|Title||Expression, purification and X-ray crystallographic analysis of the Helicobacter pylori blood group antigen-binding adhesin BabA.|
|Publication Type||Journal Article|
|Year of Publication||2014|
|Authors||Subedi, S., K. Moonens, E. Romão, A. Lo, G. Vandenbussche, J. Bugaytsova, S. Muyldermans, T. Borén, and H. Remaut|
|Journal||Acta Crystallogr F Struct Biol Commun|
|Date Published||2014 Dec 01|
|Keywords||Adhesins, Bacterial, Base Sequence, Blood Group Antigens, Crystallography, X-Ray, DNA Primers, Helicobacter pylori|
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 (BabA(25-460)) corresponding to the predicted extracellular adhesin domain of the protein are reported. X-ray diffraction data for nanobody-stabilized BabA(25-460) 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 BabA(25-460)-nanobody complexes per asymmetric unit.
|Alternate Journal||Acta Crystallogr F Struct Biol Commun|
|PubMed Central ID||PMC4259228|
Expression, purification and X-ray crystallographic analysis of the Helicobacter pylori blood group antigen-binding adhesin BabA.