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旋毛形线虫新生幼虫特异性蛋白 Ts-NBL1 与宿主细胞中间丝蛋白 vimentin 相互作用。

A Trichinella spiralis new born larvae-specific protein, Ts-NBL1, interacts with host's cell vimentin.

机构信息

UMR BIPAR, Anses, Laboratoire de Santé Animale, INRAE, Ecole Nationale Vétérinaire d'Alfort, Maisons-Alfort, France.

Key Laboratory of Zoonosis Research, Ministry of Education, Institute of Zoonosis, College of Veterinary Medicine, Jilin University, Changchun, China.

出版信息

Parasitol Res. 2022 May;121(5):1369-1378. doi: 10.1007/s00436-022-07479-7. Epub 2022 Mar 23.

Abstract

The parasitic nematode Trichinella has a special relationship with its host as it has a unique intracellular location within the feeder cell which is a structure derived from skeletal muscle fiber. It has been proposed that "parakines" secreted by Trichinella larvae serve as messengers to implement communication between the parasite and the muscle cells through a molecular cross-talk to ensure permanent coexistence within the host. The Ts-NBL1 protein is considered to be a potential key "parakine" involved in the early invasion of the muscle fiber and its transformation into a feeder cell during Trichinella spiralis infection. This study used for the first time yeast two-hybrid (Y2H) technology in Trichinella to identify Ts-NBL1 interacting proteins. GST co-affinity purification experiments confirmed vimentin as an important interactor. The discovery of the new host proteins interacting with Ts-NBL1 will help to suggest that Ts-NBL1 contributes to participate in the capsule formation of feeder cells and provide ideas for understanding the molecular and cellular mechanisms involved in the survival of Trichinella in the host.

摘要

寄生性线虫旋毛虫与宿主之间存在特殊关系,因为它在吞噬细胞中有一个独特的细胞内位置,而吞噬细胞是一种源自骨骼肌纤维的结构。有人提出,旋毛虫幼虫分泌的“副肌肽”作为信使,通过分子串扰在寄生虫和肌肉细胞之间实现通讯,以确保在宿主中永久共存。Ts-NBL1 蛋白被认为是一种潜在的关键“副肌肽”,它参与旋毛虫感染过程中肌肉纤维的早期入侵及其向吞噬细胞的转化。本研究首次在旋毛虫中使用酵母双杂交(Y2H)技术来鉴定 Ts-NBL1 的相互作用蛋白。GST 共亲和纯化实验证实波形蛋白是一个重要的相互作用蛋白。发现与 Ts-NBL1 相互作用的新宿主蛋白有助于提示 Ts-NBL1 有助于参与吞噬细胞囊泡的形成,并为理解旋毛虫在宿主中生存所涉及的分子和细胞机制提供思路。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ac4a/8993751/2144921b279f/436_2022_7479_Fig1_HTML.jpg

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