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Structural and Biomolecular Analyses of Borrelia burgdorferi BmpD Reveal a Substrate-Binding Protein of an ABC-Type Nucleoside Transporter Family




TekijätCuellar J, Åstrand M, Elovaara H, Pietikäinen A, Sirén S, Liljeblad A, Guédez G, Salminen TA, Hytönen J

KustantajaAmerican Society for Microgiology

Julkaisuvuosi2020

JournalInfection and Immunity

Tietokannassa oleva lehden nimiInfection and immunity

Lehden akronyymiInfect Immun

Vuosikerta88

Numero4

ISSN0019-9567

eISSN1098-5522

DOIhttps://doi.org/10.1128/IAI.00962-19

Verkko-osoite10.1128/IAI.00962-19

Rinnakkaistallenteen osoitehttps://research.utu.fi/converis/portal/detail/Publication/45748938


Tiivistelmä

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.


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Last updated on 2024-26-11 at 15:43