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. 2019 Apr 11;13(4):e0007215. doi: 10.1371/journal.pntd.0007215

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© 2019 Vázquez-Guerrero et al

This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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Fig 2 — rGlpQ and rBipA expression and purification. B. turicatae glpQ was expressed as a recombinant fusion protein (A). Lanes 1 and 2 are E. coli BL21 pLysS pET-19b-glpQ before and after induction with IPTG, respectively; lanes 3 and 4 are two purified fractions of rGlpQ. B. turicatae bipA was also expressed as a recombinant fusion protein (B). Lanes 1 and 2 are E. coli BL21 pLysS pET-19b-bipA before and after induction with IPTG, respectively; lanes 3 and 4 are two fractions of purified rBipA. Immunoblotting was performed using an anti-histidine probe conjugated to HRP for the histidine epitope on rGlpQ and rBipA (C). Molecular masses are shown on the left of each immunoblot in kilodaltons. MW, molecular weight; rBipA, recombinant Borrelia immunogenic protein A; rGlpQ, recombinant glycerophosphodiester phosphodiesterase.