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Expression, purification and X-ray crystallographic analysis of the Helicobacter pylori blood group antigen-binding adhesin BabA

par Subedi, Suresh;Moonens, Kristof;Romaõ, Ema;Alvin, Louis ;Vandenbussche, Guy ;Bugaytsova, Jeanna;Muyldermans, Serge;Borén, Thomas;Remaut, Han
Référence Acta Crystallographica Section F:Structural Biology Communications, 70, page (1631-1635)
Publication Publié, 2014-12

Article révisé par les pairs

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Résumé :

Helicobacter pylori is a human pathogen that colonizes about 50% of the world's population, causing chronic gastritis, duodenal ulcers and even gastric cancer. A steady emergence of multiple antibiotic resistant strains poses an important public health threat and there is an urgent requirement for alternative therapeutics. The blood group antigen-binding adhesin BabA mediates the intimate attachment to the host mucosa and forms a major candidate for novel vaccine and drug development. Here, the recombinant expression and crystallization of a soluble BabA truncation (BabA25-460) corresponding to the predicted extracellular adhesin domain of the protein are reported. X-ray diffraction data for nanobody-stabilized BabA25-460 were collected to 2.25Å resolution from a crystal that belonged to space group P21, with unit-cell parameters a = 50.96, b = 131.41, c = 123.40Å, α = 90.0, β = 94.8, γ = 90.0°, and which was predicted to contain two BabA25-460-nanobody complexes per asymmetric unit.