Proteomic analysis of the pinworm Syphacia muris (Nematoda: Oxyuridae), a parasite of laboratory rats

• Published in: Parasitology international 2012-12, Vol.61 (4), p.561-564
• Main Authors: Sotillo, Javier, Trelis, María, Cortés, Alba, Valero, María Luz, del Pino, Manuel Sánchez, Esteban, José Guillermo, Marcilla, Antonio, Toledo, Rafael
• Format: Article
• Language: English
• Subjects: adults; Animals; bioassays; biological development; calcium-binding proteins; cell cycle; computer software; enzymes; Gastroenterology and Hepatology; Gene Expression Regulation - physiology; Helminth Proteins - genetics; Helminth Proteins - metabolism; host-parasite relationships; Infectious Disease; Laboratory Animal Science; liquid chromatography; Nematoda; Nematode Infections - parasitology; Nematode Infections - veterinary; Oxyuridae; Oxyuroidea - genetics; Oxyuroidea - metabolism; parasites; parasitology; protein metabolism; proteome; Proteomics; Rats; Rats, Wistar; receptors; Rodent Diseases - parasitology; Rodents; Syphacia; Syphacia muris; tandem mass spectrometry; Transcriptome; transmembrane proteins
• ISSN: 1383-5769; 1873-0329
• DOI: 10.1016/j.parint.2012.05.004

Abstract Syphacia muris (Nematoda: Oxyuridae) is a ubiquitous nematode that commonly infects rats in the laboratory which can interfere in the development of biological assays. The somatic extract of S. muris adults collected from infected rats was investigated using a proteomic approach. A shot-gun liquid chromatography/tandem mass spectrometry procedure was used. We used the MASCOT search engine (Matrix-Science) and ProteinPilot software v2.0 (Applied Biosystems) for the database search. A total of 359 proteins were accurately identified from the worms. The largest protein families consisted of metabolic enzymes and those involved in the nucleic metabolism and cell cycle. Proteins of transmembrane receptors and those involved in protein metabolism, chaperones, structural and motor, signalling and calcium-binding proteins also were identified in the proteome of S. muris . Proteome array of S. muris may contribute to further elucidation of biological system of S. muris as well as host–parasite relationships.