Muscular myosin isoforms of Taenia solium (Cestoda)

Authors

  • Laura Gonzalez-Malerva,

    1. Departamento de Microbiologia y Parasitologia, Facultad de Medicina, Universidad Nacional Autonoma de Mexico, Circuito Interior, Ciudad Universitaria, Mexico DF 04510, Mexico
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  • Mayra Cruz-Rivera,

    1. Departamento de Microbiologia y Parasitologia, Facultad de Medicina, Universidad Nacional Autonoma de Mexico, Circuito Interior, Ciudad Universitaria, Mexico DF 04510, Mexico
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  • Olivia Reynoso-Ducoing,

    1. Departamento de Microbiologia y Parasitologia, Facultad de Medicina, Universidad Nacional Autonoma de Mexico, Circuito Interior, Ciudad Universitaria, Mexico DF 04510, Mexico
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  • Claudio Retamal,

    1. Centro de Biociencia e Biotecnologia, Universidade Estadual do Norte Fluminense, Campos dos Goytacazes, Rio de Janeiro 28015400, Brasil
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  • Ana Flisser,

    1. Departamento de Microbiologia y Parasitologia, Facultad de Medicina, Universidad Nacional Autonoma de Mexico, Circuito Interior, Ciudad Universitaria, Mexico DF 04510, Mexico
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  • Javier R. Ambrosio

    Corresponding author
    1. Departamento de Microbiologia y Parasitologia, Facultad de Medicina, Universidad Nacional Autonoma de Mexico, Circuito Interior, Ciudad Universitaria, Mexico DF 04510, Mexico
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Corresponding author. Tel.: +5255 5623 2467; fax: +5255 5623 2382. jrah@servidor.unam.mx

Abstract

Type II myosin, the primary component of the thick filament of muscle fibers, is organized as a dimeric high molecular weight protein, and is composed of a pair of heavy chains (MHC) and two pairs of light chains. Myosin II transforms ATP energy into mechanical force. All type II myosins are conserved proteins but they have two variable regions that are located in different places of the molecule. Myosin molecules are encoded by a multigene family and many isoforms are generated. The expression of myosins depends on the developmental stage and on the type and degree of contractile activity and tissue, therefore several myosin isoforms are found in the same organism. Here we describe the use of different techniques that allowed demonstrating the presence of isoforms of the heavy chain type II myosin of Taenia solium cysticerci (larvae) and tapeworms (adults), a cestode parasite of importance in public health in many developing countries. Myosin was purified and used in comparative proteolytic fragmentation, ATPase activity, detection of antigenic differences and electrophoretic separation. The results obtained showed biochemical and immunochemical differences among cysticerci and tapeworms, and demonstrate the presence of myosin isoforms in T. solium that are probably associated to physiological requirements of each developmental stage.

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