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. 2021 Feb 4;11:3126. doi: 10.1038/s41598-021-82356-4

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Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Epitope footprint of H3/H7 cross-reactive nanobodies. (a) Flow cytometry histograms (FlowJo 10.4 software) showing NB37X-01 and NB37X-05 binding to displayed wild type H7-HA0 and mutants selected (b) Nb binding activity to a panel of yeast displayed HA0 mutants. Residue numbering is relative to HA2 domain. The Nbs used for epitope mapping are highlighted in blue. Commercial antibody MIA-H7-334 is included as positive control and retains binding to all mutants. Relative binding of Nbs to each displayed mutant were categorized as follows: ≤ 15% no binding (red), between 15 and 40% intermediate binding (orange) and ≥ 40% strong binding (green). *Represents retention of binding to the HA1 head domain carrying a non-relevant mutation HA1-S135A (c) yeast cells displaying the head specific Nb NB7-14 were incubated with HA treated with low and neutral pH and binding of the stem specific Nbs NB37X-01 and NB37X-05 was detected as mean fluorescent intensity (MFI). NB7-04 was a non-competing head specific nanobody control.