Fig. 5: Structural and antigenic characterisation of bYFV DIII mutant chimeras. | Nature Communications

Fig. 5: Structural and antigenic characterisation of bYFV DIII mutant chimeras.

From: A single residue in the yellow fever virus envelope protein modulates virion architecture and antigenicity

Fig. 5

a Schematic of the YFV genome illustrating the four amino acids in DIII where YFV17D differs to both YFVES504 and YFVAsibi. b Representative micrographs of the bYFV DIII mutant chimeras at 4 °C. c IC50 values of recombinant hIgG1 anti-YFV or anti-flavivirus mAbs against the bYFV DIII mutant chimeras. Neutralisation was determined using FRNTs on C6/36 (Aedes albopictus) cells. Each symbol represents a technical replicate from three biological replicates (n = 6) and lines indicate group medians. Parental bYFV17D and bYFVES504 controls are from Fig. 1E. Significance was determined via Kruskal-Wallis tests with Dunn’s multiple comparisons test on GraphPad Prism 9.0. ***p ≤ 0.0002, **p ≤ 0.002, *p ≤ 0.03. For 5A: p = 0.035 (17D F305S vs. 17D R380T), 2A10G6: p = 0.002 (all 17D viruses vs. 17D R380T), p = 0.004 (ES504 M299I vs. ES504 T380R), p = 0.016 (ES504 S305F vs. ES504 T380R), p = 0.01 (ES504 P325S vs. ES504 T380R), 6B6C−1: p = 0.0004 (17D, 17D I299M and 17D F305S vs 17D T380R), p = 0.003 (17D S325P vs 17D R380T), p = 0.002 (ES504 M299I vs. ES504 T380R), p = 0.005 (ES504 S305F vs. ES504 T380R), p = 0.040 (ES504 P325S vs. ES504 T380R), 864: p = 0.029 (17D vs. 17D F305S), p = 0.002 (17D vs. 17D S325P), p = 0.01 (17D I299M vs. 17D F305S), p = 0.0005 (17D I299M vs. 17D S325P). Source data is provided as a Source Data file. LOD limit of detection.

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