AlaskaDenise
In Memoriam
Re: Discussion: Low-risk bird flu found in Ill. wild ducks-USDA
1918 H1N1 accomplished the same objective (high volume cleavage) another way - a mutation (on the NA I believe) that caused it to bind with the plaminogen (enzyme in all blood), so anywhere the blood flowed the virus could cleave! Same result, different mechanism......very high path.
see http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=33880
Mamabird said:.......Please be aware that the HA segment of the 1918 H1N1 virus did not contain mutliple basic amino acids at the cleavage site, at least all the sequences that we have would indicate that, and none of the later isolates had anything unusual at the cleavage site.....
1918 H1N1 accomplished the same objective (high volume cleavage) another way - a mutation (on the NA I believe) that caused it to bind with the plaminogen (enzyme in all blood), so anywhere the blood flowed the virus could cleave! Same result, different mechanism......very high path.
see http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=33880
.In a series of experiments confirming and synthesizing 25 years of experimental data (2?4), Goto and Kawaoka (1) demonstrate specifically how the neuraminidase (NA) protein of influenza A/WSN/33 (H1N1), a curious variant of the first human influenza virus ever isolated, mediates hemagglutinin (HA) cleavage. Goto and Kawaoka (1) provide evidence for a model whereby the NA of WSN/33 directly binds plasminogen, sequestering it for cleavage activation. Subsequently, active plasmin cleaves and activates influenza hemagglutinin. Being able to sequester plasminogen for hemagglutinin cleavage allows the influenza virus to infect cells other than its usual targets.
Last edited: