Publication Date:
2014-11-14
Description:
Helicobacter pyloriis 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 BabA25–460were collected to 2.25 Å resolution from a crystal that belonged to space groupP21, with unit-cell parametersa= 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.
Electronic ISSN:
2053-230X
Topics:
Biology
,
Chemistry and Pharmacology
,
Geosciences
,
Physics
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