8H62
Crystal structure of Internalin A from Listeria monocytogenes with human E-cadherin EC12
Summary for 8H62
Entry DOI | 10.2210/pdb8h62/pdb |
Descriptor | Internalin A, Cadherin-1, CALCIUM ION, ... (5 entities in total) |
Functional Keywords | internalin a cadherin bacterial invasion nanobody surface plasmon resonance isothermal titration calorimetry, cell invasion |
Biological source | Listeria monocytogenes serovar 1/2a More |
Total number of polymer chains | 2 |
Total formula weight | 73268.77 |
Authors | Caaveiro, J.M.M.,Nagatoish, S.,Tsumoto, K. (deposition date: 2022-10-14, release date: 2023-10-04, Last modification date: 2023-10-25) |
Primary citation | Yamazaki, T.,Nagatoishi, S.,Yamawaki, T.,Nozawa, T.,Matsunaga, R.,Nakakido, M.,Caaveiro, J.M.M.,Nakagawa, I.,Tsumoto, K. Anti-InlA single-domain antibodies that inhibit the cell invasion of Listeria monocytogenes. J.Biol.Chem., 299:105254-105254, 2023 Cited by PubMed Abstract: Listeriosis, caused by infection with Listeria monocytogenes, is a severe disease with a high mortality rate. The L. monocytogenes virulence factor, internalin family protein InlA, which binds to the host receptor E-cadherin, is necessary to invade host cells. Here, we isolated two single-domain antibodies (VHs) that bind to InlA with picomolar affinities from an alpaca immune library using the phage display method. These InlA-specific VHs inhibited the binding of InlA to the extracellular domains of E-cadherin in vitro as shown by biophysical interaction analysis. Furthermore, we determined that the VHs inhibited the invasion of L. monocytogenes into host cells in culture. High-resolution X-ray structure analyses of the complexes of VHs with InlA revealed that the VHs bind to the same binding site as E-cadherin against InlA. We conclude that these VHs have the potential for use as drugs to treat listeriosis. PubMed: 37716701DOI: 10.1016/j.jbc.2023.105254 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.91 Å) |
Structure validation
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