微巴贝斯虫表面抗原∆∆BmSA1的1H、13C和15N主链和侧链共振分配

IF 0.8 4区 生物学 Q4 BIOPHYSICS
Assia Mouhand, Joana Pissarra, Stéphane Delbecq, Christian Roumestand, Philippe Barthe
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引用次数: 0

摘要

人类巴贝斯虫病是一种媒介传播的人畜共患传染病,主要由Apicocomplian寄生虫微小巴贝斯虫引起,分布在世界各地。感染可导致严重症状,如溶血性贫血,尤其是免疫缺陷患者。此外,无症状患者作为未经筛查的献血者继续传播,这对公共卫生构成了风险。早期的宿主-寄生虫相互作用是由BmSA1介导的,BmSA1是微小巴贝斯虫的主要表面抗原,对入侵和免疫逃逸至关重要。因此,BmSA1蛋白的结构和功能表征构成了开发控制感染的创新工具的第一个战略里程碑。了解这种重要抗原的3D结构对于开发疫苗或新的诊断测试至关重要。在这里,我们报道了∆∆BmSA1的1H、15N和13C NMR共振归属,这是BmSA1一种没有N端信号肽和疏水性C端GPI锚的截短重组版本。使用CSI.3和TALOS-N的二级结构预测显示了高含量的α螺旋结构。这项初步研究为BMSA1的进一步结构表征提供了基础。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

1H, 13C and 15N backbone and side-chain resonance assignments of ∆∆BmSA1, the surface antigen of Babesia microti

1H, 13C and 15N backbone and side-chain resonance assignments of ∆∆BmSA1, the surface antigen of Babesia microti

Human babesiosis is a vector-borne zoonotic infection caused mostly by the Apicomplexan parasite Babesia microti, distributed worldwide. The infection can result in severe symptoms such as hemolytic anemia, especially in immunodeficient patients. Also, asymptomatic patients continue transmission as unscreened blood donors, and represent a risk for Public Health. Early host-parasite interactions are mediated by BmSA1, the major surface antigen of Babesia microti, crucial for invasion and immune escape. Hence, a structural and functional characterization of the BmSA1 protein constitutes a first strategic milestone toward the development of innovative tools to control infection. Knowledge of the 3D structure of such an important antigen is crucial for the development of vaccines or new diagnostic tests. Here, we report the 1H, 15N and 13C NMR resonance assignment of ∆∆BmSA1, a truncated recombinant version of BmSA1 without the N-terminal signal peptide and the hydrophobic C-terminal GPI-anchor. Secondary structure prediction using CSI.3 and TALOS-N demonstrates a high content of alpha-helical structure. This preliminary study provides foundations for further structural characterization of BMSA1.

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来源期刊
Biomolecular NMR Assignments
Biomolecular NMR Assignments 生物-光谱学
CiteScore
1.70
自引率
11.10%
发文量
59
审稿时长
6-12 weeks
期刊介绍: Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties. Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.
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