D-Mannose-Specific Immunoglobulin M in Grass Puffer (Takifugu niphobles), a Nonhost Fish of a Monogenean Ectoparasite Heterobothrium okamotoi, Can Act as a Trigger for Its Parasitism
Autor: | Hiroaki Suetake, Sachi Hirakawa, Tetsuo Goto, Toshiaki Miyadai, Shintaro Matsui, Satoshi Tasumi, Shigeyuki Tsutsui, Yura Tsubouchi, Osamu Nakamura |
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Rok vydání: | 2020 |
Předmět: |
Gills
DNA Complementary Takifugu rubripes Blotting Western Gene Expression Parasitism Zoology Ectoparasitic Infestations Trematode Infections Takifugu Host Specificity Pagrus major Fish Diseases Animals Parasite hosting Amino Acid Sequence Cilia Cloning Molecular Ecology Evolution Behavior and Systematics Mucous Membrane biology Host (biology) Hydrogen-Ion Concentration biology.organism_classification Mucus Immunoglobulin M Platyhelminths Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization biology.protein Electrophoresis Polyacrylamide Gel Parasitology Mannose |
Zdroj: | Journal of Parasitology. 106:276 |
ISSN: | 0022-3395 |
DOI: | 10.1645/19-21 |
Popis: | Heterobothrium okamotoi, a monogenean gill parasite, exhibits high host specificity for the tiger puffer, Takifugu rubripes, and it has been experimentally verified that the parasite cannot colonize either closely related species such as the grass puffer Takifugu niphobles or distantly related fish such as the red seabream Pagrus major. Previously, we demonstrated in T. rubripes that immunoglobulin M (IgM) with d-mannose affinity induced deciliation of the oncomiracidia, the first step of parasitism, indicating that the parasite utilizes the molecule as a receptor for infection. In the present study, we purified mannose-specific IgM from 2 nonhost species, T. niphobles and P. major, by affinity and gel-filtration chromatography techniques and compared their deciliation-inducing activity against H. okamotoi oncomiracidia. The IgM of the former showed activity, whereas the latter had no effect, suggesting that in addition to d-mannose-binding ability, the crystallizable fragment domain of IgM, which is not part of the antigen-binding domain, plays an important role in host recognition by the oncomiracidia, such as direct binding to the parasites. It also suggests that the host specificity of H. okamotoi is relatively low upon initial recognition, and the specificity is established by exclusion in nonhosts during a later stage. |
Databáze: | OpenAIRE |
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