8h64
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8h64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8h64 OCA], [https://pdbe.org/8h64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8h64 RCSB], [https://www.ebi.ac.uk/pdbsum/8h64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8h64 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8h64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8h64 OCA], [https://pdbe.org/8h64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8h64 RCSB], [https://www.ebi.ac.uk/pdbsum/8h64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8h64 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | == Function == | ||
| - | [https://www.uniprot.org/uniprot/INLA_LISMO INLA_LISMO] Mediates the entry of L.monocytogenes into cells. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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 (V(H)Hs) that bind to InlA with picomolar affinities from an alpaca immune library using the phage display method. These InlA-specific V(H)Hs 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 V(H)Hs inhibited the invasion of L. monocytogenes into host cells in culture. High-resolution X-ray structure analyses of the complexes of V(H)Hs with InlA revealed that the V(H)Hs bind to the same binding site as E-cadherin against InlA. We conclude that these V(H)Hs have the potential for use as drugs to treat listeriosis. | 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 (V(H)Hs) that bind to InlA with picomolar affinities from an alpaca immune library using the phage display method. These InlA-specific V(H)Hs 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 V(H)Hs inhibited the invasion of L. monocytogenes into host cells in culture. High-resolution X-ray structure analyses of the complexes of V(H)Hs with InlA revealed that the V(H)Hs bind to the same binding site as E-cadherin against InlA. We conclude that these V(H)Hs have the potential for use as drugs to treat listeriosis. | ||
| - | Anti-InlA single-domain antibodies that inhibit the cell invasion of Listeria monocytogenes.,Yamazaki T, Nagatoishi S, Yamawaki T, Nozawa T, Matsunaga R, Nakakido M, Caaveiro JMM, Nakagawa I, Tsumoto K J Biol Chem. 2023 | + | Anti-InlA single-domain antibodies that inhibit the cell invasion of Listeria monocytogenes.,Yamazaki T, Nagatoishi S, Yamawaki T, Nozawa T, Matsunaga R, Nakakido M, Caaveiro JMM, Nakagawa I, Tsumoto K J Biol Chem. 2023 Oct;299(10):105254. doi: 10.1016/j.jbc.2023.105254. Epub 2023 , Sep 14. PMID:37716701<ref>PMID:37716701</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
Current revision
Crystal structure of Internalin A from Listeria monocytogenes with nanobody VHH24 bound
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