Open AccessStructural and Biomolecular Analyses of Borrelia burgdorferi BmpD Reveal a Substrate-Binding Protein of an ABC-Type Nucleoside Transporter Family
Author(s) -
Julia Cuellar,
Mia Åstrand,
Heli Elovaara,
Annukka Pietikäinen,
Saija Sirén,
Arto Liljeblad,
Gabriela Guédez,
Tiina A. Salminen,
Jukka Hytönen
Publication year - 2020
Publication title -
infection and immunity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.508
H-Index - 220
eISSN - 1070-6313
pISSN - 0019-9567
DOI - 10.1128/iai.00962-19
Subject(s) - microscale thermophoresis , biology , borrelia burgdorferi , biochemistry , atp binding cassette transporter , transporter , periplasmic space , amino acid , borrelia , nucleic acid , purine , membrane transport protein , gene , genetics , antibody , enzyme , escherichia coli
Borrelia burgdorferi sensu 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. burgdorferi sensu 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.