Presence of a Motif Conserved between Helicobacter pylori TNF-α Inducing Protein (Tipα) and Penicillin-Binding Proteins(Miscellaneous)

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Here we report a primary structure conserved between Helicobacter pylori (H. pylori)-tumor necrosis factorα inducing protein (Tipα) and bacterial penicillin-binding proteins. H. pylori is a Gram-negative bacterium which plays a key part in carcinogenesis in the human stomach. We previously reported that Tipα has a carcinogenic potential as tumor promoter, and that it has no obvious homologue in other species. To investigate the structure-function relationship of Tipα and to predict its ancestral protein, we searched among proteins which have weak homology to Tipα in their primary structures, using Psi-Blast, and we identified numerous Gram-positive bacterial penicillin-binding proteins as weakly homologous to Tipα. Among these, several unique amino acids are conserved and form a motif-like structure. Phylogenic tree analysis indicated that Tipα is closer to the penicillin-binding proteins of Gram-positive bacteria, based on their primary structures, than to H. pylori. This finding suggests that Tipα and penicillin-binding proteins are derived from a common ancestral protein, and that Tipα gene may be transferred horizontally from Gram-positive bacteria to H. pylori.
公益社団法人日本薬学会の論文
2005-11-01