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. 2014 Jun 25;7:290. doi: 10.1186/1756-3305-7-290

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Copyright © 2014 McWilliam et al.; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Recombinant Sj-L6L-1 (rSj-L6L-1) contains conformational epitopes. A: The purified fusion protein of rSj-L6L-1 with thioredoxin (Trx), or rTrx alone, were analysed by SDS-PAGE under non-reducing conditions (lanes 2, 4, 6) or reducing conditions with dithiothreitol (DTT; lanes 3, 5, 7). DTT had no effect on rTrx but slightly increased the size of rSj-L6L-1. Reduced and non-reduced rSj-L6L-1 was transferred to a nitrocellulose membrane and probed with lung-LN ASC-probes (lanes 6–7). B: rSj-L6L-1 ELISA with rat ASC-probes obtained from skin-, lung- or liver-LN or spleen compared with non-infected (NI) rat serum. Relative binding to rSj-L6L-1 is the ratio of the rSj-L6L-1 optical density to that of the fusion partner, rTrx, alone. Bars represent the mean ± standard error.