Abstract 1870 Crystal structure and ligand-binding specificity of the Borrelia burgdorferi proteins BmpA and BmpB

Borrelia burgdorferi is a diderm bacterium and the causative agent of Lyme disease. Studies have shown that proteins BmpA and BmpB bind to laminin, a key component of the host's extracellular matrix. However, previous research identified a paralogous protein, BmpD, as a nucleoside-binding protein. This raises the question of whether BmpA and BmpB also share this nucleoside-binding function or exclusively bind laminin. To elucidate the structure and function of BmpA, we determined its crystal structure at a resolution of 2.90 Å.

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Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.109939
Primary Topic
Insect and Pesticide Research
Type
article
Field-Weighted Citation Impact
0.00

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article

Abstract 1870 Crystal structure and ligand-binding specificity of the Borrelia burgdorferi proteins BmpA and BmpB

Qian Liu, Daniel Fernández, Naima G. Sharaf
Journal of Biological Chemistry
Insect and Pesticide Research
article

Abstract 1870 Crystal structure and ligand-binding specificity of the Borrelia burgdorferi proteins BmpA and BmpB

Qian Liu, Daniel Fernández, Naima G. Sharaf
article en

Abstract

Borrelia burgdorferi is a diderm bacterium and the causative agent of Lyme disease. Studies have shown that proteins BmpA and BmpB bind to laminin, a key component of the host's extracellular matrix. However, previous research identified a paralogous protein, BmpD, as a nucleoside-binding protein. This raises the question of whether BmpA and BmpB also share this nucleoside-binding function or exclusively bind laminin. To elucidate the structure and function of BmpA, we determined its crystal structure at a resolution of 2.90 Å.

Journal of Biological ChemistryVol. 301(5)
Stanford University (US)
National Institutes of Health
Zero hunger
Openalex Percentile: Top 88%
Insect and Pesticide Research
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