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Fouchier H5N1 Transmission Paper Published
Recombinomics Commentary 12:45
June 22, 2012

The only amino acid substitution detected upon repeated passage of both A/H5N1wildtype and A/H5N1HA Q222L,G224S PB2 E627K was T156A

T156A was detected in 89% of the A/H5N1HA Q222L,G224S PB2 E627K sequences after 10 passages, and the other 11% of sequences possessed the substitution N154K, which removes the same potential N-linked glycosylation site in HA.

The above comments from the Fouchier Science paper highlight the importance of the abolition of the glycosylation of position 158 (H3 numbering), which was identified during ferret passage of clade 2.3 (
A/Indonesia/5/2005) above (in wild type of modified H5), which matches the Kawaoka result using clade 1 (A/Vietnam/1203/2004).  Moreover, the abolition was also present in the clade 2.2 H5 (A/egret/Egypt/1162/2006) used in the Donis (CDC) study.

The publication of the Fouchier paper also confirmed media reports on the recipe for H5N1, which involved the two most widely discussed receptor binding domain changes (Q226L and G228S) as well as the most widely discussed PB2 change (E627K) on a clade 2.1 background which is passaged in ferrets 10X.

The publication of the Science and Nature papers raising serious competency issues with regard to the NSABB board, which should resign en mass to restore credibility to that agency.

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