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可变脂蛋白血凝素蛋白的结构同源性建模与功能表征

structural homology modeling and functional characterization of variable lipoprotein hemagglutin proteins.

作者信息

Mugunthan Susithra Priyadarshni, Harish Mani Chandra

机构信息

Department of Biotechnology, Thiruvalluvar University, Vellore, India.

出版信息

Front Vet Sci. 2022 Aug 4;9:943831. doi: 10.3389/fvets.2022.943831. eCollection 2022.

DOI:10.3389/fvets.2022.943831
PMID:35990271
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9386052/
Abstract

variable lipoprotein hemagglutin (vlhA) proteins are crucial for immune evasion from the host cells, permitting the persistence and survival of the pathogen. However, the exact molecular mechanism behind the immune evasion function is still not clear. physiochemical analysis, domain analysis, subcellular localization, and homology modeling studies have been carried out to predict the structural and functional properties of these proteins. The outcomes of this study provide significant preliminary data for understanding the immune evasion by vlhA proteins. In this study, we have reported the primary, secondary, and tertiary structural characteristics and subcellular localization, presence of the transmembrane helix and signal peptide, and functional characteristics of vlhA proteins from strain R low. The results show variation between the structural and functional components of the proteins, signifying the role and diverse molecular mechanisms in functioning of vlhA proteins in host immune evasion. Moreover the 3D structure predicted in this study will pave a way for understanding vlhA protein function and its interaction with other molecules to undergo immune evasion. This study forms the basis for future experimental studies improving our understanding in the molecular mechanisms used by vlhA proteins.

摘要

可变脂蛋白血凝素(vlhA)蛋白对于病原体逃避宿主细胞免疫、实现持续存在和存活至关重要。然而,免疫逃避功能背后的确切分子机制仍不清楚。已开展了物理化学分析、结构域分析、亚细胞定位及同源建模研究,以预测这些蛋白的结构和功能特性。本研究结果为理解vlhA蛋白介导的免疫逃避提供了重要的初步数据。在本研究中,我们报告了来自R low菌株的vlhA蛋白的一级、二级和三级结构特征、亚细胞定位、跨膜螺旋和信号肽的存在情况以及功能特性。结果显示这些蛋白的结构和功能成分存在差异,这表明vlhA蛋白在宿主免疫逃避中发挥作用及具有多种分子机制。此外,本研究预测的三维结构将为理解vlhA蛋白功能及其与其他分子相互作用以实现免疫逃避铺平道路。本研究为未来实验研究奠定了基础,有助于增进我们对vlhA蛋白所采用分子机制的理解。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/56fe/9386052/8096fe0c15ca/fvets-09-943831-g0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/56fe/9386052/7532c4fdf3ca/fvets-09-943831-g0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/56fe/9386052/8fce96411ded/fvets-09-943831-g0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/56fe/9386052/9ae2e1affffb/fvets-09-943831-g0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/56fe/9386052/8096fe0c15ca/fvets-09-943831-g0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/56fe/9386052/7532c4fdf3ca/fvets-09-943831-g0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/56fe/9386052/8fce96411ded/fvets-09-943831-g0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/56fe/9386052/9ae2e1affffb/fvets-09-943831-g0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/56fe/9386052/8096fe0c15ca/fvets-09-943831-g0004.jpg

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Vet Microbiol. 2020 Dec;251:108891. doi: 10.1016/j.vetmic.2020.108891. Epub 2020 Oct 10.
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