Identification and profiling of Trichinella spiralis circulating antigens and proteins in sera of mice with trichinellosis

Abstract

Trichinellosis is a zoonotic disease caused by the ingestion of the Trichinella nematode. With a worldwide incidence of approximately 10,000 cases per year, Trichinella spiralis is responsible for most human infections. There are no specific signs or symptoms of this parasitic infection. Muscle biopsy is the gold diagnostic standard for trichinellosis, but the technique is invasive and unable to detect the early stage of infection. Although immunodiagnostics are also available, antibody detection usually occurs after 3 weeks and prolonged up to 19 years after the acute phase. Therefore, additional diagnostic biomarkers must be identified to improve trichinellosis diagnosis. This study aimed to measure concentration changes in mouse serum proteins prior to T. spiralis infection and 2, 4 and 8 weeks after infection, and to identify T. spiralis circulating proteins and antigens using mass spectrometry-based proteomics. Mouse muscle-related proteins including inter-alpha-trypsin inhibitor heavy chain H2, a protein involved in the response to muscle tissue damage, were up-regulated in mouse sera during the T. spiralis larvae invasion. Additionally, 33 circulatory parasite proteins were identified in infected mouse sera. Notably, T. spiralis long-chain fatty acid transport protein 1 could be detected in the early stage of infection and peroxidasin-like protein was identified 2, 4 and 8 weeks after infection. Seventeen T. spiralis circulating antigens were detected in mouse immune complexes, with PX domain protein being found 2, 4 and 8 weeks after infection. Because peroxidasin-like protein and PX domain protein were detected at all post-infection time points, sequence alignments of these proteins were performed, which showed they are conserved among Trichinella spp. and have less similarity to the human and murine sequences. Integrative analysis of T. spiralis biomarkers throughout the course of infection may reveal additional diagnostic targets to improve early diagnosis of trichinellosis.

Untargeted serum metabolomics analysis of Trichinella spiralis-infected mouse

“…All compounds in the KEGG pathway library were used for reference metabolome of mice ( Mus musculus ). In addition, data of serum proteome from previous study of our group [ 37 ] was integrated into metabolomic data of the current study. Uniprot protein ID of proteins and HMDB ID were input into “Joint Pathway-Analysis” module of Metaboanalyst online platform version 5.0.…”

Pleural effusion caused by Trichinella spiralis infection: two case reports

“…Therefore, it is not recommended for the diagnosis of Trichinosis . The discovery of Trichinella larvae cysts from muscle biopsy is the gold standard for the diagnosis of Trichinosis , but due to its invasiveness, the positive rate is only about 50%, and early infection cannot be detected, so it is not recommended [ 9 ]. The European Center for Disease Control has classified human Trichinosis into the clinical, laboratory, and epidemiological cases, of which laboratory cases refer to Trichinosis larvae found by muscle biopsy or seropositive.…”

Immunoproteomic Analysis of Trichinella britovi Proteins Recognized by IgG Antibodies from Meat Juice of Carnivores Naturally Infected with T. britovi

“…Unsurprisingly, there is a great interest in identifying peptide or protein biomarkers that could be used as markers to identify early Trichinella infection in humans and domestic animals (diagnostic properties) or as vaccines against Trichinella infection, e.g., in pigs (immunoprotective properties). Although recent studies have focused on the immunoreactive proteins in host serum and plasma during Trichinella infection, they have mainly been based on 2DE-electrophoresis examination coupled with LC-MS/MS, or 2DE electrophoresis followed by MALDI-TOF mass spectrometry of human, mouse, or pig samples [ 30 , 36 , 37 , 38 , 39 , 47 , 48 , 49 , 50 , 51 , 52 , 53 ]. In contrast, the present paper employs standard 1DE electrophoresis coupled with LC-MS/MS analysis to obtain preliminary findings; it is the first proteomic analysis of proteins recognized by meat juice samples collected from wildlife.…”

“…Most studies have used serum/plasma samples to determine the protein profile characteristic of Trichinella infection [ 14 , 30 , 36 , 37 , 38 , 39 , 47 , 48 , 49 , 51 , 52 , 53 ]. However, while serum or plasma are not always available for analysis, meat juice samples provide an adequate, alternative matrix that can be easily obtained for post-mortem analysis, especially from free-living animals.…”