ElTahir, Y., Al-Araimi, A., R. Nair, R. et al. Binding of Brucella protein, Bp26, to select extracellular matrix molecules. BMC Mol and Cell Biol 20, 55 (2019). https://doi.org/10.1186/s12860-019-0239-7
Binding of Brucella protein, Bp26, to select extracellular matrix molecules
|Author:||ElTahir, Yasmin1; Al-Araimi, Amna1; Nair, Remya R.1;|
1Department of Animal & Veterinary Sciences, Sultan Qaboos University. College of Agricultural & Marine Sciences, P.O.box 34. 123 Alkhod, Muscat, Sultanate of Oman
2Faculty of Biochemistry and Molecular Medicine, University of Oulu, FI-90014, Oulu, Finland
3Section for Genetics and Evolutionary Biology, Department of Biosciences, University of Oslo, 0361, Oslo, Norway
4Department of Biosciences, School of Science & Technology, Nottingham Trent University, Nottingham, NG1 4FQ, UK
|Online Access:||PDF Full Text (PDF, 2.8 MB)|
|Persistent link:|| http://urn.fi/urn:nbn:fi-fe2020040210119
|Publish Date:|| 2020-04-02
Background: Brucella is a facultative intracellular pathogen responsible for zoonotic disease brucellosis. Little is known about the molecular basis of Brucella adherence to host cells. In the present study, the possible role of Bp26 protein as an adhesin was explored. The ability of Brucella protein Bp26 to bind to extracellular matrix (ECM) proteins was determined by enzyme-linked immunosorbent assay (ELISA) and biolayer interferometry (BLI).
Results: ELISA experiments showed that Bp26 bound in a dose-dependent manner to both immobilized type I collagen and vitronectin. Bp26 bound weakly to soluble fibronectin but did not bind to immobilized fibronectin. No binding to laminin was detected. Biolayer interferometry showed high binding affinity of Bp26 to immobilized type I collagen and no binding to fibronectin or laminin. Mapping of Bp26 antigenic epitopes by biotinylated overlapping peptides spanning the entire sequence of Bp26 using anti Bp26 mouse serum led to the identification of five linear epitopes. Collagen and vitronectin bound to peptides from several regions of Bp26, with many of the binding sites for the ligands overlapping.
The strongest binding for anti-Bp26 mouse serum, collagen and vitronectin was to the peptides at the C-terminus of Bp26. Fibronectin did not bind to any of the peptides, although it bound to the whole Bp26 protein.
Conclusions: Our results highlight the possible role of Bp26 protein in the adhesion process of Brucella to host cells through ECM components. This study revealed that Bp26 binds to both immobilized and soluble type I collagen and vitronectin. It also binds to soluble but not immobilized fibronectin. However, Bp26 does not bind to laminin.
These are novel findings that offer insight into understanding the interplay between Brucella and host target cells, which may aid in future identification of a new target for diagnosis and/or vaccine development and prevention of brucellosis.
BMC molecular and cell biology
|Type of Publication:||
A1 Journal article – refereed
|Field of Science:||
1182 Biochemistry, cell and molecular biology
This work was supported by grant from HIS MAJESTY’s Sultan Qaboos Bin Said for strategic research fund (project no. SR/ANVS/14/01), Sultan Qaboos University internal research fund (project no IG/AGR/ANVS/08/03/05) (design of the study conduction of the experiments, analysis, interpretation of data and writing the manuscript), and a Young Investigator grant from the Research Council of Norway (Project 249793, to JCL) (analysis, and interpretation of data and writing the manuscript).
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