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伯氏疏螺旋体肽聚糖相互作用蛋白（BpiP）有助于伯氏疏螺旋体对宿主来源因子的适应能力，并影响莱姆病小鼠模型中的毒力。

Borrelia peptidoglycan interacting Protein (BpiP) contributes to the fitness of Borrelia burgdorferi against host-derived factors and influences virulence in mouse models of Lyme disease.

机构信息

South Texas Center for Emerging Infectious Diseases (STCEID) and Department of Biology, The University of Texas at San Antonio, San Antonio, Texas, United States of America.

出版信息

PLoS Pathog. 2021 Apr 21;17(4):e1009535. doi: 10.1371/journal.ppat.1009535. eCollection 2021 Apr.

DOI:10.1371/journal.ppat.1009535
PMID:33882111
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8092773/
Abstract

The Peptidoglycan (PG) cell wall of the Lyme disease (LD) spirochete, Borrelia burgdorferi (Bb), contributes to structural and morphological integrity of Bb; is a persistent antigen in LD patients; and has a unique pentapeptide with L-Ornithine as the third amino acid that cross-links its glycan polymers. A borrelial homolog (BB_0167) interacted specifically with borrelilal PG via its peptidoglycan interacting motif (MHELSEKRARAIGNYL); was localized to the protoplasmic cylinder of Bb; and was designated as Borrelia peptidoglycan interacting Protein (BpiP). A bpiP mutant displayed no defect under in vitro growth conditions with similar levels of several virulence-related proteins. However, the burden of bpiP mutant in C3H/HeN mice at day 14, 28 and 62 post-infection was significantly lower compared to control strains. No viable bpiP mutant was re-isolated from any tissues at day 62 post-infection although bpiP mutant was able to colonize immunodeficient SCID at day 28 post-infection. Acquisition or transmission of bpiP mutant by Ixodes scapularis larvae or nymphs respectively, from and to mice, was significantly lower compared to control strains. Further analysis of bpiP mutant revealed increased sensitivity to vancomycin, osmotic stress, lysosomal extracts, human antimicrobial peptide cathelicidin-LL37, complement-dependent killing in the presence of day 14 post-infection mouse serum and increased internalization of CFSC-labeled bpiP mutant by macrophages and dendritic cells compared to control strains. These studies demonstrate the importance of accessory protein/s involved in sustaining integrity of PG and cell envelope during different phases of Bb infection.

摘要

莱姆病螺旋体（Borrelia burgdorferi，Bb）的肽聚糖（PG）细胞壁有助于维持 Bb 的结构和形态完整性；是莱姆病患者体内持续存在的抗原；并且具有独特的五肽，其中第三个氨基酸是 L-鸟氨酸，可使聚糖聚合物交联。一种鲍氏螺旋体同源物（BB_0167）通过其肽聚糖相互作用基序（MHELSEKRARAIGNYL）与鲍氏螺旋体 PG 特异性相互作用；定位于 Bb 的原生质圆柱；并被指定为鲍氏螺旋体肽聚糖相互作用蛋白（BpiP）。bpiP 突变体在体外生长条件下没有缺陷，并且几种与毒力相关的蛋白质水平相似。然而，与对照株相比，bpiP 突变体在感染后第 14、28 和 62 天的 C3H/HeN 小鼠中的负担明显降低。尽管 bpiP 突变体能在感染后第 28 天定植免疫缺陷 SCID 小鼠，但在感染后第 62 天，从任何组织中都没有再分离出活的 bpiP 突变体。与对照株相比，bpiP 突变体在从和向小鼠的 Ixodes scapularis 幼虫或若虫中的获得或传播分别显著降低。对 bpiP 突变体的进一步分析表明，与对照株相比，该突变体对万古霉素、渗透压应激、溶酶体提取物、人抗菌肽 cathelicidin-LL37、感染后第 14 天小鼠血清存在时的补体依赖性杀伤以及 CFSC 标记的 bpiP 突变体被巨噬细胞和树突状细胞内化的敏感性增加。这些研究表明，在 Bb 感染的不同阶段，参与维持 PG 和细胞包膜完整性的辅助蛋白/复合物的重要性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5380/8092773/eca694975f6c/ppat.1009535.g018.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5380/8092773/326f02a362af/ppat.1009535.g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5380/8092773/66ad89872c51/ppat.1009535.g010.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5380/8092773/2a5642424064/ppat.1009535.g011.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5380/8092773/865a3cd7cf40/ppat.1009535.g012.jpg
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