Structural and biomolecular analyses of Borrelia burgdorferi BmpD reveal a substrate-binding protein of an ABC-type nucleoside transporter family

A1 Journal article (refereed)

Internal Authors/Editors

Publication Details

List of Authors: Julia Cuellar, Mia Åstrand, Heli Elovaaraa, Annukka Pietikäinen, Saija Sirén, Arto Liljeblad, Gabriela Guédez, Tiina A. Salminen & Jukka Hytönen
Publication year: 2020
Journal: Infection and Immunity


Borrelia burgdorferi sensu lato (sl), the causative agent of the
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 sl. As B. burgdorferi sl lacks the enzymes required for de novo
purine synthesis, BmpD may play a vital role in ensuring access to the
purines needed for sustaining an infection in the host. Further, we show
that although human LB patients develop anti-BmpD antibodies,
immunization of mice with BmpD does not confer protection against B. burgdorferi sl infection.

Last updated on 2020-26-05 at 04:49