ArticlePloS one2020
Immunoproteomic analysis of Trichinella spiralis and Trichinella britovi excretory-secretory muscle larvae proteins recognized by sera from humans infected with Trichinella.
Article in PloS one, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- Trichinella spiralis serine protease mediates larval invasion of gut epithelium via binding to CK8 and activating RhoA/ROCK1 pathway.PLoS neglected tropical diseases · 2025Article
- Comparative immunodiagnostic evaluation of recombinant serine proteases fromVeterinary world · 2025Article
- Enhanced Genomic and Transcriptomic Resources forInternational journal of molecular sciences · 2024Article
- Application of a recombinant novel trypsin from Trichinella spiralis for serodiagnosis of trichinellosis.Parasites & vectors · 2024Article
- Immunoblotting Identification of Diagnostic Antigens ofTropical medicine and infectious disease · 2023Article
- In vitro knockdown of TsDNase II-7 suppresses Trichinella spiralis invasion into the host's intestinal epithelial cells.PLoS neglected tropical diseases · 2023Article
- Infection ofInternational journal of molecular sciences · 2023Article
- Immunoproteomic Analysis ofPathogens (Basel, Switzerland) · 2022Article
- Hematological, biochemical, and serological parameters of experimentally infected rabbits withVeterinary world · 2022Article
- Insight intoPathogens (Basel, Switzerland) · 2022Article
- Identification and profiling of Trichinella spiralis circulating antigens and proteins in sera of mice with trichinellosis.PloS one · 2022Article
- Prospects of Using High-Throughput Proteomics to Underpin the Discovery of Animal Host-Nematode Interactions.Pathogens (Basel, Switzerland) · 2021Review
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6 authors at 2 institutions in 1 country.
Funding
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Abstract
The present study compares the immunogenic patterns of muscle larvae excretory-secretory proteins (ML E-S) from T. spiralis and T. britovi recognized by Trichinella-infected human sera. Samples were analyzed using two-dimensional electrophoresis (2-DE) coupled with 2D-immunoblot and liquid chromatography-tandem mass spectrometry LC-MS/MS analysis, two ELISA procedures and a confirmatory 1D-immunoblot test. Sera were obtained from nine patients with a history of ingestion of raw or undercooked meat who presented typical clinical manifestations of trichinellosis and from eleven healthy people. Specific anti-Trichinella IgG antibodies were detected in all samples tested with the Home-ELISA kits, but in only four samples for the commercially-available kit. The 1D-immunoblot results indicated that all nine serum samples were positive for T. spiralis ML E-S antigens, expressed as the presence of specific bands. In contrast, eight of the serum samples with T. britovi E-S ML antigens were positive, with one serum sample taken from a patient at 33dpi (days post infection) being negative. To identify immunoreactive proteins that are specifically recognized by host antibodies, both species of ML E-S proteins were subjected to 2D-immunoblotting with human serum taken at 49 dpi. The sera recognized 22 protein spots for T. spiralis and 18 for T. britovi in 2D-immunoblot analysis. Their molecular weights (MW) ranged from 50 to 60 kDa. LC-MS/MS analysis identified both common and specifically-recognized immunoreactive proteins: transmembrane serine protease 9, serine protease, antigen targeted by protective antibodies and Actin-1 partial were shared for both Trichinella species; hypothetical protein T01_7775 and P49 antigen, partial those specific to T. spiralis; deoxyribonuclease-2-alpha and hypothetical protein T03_17187/T12_7360 were specific to T. britovi. Our results demonstrate the value of 2-DE and 2D-immunblot as versatile tools for pinpointing factors contributing to the parasite-host relationship by comparing the secretomes of different Trichinella species.
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