Samenvatting
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.
Originele taal-2 | English |
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Pagina's (van-tot) | 1631-1635 |
Aantal pagina's | 5 |
Tijdschrift | Acta Crystallographica Section F - Structural Biology Communications |
Volume | 70 |
Nummer van het tijdschrift | 12 |
DOI's | |
Status | Published - 1 dec 2014 |
Keywords
- Adhesins, Bacterial
- Base Sequence
- Blood Group Antigens
- Crystallography, X-Ray
- DNA Primers
- Helicobacter pylori