•Superhydrophobic C-termini of hagfish VLRB leads to extremely low expression level.•C4bp oligomerization domain mediates heptameric VLRB with high binding ability and producttivity.•In vitro affinity maturation was efficiently carried out by LRRCT mutagenesis.•Fine epitope mapping revealed 37DWDTPL42 is the recognition epitope of selected arVLRBs.•The resulting arVLRBs can be used as diagnostic tools or therapeutic agents of VHSV.
Molecular Immunology – Elsevier
Published: Jul 1, 2018
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