Fig. 2: Comparison of purified Fap2-ECD with native Fn outer membrane adhesins. | Nature Communications

Fig. 2: Comparison of purified Fap2-ECD with native Fn outer membrane adhesins.

From: Structural basis of Fusobacterium nucleatum adhesin Fap2 interaction with receptors on cancer and immune cells

Fig. 2: Comparison of purified Fap2-ECD with native Fn outer membrane adhesins.

a SDS-PAGE of the isolated OM fraction of Fn ATCC25586 after co-cultivation with Jurkat cells. Proteins corresponding to the indicated bands were identified as Fap2 and RadD in peptide fingerprint analysis (Supplementary Fig. 5a, b). MW molecular weight marker. The experiment was repeated three times with similar results. b Representative cryo tomogram out of 40 of a section of Fn ATCC25586 including the inner membrane (IM), periplasm (PP) and outer membrane (OM). Rod-like structures on the surface that represent autotransporter adhesins in size and shape are indicated by arrowheads (scale bar: 100 nm). The inset shows one of these magnified. Note that the ripples in the OM might be caused by oxygen exposure of the anaerobic F. nucleatum before and during vitrification. Scale bar: 100 nm, inset: 50 nm. c Selected rod-shaped OM surface protrusions from Fn (left panel) detected in reconstructed tomograms (n = 40) in comparison with different projection views of the recombinantly produced Fap2-ECD (middle panel: micrograph, n = 12,663; right panel: 2D class averages, n = 81).

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