The Legionella collagen-like protein employs a distinct binding mechanism for the recognition of host glycosaminoglycans

Saima Rehman, Anna Katarina Antonovic, Ian E. McIntire, Huaixin Zheng, Leanne Cleaver, Maria Baczynska, Carlton O. Adams, Theo Portlock, Katherine Richardson, Rosie Shaw, Alain Oregioni, Giulia Mastroianni, Sara B-M. Whittaker, Geoff Kelly, Christian D. Lorenz, Arianna Fornili (), Nicholas P. Cianciotto () and James A. Garnett ()
Additional contact information
Saima Rehman: King’s College London
Anna Katarina Antonovic: Queen Mary University of London
Ian E. McIntire: Northwestern University Feinberg School of Medicine
Huaixin Zheng: Northwestern University Feinberg School of Medicine
Leanne Cleaver: King’s College London
Maria Baczynska: King’s College London
Carlton O. Adams: Northwestern University Feinberg School of Medicine
Theo Portlock: King’s College London
Katherine Richardson: Queen Mary University of London
Rosie Shaw: Queen Mary University of London
Alain Oregioni: The Francis Crick Institute
Giulia Mastroianni: Queen Mary University of London
Sara B-M. Whittaker: University of Birmingham
Geoff Kelly: The Francis Crick Institute
Christian D. Lorenz: King’s College London
Arianna Fornili: Queen Mary University of London
Nicholas P. Cianciotto: Northwestern University Feinberg School of Medicine
James A. Garnett: King’s College London

Nature Communications, 2024, vol. 15, issue 1, 1-16

Abstract: Abstract 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.

Date: 2024
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-024-49255-4 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-49255-4

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-024-49255-4

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().