title: Trichinella spiralis: altered expression of muscle proteins in trichinosis.
abstract: Mammalian muscle undergoes significant alterations morphologically, ultrastructurally, and biochemically following infection by Trichinella spiralis larvae. To investigate this host/parasite relationship in more detail, a new method to isolate T. spiralis-infected cells (nurse cells) in preparative quantities was developed. Nurse cells isolated by sequential protease treatments contain larvae and retain many of the characteristics of those in situ. When analyzed by SDS-PAGE, a wide range of proteins detected in nurse cells were not apparent in muscle by the methods employed. Proteins associated with the nurse cell capsule and organellar fractions appear to account for most of the dominant nurse cell proteins. In contrast, most major muscle proteins were either reduced in abundance or undetectable in nurse cells. The myofibrillar proteins myosin heavy chain, alpha-actin, and alpha- and beta-tropomyosin were identified using antibody reagents and two-dimensional PAGE analysis. None of these proteins were detectable in nurse cells and except for beta-tropomyosin, the relative abundance of these proteins was a minimum 100-fold lower compared to muscle. The data indicate that the reduction of muscle products in the nurse cell is much greater than previously reported. The inability to detect myofibrillar proteins raises the possibility that the nurse cell is not blocked in a regenerating muscle phenotype as previously suggested. Availability of isolated nurse cells in large quantity should facilitate resolution of this and other issues regarding the T. spiralis/skeletal muscle relationship.
authors.affiliation: Department of Veterinary Microbiology and Pathology, Washington State University, Pullman 99164-7040.
authors.forename: D P
authors.initials: DP
authors.lastname: Jasmer
mesh_terms: D000818:Animals; D015153:Blotting, Western; D002478:Cells, Cultured; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D051379:Mice; D009124:Muscle Proteins / Q000032:analysis*; D009132:Muscles / Q000378:metabolism / Q000469:parasitology* / Q000473:pathology; D014235:Trichinellosis / Q000378:metabolism* / Q000473:pathology
chemical_list: D009124:Muscle Proteins