Profiling excretory/secretory proteins of Trichinella spiralis muscle larvae by two-dimensional gel electrophoresis and mass spectrometry

• Published in: Veterinary parasitology 2005-09, Vol.132 (1), p.37-41
• Main Authors: Robinson, Mark W., Gare, Daniel C., Connolly, Bernadette
• Format: Article
• Language: English
• Subjects: Animals; Antigens, Helminth - chemistry; Antigens, Helminth - metabolism; Electrophoresis, Gel, Two-Dimensional; excretory-secretory products; gel electrophoresis; Helminth Proteins - chemistry; Helminth Proteins - metabolism; Larva; MALDI-TOF; MALDI-TOF mass spectrometry; mass spectrometry; Muscle larva; muscle larvae; Peptide Mapping - methods; protein identification; protein profile; Proteomics; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; T. spiralis; Trichinella spiralis; Trichinella spiralis - chemistry; Trichinella spiralis - metabolism
• ISSN: 0304-4017; 1873-2550
• DOI: 10.1016/j.vetpar.2005.05.019

Infection of mammalian skeletal muscle with the intracellular parasite Trichinella spiralis results in profound alterations in the host cell and a realignment of host cell gene expression. The role of parasite excretory/secretory (E/S) products in mediating these effects is unknown, largely due to the difficulty in identifying and assigning function to individual proteins. In this study, we have used two-dimensional electrophoresis to analyse the profile of muscle larva excreted/secreted proteins and have coupled this to protein identification using MALDI-TOF mass spectrometry. Interpretation of the peptide mass fingerprint data has relied primarily on the interrogation of a custom-made Trichinella EST database and the NemaGene cluster database for T. spiralis. Our results suggest that this proteomic approach is a useful tool to study protein expression in Trichinella spp. and will contribute to the identification of excreted/secreted proteins.