Analysis of a 43-kDa glycoprotein from the intracellular parasitic nematode Trichinella spiralis

The L1 larvae of the parasitic nematode Trichinella spiralis invade skeletal muscle and initiate a process that has been interpreted to represent skeletal muscle dedifferentiation. In this process, the infected region of the muscle cell is converted into a unique structure, called the Nurse cell. Th...

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Bibliographic Details
Published in:The Journal of biological chemistry 1992-09, Vol.267 (26), p.18459-18465
Main Authors: Vassilatis, D.K. (Merck Sharp and Dohme Research Laboratories, Rahway, NJ), Despommier, D, Misek, D.E, Polvere, R.I, Gold, A.M, Ploeg, L.H.T. van der
Format: Article
Language:English
Subjects:
ADN
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
antibodies
Base Sequence
Biochemistry & Molecular Biology
Biological and medical sciences
Blotting, Northern
Blotting, Southern
Blotting, Western
cDNA
Cell Nucleus - metabolism
DNA
formation
Fundamental and applied biological sciences. Psychology
genes
GLICOPROTEINAS
GLYCOPROTEINE
Glycoproteins
Glycoproteins - chemistry
Glycoproteins - genetics
Glycoproteins - metabolism
Immunohistochemistry
Life Sciences & Biomedicine
METABOLISME DES PROTEINES
METABOLISMO PROTEICO
Molecular Sequence Data
nucleotide sequence
Nurse cell
predictions
Protein Conformation
Proteins
RNA - analysis
Science & Technology
secretion
SECUENCIA NUCLEICA
SEQUENCE NUCLEIQUE
Trichinella - metabolism
TRICHINELLA SPIRALIS
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Summary:The L1 larvae of the parasitic nematode Trichinella spiralis invade skeletal muscle and initiate a process that has been interpreted to represent skeletal muscle dedifferentiation. In this process, the infected region of the muscle cell is converted into a unique structure, called the Nurse cell. The nematode T. spiralis can survive for tens of years within the cytoplasm of the Nurse cell and secretes proteins into the cytoplasm that are believed to play a role in mediating the Nurse cell formation or maintenance. We have cloned a cDNA encoding the T. spiralis-derived, 43-kDa secreted protein. Structural analysis of the predicted 344-amino acid sequence revealed an N terminally located signal peptide and a potential helix-loop-helix motif in the main body of the protein. Antibodies raised against the 43-kDa recombinant protein were used in immunocytolocalizations of T. spiralis-infected skeletal muscle sections. These antibodies strongly stained the Nurse cell nuclei and the nematode itself. Specific, though slightly weaker staining also occurred in the Nurse cell cytoplasm. In Western blots, the antibodies react with the 43-kDa protein but also detected at least two other T. spiralis-secreted proteins. DNA hybridizations reveal at least one additional 43-kDa-related sequence encoded in the T. spiralis genome. We conclude that either the 43-kda protein and/or a closely related 43-kDa family member is secreted into the muscle and translocates to the muscle-derived nuclei. This model may provide insights into the mechanisms involved in Nurse cell formation
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)36985-6