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一种吸血寄生线虫的N-糖组和N-糖蛋白质组

N-glycome and N-glycoproteome of a hematophagous parasitic nematode .

作者信息

Wang Chunqun, Gao Wenjie, Yan Shi, Zhu Xing-Quan, Suo Xun, Liu Xin, Gupta Nishith, Hu Min

机构信息

State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, China.

College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, China.

出版信息

Comput Struct Biotechnol J. 2021 Apr 18;19:2486-2496. doi: 10.1016/j.csbj.2021.04.038. eCollection 2021.

DOI:10.1016/j.csbj.2021.04.038
PMID:34025939
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8113779/
Abstract

N-glycosylation is a physiologically vital post-translational modification of proteins in eukaryotic organisms. Initial work on - a blood-sucking nematode of ruminants with a broad geographical distribution - has shown that this parasite harbors N-glycans with exclusive chitobiose modifications. Besides, several immunogenic proteins (, amino- and metallo-peptidases) are known to be N-glycosylated in adult worms. However, an informative atlas of N-glycosylation in is not yet available. Herein, we report 291 N-glycosylated proteins with a total of 425 modification sites in the parasite. Among them, many peptidase families (, peptidase C1 and M1) including potential vaccine targets were enriched. Notably, the glycan-rich conjugates are distributed primarily in the intestine and gonads of adult worms, and consequently hidden from the host's immune system. Collectively, these data provide a comprehensive atlas of N-glycosylation in a prevalent parasitic nematode while underlining its significance for infection, immunity and prevention.

摘要

N-糖基化是真核生物中蛋白质一种对生理功能至关重要的翻译后修饰。对捻转血矛线虫(一种广泛分布的反刍动物吸血线虫)的初步研究表明,这种寄生虫含有仅带有壳二糖修饰的N-聚糖。此外,已知几种免疫原性蛋白(如丝氨酸蛋白酶、氨基肽酶和金属肽酶)在成虫中发生N-糖基化。然而,目前尚无捻转血矛线虫N-糖基化的信息图谱。在此,我们报告了该寄生虫中291种N-糖基化蛋白,共有425个修饰位点。其中,包括潜在疫苗靶点在内的许多肽酶家族(如肽酶C1和M1)得到了富集。值得注意的是,富含聚糖的结合物主要分布在成虫的肠道和性腺中,因此能躲避宿主的免疫系统。总体而言,这些数据提供了一种常见寄生线虫N-糖基化的综合图谱,同时强调了其在感染、免疫和预防方面的重要性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/488c/8113779/f07bc8ec44ab/fx1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/488c/8113779/5ab95d56c175/ga1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/488c/8113779/4aa59269ae71/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/488c/8113779/08661a7f4a88/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/488c/8113779/380e1059593a/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/488c/8113779/cc4e7d6936a3/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/488c/8113779/d1eb4a55776e/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/488c/8113779/b12918649561/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/488c/8113779/f07bc8ec44ab/fx1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/488c/8113779/5ab95d56c175/ga1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/488c/8113779/4aa59269ae71/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/488c/8113779/08661a7f4a88/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/488c/8113779/380e1059593a/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/488c/8113779/cc4e7d6936a3/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/488c/8113779/d1eb4a55776e/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/488c/8113779/b12918649561/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/488c/8113779/f07bc8ec44ab/fx1.jpg

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