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Immunolabelling of fish host molecules on the tegumental surface of Ligula intestinalis (Cestoda: Pseudophyllidea)
1Department of Biological Sciences, Keele University, Staffordshire, UK.
Insights
A carp IgM antibody cross-reacts with roach serum proteins, identifying potential fish host molecules on the tapeworm Ligula intestinalis tegument. This cross-reactivity aids in localizing these molecules on the parasite
Area of Science:
- Immunology
- Parasitology
- Biochemistry
Background:
- The study investigates the interaction between fish hosts and parasitic organisms at a molecular level.
- Understanding host-parasite molecular interactions is crucial for developing effective treatments and control strategies.
Purpose of the Study:
- To demonstrate cross-reactivity between a carp IgM antibody and roach serum components.
- To utilize this cross-reactivity to identify and localize fish host molecules on the tapeworm Ligula intestinalis.
Main Methods:
- Immunoblotting, SDS-PAGE, and western blotting were employed to analyze serum components.
- Immunofluorescence and immunogold labeling were used to visualize host molecules on the parasite's tegument.
Main Results:
- A polyclonal anti-carp IgM antibody cross-reacted with two major bands (90 kDa and 65 kDa) in roach serum.
- The 65 kDa band was identified as a fish immunoglobulin heavy chain; the 90 kDa band's identity is uncertain.
- Fish host molecules were localized on the microthrix spines of Ligula intestinalis tegument.
Conclusions:
- The cross-reactivity of carp IgM antibody with roach serum provides a tool for studying host-parasite molecular interactions.
- Fish host molecules are present on the tegument of Ligula intestinalis, particularly associated with microthrix spines.
Abstract:
Immunoblotting, SDS-PAGE and western blotting procedures were used to demonstrate cross-reactivity of a polyclonal anti-carp IgM antibody with components of roach serum. The polyclonal antibody labelled 2 major bands in both immune and normal roach sera corresponding to molecular masses of approximately 90 and 65 kDa. One of these bands (65 kDa) was considered to be heavy chain of fish immunoglobulin whilst the identity of the other remains uncertain. This cross-reaction has been exploited in immunofluorescence and immunogold labelling studies to localize fish host molecules on the tegumental membrane of Ligula intestinalis freshly removed from roach fry. Immunogold studies revealed a low level of host molecules to be associated mainly with the microthrix spines of the tegument with less gold labelling being observed on the microthrix shafts.