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Volume 30, Number 8—August 2024
Dispatch

Characterization of Influenza D Virus Reassortant Strain in Swine from Mixed Pig and Beef Farm, France

Stéphane Gorin1, Gautier Richard1, Séverine Hervé, Eric Eveno, Yannick Blanchard, Agnès Jardin, Nicolas Rose, and Gaëlle SimonComments to Author 
Author affiliations: French Agency for Food, Environmental and Occupational Health & Safety, Ploufragan, France (S. Gorin, G. Richard, S. Hervé, E. Eveno, Y. Blanchard, N. Rose, G. Simon); CEVA Santé Animale, Libourne, France (A. Jardin)

Main Article

Figure 3

Alignments of hemagglutinin-esterase fusion protein sequences and structure prediction of the receptor-binding site of the influenza D virus strain recovered from swine in France. A) HEF sequence alignment and 2D structure prediction. From top to bottom: amino acid coordinates based on previously published research (9), amino acid coordinates based on GenBank MSAA and translation to protein, HEF domain based on previously published research (9), HEF sequence logo based on amino acid occurrence in the 151 HEF sequence alignment, HEF consensus sequence and percentage of amino occurrence in the 151 HEF sequence alignment, and representative HEF sequences from the D/660 lineage and their predicted secondary structures. Blue highlights indicate residues involved in α-helices and green highlights residues involved in β-strands. Red (A236V/A252V) and orange (R268K/R284K) underlines or arrows indicate unique mutations identified in D/swine/France/29-220655/2022. B) Predicted RBS structure of D/swine/France/29-220655/2022 compared with the closely related D/bovine/Italy/7368/2022. Blue colors on the protein 3D structures depict low hydrophobicity and red colors depict high hydrophobicity. HEF, hemagglutinin-esterase fusion; MSAA, multisequence alignment; RBS, receptor-binding site.

Figure 3. Alignments of hemagglutinin-esterase fusion protein sequences and structure prediction of the receptor-binding site of the influenza D virus strain recovered from swine in France. A) HEF sequence alignment and 2D structure prediction. From top to bottom: amino acid coordinates based on previously published research (9), amino acid coordinates based on GenBank MSAA and translation to protein, HEF domain based on previously published research (9), HEF sequence logo based on amino acid occurrence in the 151 HEF sequence alignment, HEF consensus sequence and percentage of amino occurrence in the 151 HEF sequence alignment, and representative HEF sequences from the D/660 lineage and their predicted secondary structures. Blue highlights indicate residues involved in α-helices and green highlights residues involved in β-strands. Red (A236V/A252V) and orange (R268K/R284K) underlines or arrows indicate unique mutations identified in D/swine/France/29-220655/2022. B) Predicted RBS structure of D/swine/France/29-220655/2022 compared with the closely related D/bovine/Italy/7368/2022. Blue colors on the protein 3D structures depict low hydrophobicity and red colors depict high hydrophobicity. HEF, hemagglutinin-esterase fusion; MSAA, multisequence alignment; RBS, receptor-binding site.

Main Article

References
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1These first authors contributed equally to this article.

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