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缺乏所有cp32原噬菌体质粒的伯氏疏螺旋体在小鼠中仍具有完全的感染性。

Borrelia burgdorferi lacking all cp32 prophage plasmids retains full infectivity in mice.

作者信息

Hillman Chad, Theriault Hannah, Dmitriev Anton, Hansra Satyender, Rosa Patricia A, Wachter Jenny

机构信息

Laboratory of Bacteriology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT, USA.

Department of Biomedical Sciences, School of Public Health, State University of New York, Albany, NY, 12144, USA.

出版信息

EMBO Rep. 2025 Apr;26(8):1997-2012. doi: 10.1038/s44319-025-00378-9. Epub 2025 Mar 19.

DOI:10.1038/s44319-025-00378-9
PMID:40108404
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC12018966/
Abstract

The causative agent of Lyme disease, Borrelia burgdorferi, contains a unique, segmented genome comprising multiple linear and circular plasmids. To date, the genomes of over 63 sequenced Lyme disease Borrelia carry one or more 32 kbp circular plasmids (cp32) or cp32-like elements. The cp32 plasmids are endogenous prophages and encode, among other elements, a family of surface exposed lipoproteins termed OspEF-related proteins. These lipoproteins are synthesized during mammalian infection and are considered important components of the spirochete's adaptive response to the vertebrate host. Here, we detail the construction and infectivity of the first described B. burgdorferi strain lacking all cp32 plasmids. Despite their universal presence, our findings indicate that B. burgdorferi does not require any cp32 plasmids to complete the experimental mouse-tick-mouse infectious cycle and a total lack of cp32s does not impair spirochete infectivity.

摘要

莱姆病的病原体伯氏疏螺旋体含有一个独特的分段基因组,由多个线性和环状质粒组成。迄今为止,超过63个已测序的莱姆病疏螺旋体基因组携带一个或多个32 kbp的环状质粒(cp32)或cp32样元件。cp32质粒是内源性原噬菌体,除其他元件外,还编码一类表面暴露的脂蛋白,称为OspEF相关蛋白。这些脂蛋白在哺乳动物感染期间合成,被认为是螺旋体对脊椎动物宿主适应性反应的重要组成部分。在这里,我们详细描述了首个被描述的缺乏所有cp32质粒的伯氏疏螺旋体菌株的构建及其感染性。尽管cp32普遍存在,但我们的研究结果表明,伯氏疏螺旋体完成实验性小鼠-蜱-小鼠感染周期不需要任何cp32质粒,完全缺乏cp32也不会损害螺旋体的感染性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75a6/12018966/6406fdec17e6/44319_2025_378_Fig5_ESM.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75a6/12018966/d9e6bda63f22/44319_2025_378_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75a6/12018966/fc4808ff5f3f/44319_2025_378_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/75a6/12018966/2b52902e2c57/44319_2025_378_Fig4_ESM.jpg
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PLoS Pathog. 2023 Aug 31;19(8):e1011243. doi: 10.1371/journal.ppat.1011243. eCollection 2023 Aug.
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Nat Commun. 2023 Jan 13;14(1):198. doi: 10.1038/s41467-023-35897-3.
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Outer surface lipoproteins from the Lyme disease spirochete exploit the molecular switch mechanism of the complement protease C1s.
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Proc Natl Acad Sci U S A. 2022 Mar 29;119(13):e2117770119. doi: 10.1073/pnas.2117770119. Epub 2022 Mar 21.
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