Last year a mutation in the HA gene of the 2009 H1N1 influenza virus was identified in isolates from patients with severe disease. At the time I concluded that the emergence of this change was not a concern. Recently the Norwegian Institute of Public Health reported that the mutation, which causes a change from the amino …
Download: .wmv (386 MB) | .mp4 (131 MB) There are some errors in this lecture – I’ll correct them during the next session. Visit the virology W3310 home page for a complete list of course resources.
Hosts: Vincent Racaniello, Dickson Despommier, and Alan Dove On episode #62 of the podcast This Week in Virology, Vincent, Dickson, and Alan discuss STEP HIV-1 vaccine failure caused by the adenovirus vector, presence of West Nile virus in kidneys for years after initial infection, adaptation of the influenza viral RNA polymerase for replication in human …
The Norwegian Institute of Public Health recently identified a mutation in 2009 H1N1 influenza virus isolated from two patients who died and one with severe disease. It has been suggested that this mutation, which causes a change from the amino acid aspartic acid to glycine at position 225 of the viral HA protein (D225G), could …
The D225G change in 2009 H1N1 influenza virus is not a concern Read More »
As we discussed previously, attachment of all influenza A virus strains to cells requires sialic acids. However, there are a number of chemically different forms of sialic acids, and influenza virus strains vary in their affinity for them. These differences may determine which animal species can be infected. In the example shown below, sialic acid …
Influenza virus attachment to cells: role of different sialic acids Read More »
