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Cloning and identification of Bartonella α-enolase as a plasminogen-binding protein.
- Source :
-
Microbial pathogenesis [Microb Pathog] 2019 Oct; Vol. 135, pp. 103651. Date of Electronic Publication: 2019 Aug 06. - Publication Year :
- 2019
-
Abstract
- Bartonella infection is distributed worldwide with animal and public health. Recent studies have shown that host cells infection by Bartonella has a series of different infection stages, beginning with encounter and adherence to the cells. In this study, we expressed and purified recombinant Bartonella henselae (B. henselae) α-enolase. And we found that B. henselae α-enolase is highly conserved in Bartonella species. The interacting protein partners of B. henselae α-enolase were showed by String-11. The interactions between B. henselae α-enolase and human plasminogen were subsequently confirmed by ELISA, pull down, T7 phage display and molecular docking assays. And the plasminogen-binding sites of B. henselae α-enolase are predicted at <superscript>247</superscript> FYKNGSYFY <superscript>255</superscript> . These findings will help elucidate and improve the understanding of the molecular mechanisms of Bartonella infection.<br /> (Copyright © 2019 Elsevier Ltd. All rights reserved.)
- Subjects :
- Amino Acid Sequence
Bartonella henselae enzymology
Bartonella henselae genetics
Binding Sites
Carrier Proteins chemistry
Cloning, Molecular
Gene Expression Regulation, Bacterial
Humans
Models, Molecular
Molecular Docking Simulation
Phosphopyruvate Hydratase chemistry
Phosphopyruvate Hydratase classification
Phylogeny
Plasminogen chemistry
Recombinant Proteins
Bartonella enzymology
Bartonella genetics
Carrier Proteins metabolism
Phosphopyruvate Hydratase genetics
Phosphopyruvate Hydratase isolation & purification
Plasminogen metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1096-1208
- Volume :
- 135
- Database :
- MEDLINE
- Journal :
- Microbial pathogenesis
- Publication Type :
- Academic Journal
- Accession number :
- 31398532
- Full Text :
- https://doi.org/10.1016/j.micpath.2019.103651