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Publication Abstract from PubMed

We solved the crystal structure of a functionally uncharacterized protein, HP0902, from Helicobacter pylori. Its structure demonstrated an all-beta cupin fold that cannot bind metal ions due to the absence of a metal-binding histidine that is conserved in many metallo-cupins. In contrast, isothermal titration calorimetry and NMR titration demonstrated that HP0902 is able to bind bacterial endotoxin lipopolysaccharides (LPS) through its surface-exposed loops, where metal-binding sites are usually found in other metallo-cupins. This report constitutes the first identification of an LPS-interacting protein, both in the cupin family and in H. pylori. Furthermore, identification of the ability of HP0902 to bind LPS uncovers a putative role for this protein in H. pylori pathogenicity.

Structural identification of the lipopolysaccharide-binding capability of a cupin-family protein from Helicobacter pylori.,Sim DW, Kim JH, Kim HY, Jang JH, Lee WC, Kim EH, Park PJ, Lee KH, Won HS FEBS Lett. 2016 Sep;590(17):2997-3004. doi: 10.1002/1873-3468.12332. Epub 2016, Aug 11. PMID:27466800^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.