TY - JOUR
T1 - Molecular cloning of Schistosoma mansoni myosin
AU - Newport, George R.
AU - Harrison, Robert A.
AU - McKerrow, James
AU - Tarr, Phil
AU - Kallestad, Jeff
AU - Agabian, Nina
N1 - Funding Information:
The authors express their appreciation to R. Hedstrom and E. Jong for useful discussions. We also thank Dr. R. Doolittle for help in aligning our predicted amino acid sequences with that of other proteins, and Caro Hopper for assistance in preparing the manuscript. This work was funded, in part, by grants from the National Institutes of Health (NIH), the Rockefeller Foundation GND, the Edna McConnell Clark Foundation, the John D. and Catherine T. MacArthur Foundation, and the Office of Naval Research, Contract N00014-81-C-0570. R.H. is a recipient of a Wellcome Trust Advanced Training Fellowship and N.A. is a Burroughs Wellcome Scholar of Molecular Parasitology.
PY - 1987/11
Y1 - 1987/11
N2 - A cDNA library representative of adult Schistosoma mansoni mRNA populations was screened with serum from infected rats (refractory hosts), positive plaques being rescreened with serum from infected mice and humans. Based on general reactivity, one clone was selected for further study. As judged by immunofluorescence data, size of corresponding mRNA, and nucleotide sequence analysis, the recombinant expresses approximately 625 amino acids of a schistosome muscle myosin rod. Antibodies evoked by the protein do not cross-react with human cardiac or skeletal muscle, are not invariably stimulated in naturally infected human beings, and rise in titer after chemotherapeutic cure, findings which suggest that the antigen is not a causative agent of Katayama fever, and is probably presented by degenerating worms. The schistosome myosin gene, the most primitive examined to date, appears to be unique inasmuch as it may not be a member of a multigene family and encodes a single mRNA transcript; nonetheless, predicted higher order structure of its translation product is consistent with expected function.
AB - A cDNA library representative of adult Schistosoma mansoni mRNA populations was screened with serum from infected rats (refractory hosts), positive plaques being rescreened with serum from infected mice and humans. Based on general reactivity, one clone was selected for further study. As judged by immunofluorescence data, size of corresponding mRNA, and nucleotide sequence analysis, the recombinant expresses approximately 625 amino acids of a schistosome muscle myosin rod. Antibodies evoked by the protein do not cross-react with human cardiac or skeletal muscle, are not invariably stimulated in naturally infected human beings, and rise in titer after chemotherapeutic cure, findings which suggest that the antigen is not a causative agent of Katayama fever, and is probably presented by degenerating worms. The schistosome myosin gene, the most primitive examined to date, appears to be unique inasmuch as it may not be a member of a multigene family and encodes a single mRNA transcript; nonetheless, predicted higher order structure of its translation product is consistent with expected function.
KW - Immunogen
KW - Muscle
KW - Myosin
KW - Schistosoma mansoni
UR - http://www.scopus.com/inward/record.url?scp=0023446109&partnerID=8YFLogxK
U2 - 10.1016/0166-6851(87)90127-7
DO - 10.1016/0166-6851(87)90127-7
M3 - Article
C2 - 3431565
AN - SCOPUS:0023446109
SN - 0166-6851
VL - 26
SP - 29
EP - 38
JO - Molecular and Biochemical Parasitology
JF - Molecular and Biochemical Parasitology
IS - 1-2
ER -