animais , DNA Viral/química , DNA Viral/genética , Europa Oriental , Itália , Infecções por Parvoviridae/virologia , Parvovirus Canino/genética , Filogenia , Viagem
2.
J Mol Biol ; 210(1): 91-111, 1989 Nov 05.
Artigo em Inglês | MEDLINE | ID: mdl-2555523

RESUMO

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.


Assuntos
Rhinovirus/ultraestrutura , Sequência de Aminoácidos , Antivirais/metabolismo , Capsídeo , Cristalização , Humanos , Modelos Biológicos , Dados de Sequência Molecular , Estrutura Molecular , Receptores de Droga/metabolismo , Receptores de Droga/ultraestrutura , Rhinovirus/imunologia , Sorotipagem
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