Cloning and identification of Bartonella α-enolase as a plasminogen-binding protein.

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 247FYKNGSYFY255. These findings will help elucidate and improve the understanding of the molecular mechanisms of Bartonella infection.

• Publication year

  2019

• Venue

  Microbial Pathogenesis

• Publication date

  2019-10-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1016/j.micpath.2019.103651PMID 31398532
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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