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. 2018 Feb 26;46(9):4733–4751. doi: 10.1093/nar/gky124

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© The Author(s) 2018. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 5. — Potential type I toxin proteins alignment and analysis. (A) Proteins alignment using ClustalW. ‘*’ on the right indicates toxins from three TA modules selected for detailed analysis. ‘*’ at the bottom indicates conserved residues. (B) Western-blot detection and localization of HA-tagged small proteins in the membrane fraction of C. difficile cell extracts. WCL: whole cell lysate; SN: supernatant; CW: cell wall; Mb: membrane; Cy: cytosolic fraction. Immunoblotting with anti-HA antibodies detected a major polypeptide of ∼10 kDa in whole cell lysates of the strain carrying P_tet-T(CD2517.1 or CD2907.1/CD0956.2)-HA (pT-HA) construct grown in the presence of the 250 ng/ml ATc inducer but not in extracts of strains expressing non-tagged toxins (pT) (left panel). The culture of strains carrying P_tet-T-HA plasmids induced with 250 ng/ml ATc was fractionated into cell wall (CW), membrane (Mb) and cytosolic (Cy) compartments and immunoblotted with anti-HA antibodies (middle and right panels). Proteins were separated on 12% Bis-Tris polyacrylamide gels in MES buffer.