Evidence map›Paper›PMID 31547875›Full record

ArticleVeterinary research2019

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

Hua Nan Ren, Ruo Dan Liu, Yan Yan Song, Tong Xu Zhuo, Kai Xia Guo, Yao Zhang, Peng Jiang, Zhong Quan Wang, Jing Cui

Open access · goldAbstract read
In one paragraph

Article in Veterinary research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.2field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

39 citing papers in PubMed, 75 citations in OpenAlex.

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  8. A NovelInternational journal of molecular sciences · 2024
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  11. AdvancingPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 1 institution in 1 country.

Hua Nan RenDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China.
Ruo Dan LiuDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China.
Yan Yan SongDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China.
Tong Xu ZhuoDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China.
Kai Xia GuoDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China.
Yao ZhangDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China.
Peng JiangDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China.
Zhong Quan WangDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China. wangzq2015@126.com.
Jing CuiDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China. cuij@zzu.edu.cn.
Zhengzhou University · CN

Funding

National Natural Science Foundation of China 81871673
6 · The paper itself

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.

Indexed as

AnimalsChromatography, LiquidFemaleHelminth ProteinsLarvaMiceMoltingProteomicsSpecific Pathogen-Free OrganismsSus scrofaSwineSwine DiseasesTandem Mass SpectrometryTrichinella spiralisTrichinellosisHelminth Proteins

Identifiers

PMID31547875
PMCPMC6757440
OpenAlexW2975983327

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.