Structural analysis of Borreliaburgdorferi periplasmic lipoprotein BB0365 involved in Lyme disease infection

FEBS Letters

article

Kalvis Brangulis¹  Inara Akopjana¹  Ivars Petrovskis¹  Andris Kazaks¹  Atis Jekabsons²  Kristaps Jaudzems²  Arturs Viksna³  Maris Bertins³  Kaspars Tars¹ 

[1] Latvian Biomedical Research and Study Centre;Latvian Institute of Organic Synthesis;Faculty of Chemistry, University of Latvia;Faculty of Biology, University of Latvia

关键词: Ixodes ticks;    Lyme borreliosis;    Lyme disease;    metalloenzyme;    spirochete;   

DOI  :  10.1002/1873-3468.13594

来源: John Wiley & Sons Ltd.

【 摘 要 】

The periplasmic lipoprotein BB0365 of the Lyme disease agent Borrelia burgdorferi is expressed throughout mammalian infection and is essential for all phases of Lyme disease infection; its function, however, remains unknown. In the current study, our structural analysis of BB0365 revealed the same structural fold as that found in the NqrC and RnfG subunits of the NADH:quinone and ferredoxin:NAD+ sodium-translocating oxidoreductase complexes, which points to a potential role for BB0365 as a component of the sodium pump. Additionally, BB0365 coordinated Zn2+ by the His51, His55, His140 residues, and the Zn2+ -binding site indicates that BB0365 could act as a potential metalloenzyme; therefore, this structure narrows down the potential functions of BB0365, an essential protein for B. burgdorferi to cause Lyme disease.

【 授权许可】

Unknown