8T8DSummary for 8T8D
| Entry DOI | 10.2210/pdb8t8d/pdb |
| Descriptor | Neuraminyllactose-binding hemagglutinin, ACETATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | helicobacter pylori, adhesion, vaccine candidate, cell adhesion |
| Biological source | Helicobacter pylori |
| Total number of polymer chains | 4 |
| Total formula weight | 97475.21 |
| Authors | Martini, C.,Calmettes, C. (deposition date: 2023-06-22, release date: 2024-01-31, Last modification date: 2024-03-20) |
| Primary citation | Martini, C.,Araba, V.,Beniani, M.,Armoa Ortiz, P.,Simmons, M.,Chalbi, M.,Mellouk, A.,El Bakkouri, M.,Calmettes, C. Unraveling the crystal structure of the HpaA adhesin: insights into cell adhesion function and epitope localization of a Helicobacter pylori vaccine candidate. Mbio, 15:e0295223-e0295223, 2024 Cited by PubMed Abstract: is a bacterium that exhibits strict host restriction to humans and non-human primates, and the bacterium is widely acknowledged as a significant etiological factor in the development of chronic gastritis, peptic ulcers, and gastric cancers. The pathogenic potential of this organism lies in its adeptness at colonizing the gastric mucosa, which is facilitated by a diverse repertoire of virulence factors, including adhesins that promote the attachment of the bacteria to the gastric epithelium. Among these adhesins, HpaA stands out due to its conserved nature and pivotal role in establishing colonization. Moreover, this lipoprotein holds promise as an antigen for the development of effective vaccines, thus attracting considerable attention for in-depth investigations into its molecular function and identification of binding determinants. Here, we present the elucidation of the crystallographic structure of HpaA at 2.9 Å resolution. The folding adopts an elongated protein shape, which is distinctive to the family, and features an apical domain extension that plays a critical role in the cell-adhesion activity on gastric epithelial cells. Our study also demonstrates the ability of HpaA to induce TNF-α expression in macrophages, highlighting a novel role as an immunoregulatory effector promoting the pro-inflammatory response . These findings not only contribute to a deeper comprehension of the multifaceted role of HpaA in pathogenesis but also establish a fundamental basis for the design and development of structure-based derivatives, aimed at enhancing the efficacy of vaccines. PubMed: 38376163DOI: 10.1128/mbio.02952-23 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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