Figure 2 | Scientific Reports

Figure 2

From: Attenuation of Streptococcus suis virulence by the alteration of bacterial surface architecture

Figure 2

Multiple sequence alignments of S. suis NeuB homologue with two known NeuB proteins from E. coli and N. meningitides.

The amino acid sequences of NeuB proteins used here are separately collected from S. suis 05ZYH33 (YP_001197944), E. coli K12 (NC_010498) and N. meningitides (AAA20477). S. suis was indicated in red and N. meningitides is an abbreviation for Neisseria meningitides. Identical residues are indicated with white letters on a red background, similar residues are red letters on white, varied residues are in black letters and dots represent gaps. The predicted secondary structure of the NeuB protein is shown on top. α: α-helix; β: β-sheet; T: β-turns/coils. Fifteen critical residues (such as E25, 53K, 55Q, etc.) visualized in crystal structure of N. meningitidis NeuB protein for its enzymatic activity and/or Mn2+ binding28 are found to be extremely conserved and thereby highlighted with blue triangles.

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