A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Structural and Biomolecular Analyses of Borrelia burgdorferi BmpD Reveal a Substrate-Binding Protein of an ABC-Type Nucleoside Transporter Family
Tekijät: Cuellar J, Åstrand M, Elovaara H, Pietikäinen A, Sirén S, Liljeblad A, Guédez G, Salminen TA, Hytönen J
Kustantaja: American Society for Microgiology
Julkaisuvuosi: 2020
Journal: Infection and Immunity
Tietokannassa oleva lehden nimi: Infection and immunity
Lehden akronyymi: Infect Immun
Vuosikerta: 88
Numero: 4
ISSN: 0019-9567
eISSN: 1098-5522
DOI: https://doi.org/10.1128/IAI.00962-19
Verkko-osoite: 10.1128/IAI.00962-19
Rinnakkaistallenteen osoite: https://research.utu.fi/converis/portal/detail/Publication/45748938
Borrelia burgdorferisensu lato, the causative agent of tick-borne Lyme borreliosis (LB), has a limited metabolic capacity and needs to acquire nutrients, such as amino acids, fatty acids, and nucleic acids, from the host environment. Using X-ray crystallography, liquid chromatography-mass spectrometry, microscale thermophoresis, and cellular localization studies, we show that basic membrane protein D (BmpD) is a periplasmic substrate-binding protein of an ABC transporter system binding to purine nucleosides. Nucleosides are essential for bacterial survival in the host organism, and these studies suggest a key role for BmpD in the purine salvage pathway of B. burgdorferi sensu lato Because B. burgdorferisensu lato lacks the enzymes required for de novo purine synthesis, BmpD may play a vital role in ensuring access to the purines needed to sustain an infection in the host. Furthermore, we show that, although human LB patients develop anti-BmpD antibodies, immunization of mice with BmpD does not confer protection against B. burgdorferi sensu lato infection.
Ladattava julkaisu This is an electronic reprint of the original article. |