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

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 2.25 Å resolution from a crystal that belonged to space group P21, with unit-cell parameters a = 50.96, b = 131.41, c = 123.40 Å, α = 90.0, β = 94.8, γ = 90.0°, and which was predicted to contain two BabA25–460–nanobody complexes per asymmetric unit.

Source: Acta Crystallographica Section F - November 14, 2014 Category: Biochemistry Authors: Subedi, S.Moonens, K.Romão, E.Lo, A.Vandenbussche, G.Bugaytsova, J.Muyldermans, S.Borén, T.Remaut, H. Tags: Helicobacter pylori BabA adhesin nanobody crystallization communications Source Type: research