Structural highlights
Publication Abstract from PubMedBorrelia 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. Structural and biomolecular analyses of Borrelia burgdorferi BmpD reveal a substrate-binding protein of an ABC-type nucleoside transporter family.,Cuellar J, Astrand M, Elovaara H, Pietikainen A, Siren S, Liljeblad A, Guedez G, Salminen TA, Hytonen J Infect Immun. 2020 Jan 27. pii: IAI.00962-19. doi: 10.1128/IAI.00962-19. PMID:31988175[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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