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Volume 12, Number 6—June 2006

Perspective

Host Range Restriction and Pathogenicity in the Context of Influenza Pandemic

Gabriele Neumann* and Yoshihiro Kawaoka*†‡Comments to Author 
Author affiliations: *University of Wisconsin-Madison, Madison, USA; †University of Tokyo, Tokyo, Japan; ‡Japan Science and Technology Agency, Saitama, Japan

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Table

Comparison of the hemagglutinin (HA) cleavage sites of highly pathogenic avian influenza viruses and their nonpathogenic predecessors

Isolate Type Amino acid sequence* Reference
A/chicken/Pennsylvania/1/83 (H5N2) Avirulent P Q - - - - - - - - - - - K K K R/ G L F (36)
A/chicken/Pennsylvania/1370/83 (H5N2) Virulent P Q - - - - - - - - - - - K K K R/ G L F† (36)
A/chicken/Mexico/31381-7/94 (H5N2) Avirulent P Q - - - - - - - - - - - R E T R/ G L F (37)
A/chicken/Queretaro/14588-19/95 (H5N2) Virulent P Q - - - - - - - - - R K R K T R/ G L F (37)
A/turkey/Italy/99 (H7N1) consensus Avirulent P E I P K G - - - - - - - - - - R/ G L F (38)
A/turkey/Italy/99 (H7N1) consensus Virulent P E I P K G - - - - - - S R V R R/ G L F (38)
A/chicken/Chile/176822/02 (H7N3) Avirulent P E K P K - - - - - - - - - - T R/ G L F (39)
A/chicken/Chile/4957/02 (H7N3) Virulent P E K P K T C S P L S R C R K T R/ G L F (39)
A/chicken/Chile/4322/02 (H7N3) Virulent P E K P K T C S P L S R C R E T R/ G L F (39)
Isolate CN6/04 Avirulent P E N P K - - - - - - - - - - T R/ G L F (40)
A/chicken/BC/CN12/04(H7N3) Virulent P E N P K - - --Q A Y Q K R M T R/ G L F (40)
A/chicken/BC/NS1337-1/04 (H7N3) Virulent P E N P K - - - Q A Y K K R M T R/ G L F (40)
A/chicken/BC/NS-1319-2/04(H7N3) Virulent P E N P K - - - Q A Y H K R M T R/ G L F (40)
A/chicken/BC/CN7-3/04 (H7N3) Virulent P E N P K - - - Q A Y R K R M T R/ G L F (40)
A/chicken/BC/NS-1390-2/04(H7N3) Virulent P E N P K - - - Q A H Q K R M T R/ G L F (40)
A/chicken/BC/NS-2035-12/04(H7N3) Virulent P E N P K - - - Q A C Q K R M T R/ G L F (40)

*HA cleavage sites are indicated by /. For sequence variants, the amino acids that differ from most sequences found are underlined.
†HA cleavability was enhanced by a single amino acid substitution that abrogated glycosylation near the HA cleavage site.

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