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1.
Journal of Veterinary Science ; : 219-222, 2012.
Artigo em Inglês | WPRIM | ID: wpr-65173

RESUMO

Reports of influenza A virus infections in dogs has received considerable attention from veterinarians, virologists, and epidemiologists. Interaction between influenza viral hemagglutinin and cell oligosaccharides containing sialic acid residues results in infection. Sialic acids have an alpha-2,3-linkage to the penultimate galactose in the avian influenza virus receptor and an alpha-2,6-linkage in the human receptor. To date, there are no detailed data on the tissue distribution or histological features of either type of sialic acid-linked influenza virus receptors in beagle dogs, which are common laboratory animals and pets. We conducted the current study to visualize the in situ tissue distribution of both sialic acid-linked influenza virus receptors in various organs of beagle dogs using Maackia amurensis lectin II and Sambucus nigra agglutinin. Both alpha-2,3- and alpha-2,6-sialic acid-linked receptors were detected in the endothelial cells of the respiratory tract and other organs. Endothelial cells of most gastrointestinal organs were negative for alpha-2,3-sialic acid-linked receptors in the dogs. Our results suggested that these canine organs may be affected by influenza virus infection. The findings from our study will also help evaluate the occurrence and development of influenza virus infections in dogs.


Assuntos
Animais , Feminino , Masculino , Doenças do Cão/metabolismo , Cães/metabolismo , Virus da Influenza A Subtipo H5N1/metabolismo , Maackia/química , Ácido N-Acetilneuramínico/metabolismo , Especificidade de Órgãos , Infecções por Orthomyxoviridae/metabolismo , Lectinas de Plantas/metabolismo , Receptores de Superfície Celular/análise , Receptores Virais/análise , Sambucus nigra/química
2.
Journal of Veterinary Science ; : 293-301, 2002.
Artigo em Inglês | WPRIM | ID: wpr-148810

RESUMO

Lectins are glycoproteins that specifically bind carbohydrate structures and may participate in the biodefense mechanisms of fish. In this study, the binding of three lectins, Dolichos biflorus agglutinin (DBA), soybean agglutinin (SBA), Bandeiraea simplicifolia BS-1 (isolectin B4), Triticum vulgaris (WGA), Arachis hypogaea (PNA) and Ulex europaeus (UEA-I) were studied in the gill, liver, intestine, kidney, heart, and spleen of the flat fish Paralichthys olivaceus. DBA was detected in intestinal mucous cells, as well as in gill epithelial and mucous cells. It was weakly detected in renal tubule epithelial cells and in bile duct epithelial cells. The strong SBA staining was seen in the intestinal club cells, in bile duct epithelial cells and renal tubule epithelial cells. There were intense positive reactions for isolectin B4 in gill epithelial and mucous cells, and the strong isolectin B4 staining was seen in epithelial cells of the bile duct and intestine. The strong WGA staining was seen in the gill mucosal cells, sinusoid, renal tubule epithelial cells and mucosal cells of the intestine. UEA-I was detected in the gill epithelial and mucosal cells, bile duct epithelial cells and renal tubular epithelial cells. These results suggest that the six lectins examined were localized in the covering epithelia of the various organs of the flat fish and they may participate in the biodefense mechanism of the intra body surface in which is exposed to various antigens.


Assuntos
Animais , Células Epiteliais/metabolismo , Linguados/metabolismo , Histocitoquímica/veterinária , Lectinas/metabolismo , Muco/metabolismo , Aglutinina de Amendoim/metabolismo , Lectinas de Plantas/metabolismo , Proteínas de Soja/metabolismo , Aglutininas do Germe de Trigo/metabolismo
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