Label-free quantitative proteomic analysis of molting-related proteins of Trichinella spiralis intestinal infective larvae

Abstract Molting is a key step for body-size expansion and environmental adaptation of parasitic nematodes, and it is extremely important for Trichinella spiralis growth and development, but the molting mechanism is not fully understood. In this work, label-free LC–MS/MS was used to determine the pr...

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Main Authors: Hua Nan Ren, Ruo Dan Liu, Yan Yan Song, Tong Xu Zhuo, Kai Xia Guo, Yao Zhang, Peng Jiang, Zhong Quan Wang, Jing Cui
Format: Article
Language:English
Published: BMC 2019-09-01
Series:Veterinary Research
Online Access:http://link.springer.com/article/10.1186/s13567-019-0689-0
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spelling doaj-0a4a021256fd46e682a88d7ead9ad97a2020-11-25T03:01:50ZengBMCVeterinary Research1297-97162019-09-0150111410.1186/s13567-019-0689-0Label-free quantitative proteomic analysis of molting-related proteins of Trichinella spiralis intestinal infective larvaeHua Nan Ren0Ruo Dan Liu1Yan Yan Song2Tong Xu Zhuo3Kai Xia Guo4Yao Zhang5Peng Jiang6Zhong Quan Wang7Jing Cui8Department of Parasitology, Medical College, Zhengzhou UniversityDepartment of Parasitology, Medical College, Zhengzhou UniversityDepartment of Parasitology, Medical College, Zhengzhou UniversityDepartment of Parasitology, Medical College, Zhengzhou UniversityDepartment of Parasitology, Medical College, Zhengzhou UniversityDepartment of Parasitology, Medical College, Zhengzhou UniversityDepartment of Parasitology, Medical College, Zhengzhou UniversityDepartment of Parasitology, Medical College, Zhengzhou UniversityDepartment of Parasitology, Medical College, Zhengzhou UniversityAbstract Molting is a key step for body-size expansion and environmental adaptation of parasitic nematodes, and it is extremely important for Trichinella spiralis growth and development, but the molting mechanism is not fully understood. In this work, label-free LC–MS/MS was used to determine the proteome differences between T. spiralis muscle larvae (ML) at the encapsulated stage and intestinal infective larvae (IIL) at the molting stage. The results showed that a total of 2885 T. spiralis proteins were identified, 323 of which were differentially expressed. These proteins were involved in cuticle structural elements, regulation of cuticle synthesis, remodeling and degradation, and hormonal regulation of molting. These differential proteins were also involved in diverse intracellular pathways, such as fatty acid biosynthesis, arachidonic acid metabolism, and mucin type O-glycan biosynthesis. qPCR results showed that five T. spiralis genes (cuticle collagen 14, putative DOMON domain-containing protein, glutamine synthetase, cathepsin F and NADP-dependent isocitrate dehydrogenase) had significantly higher transcriptional levels in 10 h IIL than ML (P < 0.05), which were similar to their protein expression levels, suggesting that they might be T. spiralis molting-related genes. Identification and characterization of T. spiralis molting-related proteins will be helpful for developing vaccines and new drugs against the early enteral stage of T. spiralis.http://link.springer.com/article/10.1186/s13567-019-0689-0
collection DOAJ
language English
format Article
sources DOAJ
author Hua Nan Ren
Ruo Dan Liu
Yan Yan Song
Tong Xu Zhuo
Kai Xia Guo
Yao Zhang
Peng Jiang
Zhong Quan Wang
Jing Cui
spellingShingle Hua Nan Ren
Ruo Dan Liu
Yan Yan Song
Tong Xu Zhuo
Kai Xia Guo
Yao Zhang
Peng Jiang
Zhong Quan Wang
Jing Cui
Label-free quantitative proteomic analysis of molting-related proteins of Trichinella spiralis intestinal infective larvae
Veterinary Research
author_facet Hua Nan Ren
Ruo Dan Liu
Yan Yan Song
Tong Xu Zhuo
Kai Xia Guo
Yao Zhang
Peng Jiang
Zhong Quan Wang
Jing Cui
author_sort Hua Nan Ren
title Label-free quantitative proteomic analysis of molting-related proteins of Trichinella spiralis intestinal infective larvae
title_short Label-free quantitative proteomic analysis of molting-related proteins of Trichinella spiralis intestinal infective larvae
title_full Label-free quantitative proteomic analysis of molting-related proteins of Trichinella spiralis intestinal infective larvae
title_fullStr Label-free quantitative proteomic analysis of molting-related proteins of Trichinella spiralis intestinal infective larvae
title_full_unstemmed Label-free quantitative proteomic analysis of molting-related proteins of Trichinella spiralis intestinal infective larvae
title_sort label-free quantitative proteomic analysis of molting-related proteins of trichinella spiralis intestinal infective larvae
publisher BMC
series Veterinary Research
issn 1297-9716
publishDate 2019-09-01
description Abstract Molting is a key step for body-size expansion and environmental adaptation of parasitic nematodes, and it is extremely important for Trichinella spiralis growth and development, but the molting mechanism is not fully understood. In this work, label-free LC–MS/MS was used to determine the proteome differences between T. spiralis muscle larvae (ML) at the encapsulated stage and intestinal infective larvae (IIL) at the molting stage. The results showed that a total of 2885 T. spiralis proteins were identified, 323 of which were differentially expressed. These proteins were involved in cuticle structural elements, regulation of cuticle synthesis, remodeling and degradation, and hormonal regulation of molting. These differential proteins were also involved in diverse intracellular pathways, such as fatty acid biosynthesis, arachidonic acid metabolism, and mucin type O-glycan biosynthesis. qPCR results showed that five T. spiralis genes (cuticle collagen 14, putative DOMON domain-containing protein, glutamine synthetase, cathepsin F and NADP-dependent isocitrate dehydrogenase) had significantly higher transcriptional levels in 10 h IIL than ML (P < 0.05), which were similar to their protein expression levels, suggesting that they might be T. spiralis molting-related genes. Identification and characterization of T. spiralis molting-related proteins will be helpful for developing vaccines and new drugs against the early enteral stage of T. spiralis.
url http://link.springer.com/article/10.1186/s13567-019-0689-0
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