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. 2016 Apr 15;12(4):e1005533. doi: 10.1371/journal.ppat.1005533

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© 2016 Martinelli 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 properly credited.

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Fig 6 — (a) SDS-PAGE analysis of G37 wild type and mutant strains Δmg491, Δmg491-mg491cat, Δmg491-mg491-C87S, Δmg491-mg491-F157A-F158A, Δmg491-mg491-loopL2 and Δmg491-mg491ΔNt. Bands for proteins MG386, MG312, MG218, P140 and P110 were identified by their typical electrophoretic mobility [18]. The levels found for the cytadherence accessory proteins MG312, MG218 and for the P140 and P110 adhesins are highly reduced in the Δmg491 strain. Normal levels of these proteins are recovered in strains Δmg491-mg491cat, Δmg491-mg491-C87S, Δmg491-mg491-F157A-F158A and in Δmg491-mg491-loopL2, but not in Δmg491-mg491ΔNt. (b) Levels of the cytadherence accessory proteins MG317, MG200, MG217, P32 and MG219 as observed by western immunoblot analysis of the M. genitalium mutant strains produced in this study. Lanes are the same as described for panel (a). The levels of MG317, MG217 and P32 are reduced in the Δmg491 and Δmg491-mg491ΔNt mutant strains but these proteins are found at normal levels in the Δmg491-mg491cat, Δmg491-mg491-C87S, Δmg491-mg491-F157A-F158A and Δmg491-mg491-loopL2 mutant strains.