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. 2014 Jan 22;4(1):130202. doi: 10.1098/rsob.130202

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© 2014 The Authors. Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/3.0/, which permits unrestricted use, provided the original author and source are credited.

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Figure 3. — O-Glycosylation but not N-glycosylation modulates C. jejuni BgAg binding. (a) NCTC11168 and 11168ΔpglB were examined for binding to core-II, core-I, H-I, H-II, Le^b, Le^x and Le^y. Binding was not significantly reduced following pglB mutation. Error bars: mean of triplicate values ± s.e.m. from three independent experiments. (b) NCTC11168 and 11168ΔpseD were examined for binding to core-II, H-I, H-II, Le^b and Le^y. The binding of 11168ΔpseD was significantly reduced compared with the wild-type (***p < 0.001). Error bars: mean of triplicate values ± s.e.m. from three independent experiments. (c) Immunoblot analysis of purified MOMP from wild-type NCTC11168, 11168MOMP^268T/G and 11168ΔpseD strains using anti-MOMP antibodies. MOMP from the latter two strains showed an apparent size shift compared with the wild-type protein indicating a loss of glycosylation.