Hostname: page-component-76fb5796d-45l2p Total loading time: 0 Render date: 2024-04-26T00:58:57.491Z Has data issue: false hasContentIssue false

Identification, isolation and characterization of a Fyn-like tyrosine kinase from Schistosoma mansoni

Published online by Cambridge University Press:  07 May 2002

K. KAPP
Affiliation:
Institute for Genetics, Genetic Parasitology and Center for Biological and Medical Research, 40225 Düsseldorf, Germany
P. SCHÜSSLER
Affiliation:
Institute for Genetics, Genetic Parasitology and Center for Biological and Medical Research, 40225 Düsseldorf, Germany
W. KUNZ
Affiliation:
Institute for Genetics, Genetic Parasitology and Center for Biological and Medical Research, 40225 Düsseldorf, Germany
C.G. GREVELDING
Affiliation:
Institute for Genetics, Genetic Parasitology and Center for Biological and Medical Research, 40225 Düsseldorf, Germany

Abstract

Growth and development of adult schistosomes requires permanent communication processes of the parasites with their specific host environment and, additionally, between the two genders. Accumulating evidence suggests that, at the molecular level, the mandatory interactions are mediated by signal transduction processes. During recent years, a considerable interest has emerged in the identification of signalling molecules from this parasite and to elucidate their roles during development. In this organism, a number of different molecules have been identified which belong to diverse classes of evolutionary conserved signal transduction cascades. However, up to now no representative of the conserved family of cellular tyrosine kinases has been identified. In this study we present a suitable approach to identify this class of molecules and demonstrate the successful cloning and molecular characterization of one of the isolated genes, the tyrosine kinase 5 (TK5). An unexpected finding was that in the Liberian strain of Schistosoma mansoni the TK5 gene exhibits an allelic polymorphism.

Type
Research article
Copyright
2001 Cambridge University Press

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)