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

DOI: 10.1107/S2053230X14023188 DOI Help
PMID: 25484214 PMID Help

Authors: Suresh Subedi (Structural Biology Brussels, Vrije Universiteit Brussel) , Kristof Moonens (Structural Biology Brussels, Vrije Universiteit Brussel) , Ema Romão (Research Group Cellular and Molecular Immunology, Vrije Universiteit Brussel) , Alvin Wei Han Lo (Structural Biology Brussels, Vrije Universiteit Brussel) , Guy Vandenbussche (Structure and Function of Biological Membranes, Université Libre de Bruxelles) , Jeanna Bugaytsova (Department of Medical Biochemistry and Biophysics, Umea University) , Serge Muyldermans (Research Group Cellular and Molecular Immunology, Vrije Universiteit Brussel) , Thomas Borén (Department of Medical Biochemistry and Biophysics, Umea University) , Han Remaut (Vrije Universiteit Brussel)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 70 , PAGES 1631 - 1635

State: Published (Approved)
Published: December 2014
Diamond Proposal Number(s): 9426

Abstract: 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, [alpha] = 90.0, [beta] = 94.8, [gamma] = 90.0°, and which was predicted to contain two BabA25-460-nanobody complexes per asymmetric unit.

Journal Keywords: Helicobacter pylori; BabA; adhesin; nanobody

Subject Areas: Biology and Bio-materials, Medicine


Instruments: I04-Macromolecular Crystallography