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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 multi-sequence alignment 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. B) Predicted RBS structure of D/swine/France/29-220655/2022 compared with the closely related D/bovine/Italy/7368/2022. Blue text indicates low hydrophobicity and red text high hydrophobicity. Blue highlights indcate 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. HEF, hemagglutinin-esterase fusion; MSAA, multi-sequence 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 multi-sequence alignment 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. B) Predicted RBS structure of D/swine/France/29-220655/2022 compared with the closely related D/bovine/Italy/7368/2022. Blue text indicates low hydrophobicity and red text high hydrophobicity. Blue highlights indcate 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. HEF, hemagglutinin-esterase fusion; MSAA, multi-sequence alignment; RBS, receptor-binding site.

Main Article

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1These first authors contributed equally to this article.

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