Novel avian influenza H7N3 strain outbreak, British Columbia - PubMed (original) (raw)

. 2004 Dec;10(12):2192-5.

doi: 10.3201/eid1012.040743.

Caroline R Astell, Malachi Griffith, Shaun M Coughlin, Michelle Moksa, Thomas Zeng, Duane E Smailus, Robert A Holt, Steven Jones, Marco A Marra, Martin Petric, Mel Krajden, David Lawrence, Annie Mak, Ron Chow, Danuta M Skowronski, S Aleina Tweed, SweeHan Goh, Robert C Brunham, John Robinson, Victoria Bowes, Ken Sojonky, Sean K Byrne, Yan Li, Darwyn Kobasa, Tim Booth, Mark Paetzel

Affiliations

Novel avian influenza H7N3 strain outbreak, British Columbia

Martin Hirst et al. Emerg Infect Dis. 2004 Dec.

Abstract

Genome sequences of chicken (low pathogenic avian influenza [LPAI] and highly pathogenic avian influenza [HPAI]) and human isolates from a 2004 outbreak of H7N3 avian influenza in Canada showed a novel insertion in the HA0 cleavage site of the human and HPAI isolate. This insertion likely occurred by recombination between the hemagglutination and matrix genes in the LPAI virus.

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Figures

Figure 1

Figure 1

Alignment of the hemagglutinin cleavage region from four isolates of Fraser Valley H7N3 virus. A/Chicken/Canada/AVFV1/04 is designated AVFV1; A/Chicken/Canada/AVFV2/04 is designated AVFV2; A/Canada/444/04 (human) is Hu444, and A/Canada/504/04 (human) is Hu504). A 7–amino-acid (aa) insertion associated with the AVFV2 isolate and both human isolates is shown at aa 338.

Figure 2

Figure 2

A homology model of the human A/Canada/504/04 (Hu504) hemagglutinin precursor (HA0) trimer based on the crystal structure of the human strain CV-1 HA0 (PDB: 1HA0) sequence identity 49.9%. A) Molecule A is shown as a green ribbon diagram; molecules B and C are shown in blue and yellow molecular surfaces, respectively. The 8–amino-acid (aa) sequence 335-342 (NPKQAYQK) is shown in red. B) A close up of this region located between molecules A (in green ribbon) and molecule C (in yellow surface). This 8-aa sequence forms a loop, which bumps into the adjoining molecule before energy minimization (gray). Shown in red is the loop after energy minimization, which results in the cleavage site's being pushed out slightly. Shown in blue is the corresponding region for the template structure (PDB code 1HA0). The side chains for arginine 343 and arginine 346 (–1 residue) are shown in stick form. (Since the preparation of this manuscript, the structure of an H7 HA protein has been reported [_12_]).

Figure A1

Figure A1

Complete nucleotide (A) and protein (B) alignments from the 5 isolates sequenced in this study. The alignments were generated by ClustalX (1.82) (

http://www.embl.de/\~chenna/clustal/darwin/

). [A/Canada/AVFV1/04 (environmental) is designated as chicken_A; A/Chicken/Canada/AVFV2/04 is designated as chicken_B; A/Canada/444/04 (human) is human_A and A/Canada/504/04 (human) is human_B. Full sequenced segments for chicken_D and chicken_E, not described in the text, are included for completeness.

Figure A2

Figure A2

Phylogenetic tree of isolates described in the text with 65 full-length H7 HA gene segments present in GenBank. The tree was generated with nucleotide sequences by the neighbor-joining method in Bonsai (1.1.4.) (

http://calliope.gs.washington.edu/software/

). Corrected distance estimate is indicated by the scale bar. The H7N3 avian influenza isolates reported in this article are at the bottom of the tree.

Figure A3

Figure A3

A structure-based sequence alignment of the influenza A virus hemagglutinin precursor protein from human A/Canada/504/04 (Hu504) with that of the hemagglutinin precursor protein (HA0) from influenza A virus, human strain CV-1 whose structure was solved by Wiley and colleagues in 1998 (PDBcode 1HAO) (22). The alignment shows 49.9% identity in sequence. Insertions and deletions are highlighted in grey and nonconservative mutations are shown in yellow. Conserved cysteines are boxed. The glycosylated aparagines which are conserved are boxed with thin lines; the glycosylated asparagines that are not conserved are boxed with thick lines.

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References

    1. Garcia M, Crawford JM, Latimer JW, Rivera-Cruz MVZE, Perdue ML. Heterogeneity in the hemagglutinin gene and emergence of the highly pathogenic phenotype among recent H5N2 avian influenza viruses from Mexico. J Gen Virol. 1996;77:1493–504. 10.1099/0022-1317-77-7-1493 - DOI - PubMed
    1. Perdue M, Crawford J, Garcia M, Latimer JE, Swayne D. Occurrence and possible mechanisms of cleavage site insertions in the avian influenza hemagglutinin gene. Swayne DE, Slemons RD, editors. Proceedings of the Fourth International Symposium on Avian Influenza. Kennett Square (PA): American Association of Avian Pathologists; 1998. p. 182–93.
    1. Rott R. The pathogenic determinant of influenza virus. Vet Microbiol. 1992;33:303–10. 10.1016/0378-1135(92)90058-2 - DOI - PubMed
    1. Stieneke Grober A, Vey M, Angliker H, Shaw E, Thomas G, Roberts C, et al. Influenza virus hemagglutinin with multibasic cleavage site is activated furin, a subtilisin-like endoprotease. EMBO J. 1992;11:2407–14. - PMC - PubMed
    1. Steinhauer DA. Role of hemagglutinin cleavage for the pathogenicity of influenza virus. Virology. 1999;258:1–20. 10.1006/viro.1999.9716 - DOI - PubMed

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