Expression, purification and characterization of neuraminidase from avian flu virus (H5N1) in Pichia pastoris ...
The avian influenza A (H5N1) virus is highly contagious in both wild bird populations and domestic poultry flocks in various continents posing a serious threat to human health. Previous studies revealed that the major surface glycoprotein of the virion namely, neuraminidase (NA) plays an important r...
| Main Author: | |
|---|---|
| Format: | Dataset |
| Language: | unknown |
| Published: |
Chulalongkorn University
2011
|
| Subjects: | |
| Online Access: | https://dx.doi.org/10.14457/cu.the.2011.1718 http://doi.nrct.go.th/?page=resolve_doi&resolve_doi=10.14457/CU.the.2011.1718 |
| Summary: | The avian influenza A (H5N1) virus is highly contagious in both wild bird populations and domestic poultry flocks in various continents posing a serious threat to human health. Previous studies revealed that the major surface glycoprotein of the virion namely, neuraminidase (NA) plays an important role in viral replication and infection. The NA is a mushroom-shaped spike protein composed of a single polypeptide chain with three distinct domains: head domain containing the enzyme active site, a highly variable stalk region, and N- terminal signal anchor domain by which the enzyme is embedded in the viral envelope. The function is to hydrolyze the terminal sialic acids of sialoglycans and promotes the release of progeny virus from an infected host cell by destroying receptors on the host cell and the virus itself. The inhibition of NA activity will limit the spread of viral infection thereby suppressing the onset of disease. In this research, the full length and globular head domain of NA were expressed in ... |
|---|