Eggshell precursor proteins of Fasciola hepatica, I. Structure and expression of vitelline protein B

Antibody raised against the major eggshell protein of Fasciola hepatica (vitelline protein B, vpB) is employed to isolate cDNAs from an expression library and to localize the protein in whole worms. Two cDNAs corresponding to the protein are homologous through the N-terminal and C-terminal coding re...

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Veröffentlicht in:Molecular and biochemical parasitology 1992-09, Vol.54 (2), p.129-141
Hauptverfasser: Rice-Ficht, Allison C., Dusek, Kathryn A., John Kochevar, G., Herbert Waite, J.
Format: Artikel
Sprache:eng
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Zusammenfassung:Antibody raised against the major eggshell protein of Fasciola hepatica (vitelline protein B, vpB) is employed to isolate cDNAs from an expression library and to localize the protein in whole worms. Two cDNAs corresponding to the protein are homologous through the N-terminal and C-terminal coding regions and widely divergent internally. No repeated regions are apparent and no significant sequence homology is seen with chorion proteins of other genera although the amino acid composition closely reflects that of other chorion proteins. Microheterogeneity observed in the vpB is due to the presence of multiple coding sequences, transcripts and a gradient of post-translational modification. Relative transcription of the vpB mRNA throughout the female reproductive tract is demonstrated.
ISSN:0166-6851
1872-9428
DOI:10.1016/0166-6851(92)90106-T