The Legionella collagen-like protein employs a distinct binding mechanism for the recognition of host glycosaminoglycans.
Autor: | Rehman S; Centre for Host-Microbiome Interactions, Faculty of Dental, Oral & Craniofacial Sciences, King's College London, London, UK., Antonovic AK; Department of Chemistry, School of Physical and Chemical Sciences, Queen Mary University of London, London, UK., McIntire IE; Department of Microbiology and Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL, USA., Zheng H; Department of Microbiology and Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL, USA., Cleaver L; Centre for Host-Microbiome Interactions, Faculty of Dental, Oral & Craniofacial Sciences, King's College London, London, UK., Baczynska M; Centre for Host-Microbiome Interactions, Faculty of Dental, Oral & Craniofacial Sciences, King's College London, London, UK.; Biological Physics & Soft Matter Research Group, Department of Physics, King's College London, London, UK., Adams CO; Department of Microbiology and Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL, USA., Portlock T; Centre for Host-Microbiome Interactions, Faculty of Dental, Oral & Craniofacial Sciences, King's College London, London, UK.; School of Biological and Behavioural Sciences, Queen Mary University of London, London, UK., Richardson K; School of Biological and Behavioural Sciences, Queen Mary University of London, London, UK., Shaw R; School of Biological and Behavioural Sciences, Queen Mary University of London, London, UK., Oregioni A; The Medical Research Council Biomedical NMR Centre, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK., Mastroianni G; Department of Chemistry, School of Physical and Chemical Sciences, Queen Mary University of London, London, UK., Whittaker SB; School of Cancer Sciences, College of Medical and Dental Sciences, University of Birmingham, Birmingham, UK., Kelly G; The Medical Research Council Biomedical NMR Centre, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK., Lorenz CD; Biological Physics & Soft Matter Research Group, Department of Physics, King's College London, London, UK., Fornili A; Department of Chemistry, School of Physical and Chemical Sciences, Queen Mary University of London, London, UK. a.fornili@qmul.ac.uk., Cianciotto NP; Department of Microbiology and Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL, USA. n-cianciotto@northwestern.edu., Garnett JA; Centre for Host-Microbiome Interactions, Faculty of Dental, Oral & Craniofacial Sciences, King's College London, London, UK. james.garnett@kcl.ac.uk. |
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Jazyk: | angličtina |
Zdroj: | Nature communications [Nat Commun] 2024 Jun 08; Vol. 15 (1), pp. 4912. Date of Electronic Publication: 2024 Jun 08. |
DOI: | 10.1038/s41467-024-49255-4 |
Abstrakt: | Bacterial adhesion is a fundamental process which enables colonisation of niche environments and is key for infection. However, in Legionella pneumophila, the causative agent of Legionnaires' disease, these processes are not well understood. The Legionella collagen-like protein (Lcl) is an extracellular peripheral membrane protein that recognises sulphated glycosaminoglycans on the surface of eukaryotic cells, but also stimulates bacterial aggregation in response to divalent cations. Here we report the crystal structure of the Lcl C-terminal domain (Lcl-CTD) and present a model for intact Lcl. Our data reveal that Lcl-CTD forms an unusual trimer arrangement with a positively charged external surface and negatively charged solvent exposed internal cavity. Through molecular dynamics simulations, we show how the glycosaminoglycan chondroitin-4-sulphate associates with the Lcl-CTD surface via distinct binding modes. Our findings show that Lcl homologs are present across both the Pseudomonadota and Fibrobacterota-Chlorobiota-Bacteroidota phyla and suggest that Lcl may represent a versatile carbohydrate-binding mechanism. (© 2024. The Author(s).) |
Databáze: | MEDLINE |
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