Binding of Brucella protein, Bp26, to select extracellular matrix molecules

ElTahir, Y, Al-Araimi, A, Nair, RR, Autio, KJ, Tu, H, Leo, JC ORCID: https://orcid.org/0000-0002-7066-7527, Al-Marzooqi, W and Johnson, EH, 2019. Binding of Brucella protein, Bp26, to select extracellular matrix molecules. BMC Molecular and Cell Biology, 20 (1): 55. ISSN 2661-8850

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Abstract

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.

Item Type:	Journal article
Publication Title:	BMC Molecular and Cell Biology
Creators:	ElTahir, Y., Al-Araimi, A., Nair, R.R., Autio, K.J., Tu, H., Leo, J.C., Al-Marzooqi, W. and Johnson, E.H.
Publisher:	Springer
Date:	2019
Volume:	20
Number:	1
ISSN:	2661-8850
Identifiers:	Number Type 10.1186/s12860-019-0239-7 DOI 1250524 Other
Rights:	© The Author(s). 2019 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
Divisions:	Schools > School of Science and Technology
Record created by:	Linda Sullivan
Date Added:	24 Feb 2020 09:11
Last Modified:	24 Feb 2020 09:14
URI:	https://irep.ntu.ac.uk/id/eprint/39260

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