All subtypes of the Pmp adhesin family are implicated in chlamydial virulence and show species-specific function
Version of Record online: 1 JUL 2014
© 2014 The Authors. MicrobiologyOpen published by John Wiley & Sons Ltd.
This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Volume 3, Issue 4, pages 544–556, August 2014
How to Cite
MicrobiologyOpen 2014; 3(4): 544–556
- Issue online: 14 AUG 2014
- Version of Record online: 1 JUL 2014
- Manuscript Accepted: 15 MAY 2014
- Manuscript Revised: 30 APR 2014
- Manuscript Received: 23 DEC 2013
- Deutsche Forschungsgemeinschaft
- Federal Ministry for Education and Research
|mbo3186-sup-0001-FigS1.tif||image/tif||2347K||Figure S1. Yeast cells presenting chlamydial Pmps on their cell surface. (A) Detection of Aga2 and Aga2-Pmp fusion proteins on the yeast cell surface. Green fluorescent yeast cells expressing Aga2 and Aga2–Pmp fusion proteins were fixed and stained with an anti-V5 antibody (red) against the C-terminal V5-Tag. Top panel: Phase contrast microscopy. Bottom panel: Fluorescence microscopy. (B) Western blot analysis of Aga2 and Aga2-Pmp fusion proteins. Total protein extracts from yeast strains expressing Aga2 or Aga2–Pmp fusion proteins were digested with α-mannosidase to remove Aga2 O-glycosylation, resolved by SDS-PAGE and probed with an anti-His antibody. Protein size markers (in kDa) are indicated to the left of each blot.|
|mbo3186-sup-0002-FigS2.tif||image/tif||538K||Figure S2. Coating efficiency of latex beads. Western blot analysis of recombinant proteins coated on 2 × 107 latex beads (adhesion data shown in Fig. 1C). Proteins were removed from the bead surface by SDS-loading buffer and DTT, resolved by SDS-PAGE, and probed with an antibody against the N-terminal His tag. Lane M, molecular mass marker.|
|mbo3186-sup-0003-TableS1.pdf||application/PDF||248K||Table S1. List of oligonucleotides used for plasmid construction.|
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