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. 2021 Sep 13;12:738619. doi: 10.3389/fpls.2021.738619

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Copyright © 2021 Stander, Chabeda, Rybicki and Meyers.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Analysis of ST-AP205 and EDIII-SC coupling. Schematic diagram of coupling components: each AP205 CP has an ST peptide (16.5 kDa) and 180 CP proteins make up the icosahedral (T = 3) ST-AP205 virus-like particles (VLP) and as a result, there are 180 binding motifs that can couple to WNV-EDIII-SC (25 kDa). Western blot analysis of complex formation visualised with rabbit anti-WNV-EDIII antiserum (A) or rabbit anti-ST-AP205 antiserum (B). Successful coupling is indicated by a molecular weight shift to 41.5 kDa (monomer—shaded triangle, ~58 kDa coupled dimer—AP205 CP dimer with one coupled WNV-EDIII protein) only in co-purified extracts containing ST-AP205 and WNV-EDIII-SC. pTRAkc-ERH: empty plant-expression vector. AP205: Acinetobacter bacteriophage AP205 CP. EDIII: West Nile virus (WNV) envelope domain III. ST, SpyTag; SC, SpyCatcher. Red arrows: ST-AP205 protein subunits (16.5 kDa monomer, 33 kDa dimer, 66 kDa tetramer). Blue arrows: WNV-EDIII-SC protein subunits (25 kDa monomer, ~50 kDa dimer). Black arrow: 41.5 kDa AP205:EDIII coupled complex monomer. Green arrow: ~58 kDa AP205:EDIII coupled complex dimer.