Vetnews | April 2025 24 « BACK TO CONTENTS Figure 4: Homology modeling of the N. albiventris N protein. A. Alignment of the amino acid sequence of the N. albiventris NA protein with the N11 subtypes from Peru and Bolivia. B. 3D structure of the tetramer from a bottom transmembrane view and a top view showing the putative active site of the protein with five mutations (K363R, T242K, M138F, G361S, and I139V) relative to the N11 sequence from Peru and Bolivia. Conserved regions are shown in purple, and divergent amino acids in white. Figure 5: Molecular analysis and docking of the N protein. A A/bat/Peru N11 protein. B. N protein of N. albiventris. C. Monomer of the N protein of N. albiventris bound to the bat HLA-DR. The contact region (2935.1 ˚A2) between the two proteins is indicated. The Van der Waal energy was 67.8. D. Binding details between residues of the N protein of N. albiventris and bat HLA-DR. The binding of the three mutations Ser361, Ar363, and Lys242 of the hypothetical active site of the N protein with Lys111, pro87, and Val97/Glu98, respectively, with the bat HLA-DR is evident. Bats from the Colombian Caribbean Reveal a new subtype of Influenza A (H18N12) <<<23 Article References are available on request v
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