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  • Structure of Sm25, an antigenic integral membrane glycoprotein of adult Schistosoma mansoni☆
  • Add time:08/28/2019         Source:sciencedirect.com

    Sm25 is the principal antigen recognised by antibodies from mice protectively vaccinated with isolated tegumental membranes of adult Schistosoma mansoni. The full-length amino acid sequence of this protein has been deduced from the sequence of two cDNAs, one isolated by screening a cDNA library and the other, including the 5′ end of the gene, amplified directly from adult worm RNA using the polymerase chain reaction. The predicted sequence represents a nascent polypeptide of MΓ 21 500. Following cleavage of a predicted signal sequence, the MΓ of the resulting polypeptide is 17 600. The polypeptide contains 2 potential sites for N-linked glycosylation and a hydrophobic domain at the C-terminus that could facilitate membrane association. Analysis of the mature gene product confirmed that Sm25 is an N-glycosylated integral membrane protein and that the MΓ of the deglycosylated polypeptide is between 15 000 and 20 000.

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