Neisseria gonorrhoeae employs two protein inhibitors to evade killing by human lysozyme
Fig 1
In silico analysis of Ng_1063.
A. MUSCLE alignment of Ng_1063 (strain MS11, orange text) with P. aeruginosa and E. coli MliC proteins. Signal sequence is underlined. Asterisks (*) denote positions in the sequence with a fully conserved residue. Colons (:) and periods (.) denote amino acids with strongly or weakly similar properties, respectively. The serine and lysine residues implicated in MliC inhibition of lysozyme are highlighted in magenta and red boxes, respectively. B. Alignment of the predicted structure of Ng_1063 (orange) with P. aeruginosa MliC (grey). The structure of Ng_1063 (strain MS11) was predicted using the PHYRE2 server and subsequently aligned to P. aeruginosa MliC (PDB 3f6z) via PyMOL. Inset shows the S83 (magenta) and K103 (red) residues from Ng_1063 and the S89 (black) and K103 (light blue) residues from P. aeruginosa MliC. C. Predicted Ng_1063 (orange) complex with lysozyme (hen egg white, blue). The P. aeruginosa MliC complex with lysozyme (PDB 3f6z) was used as a platform to model the Ng_1063-lysozyme complex via PyMOL. Inset shows the S83 (magenta) and K103 (red) residues from Ng_1063 with the lysozyme active site residues, E53 (yellow) and D70 (cyan).