Isolation and partial characterization of a pentraxin-like protein with complement-fixing activity from snapper (Pagrus auratus, Sparidae) serum

Pentraxin-like molecules have been isolated from a number of fish species. However, little is known about the function of these proteins in the teleosts. In this study we report the isolation and characterization of a pentraxin-like molecule from the serum of snapper (Pagrus auratus) that has the ab...

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Bibliographic Details
Published in:Developmental & Comparative Immunology
Main Authors: Cook, M., Hayball, P., Birdseye, L., Bagley, C., Nowak, B., Hayball, J.
Format: Article in Journal/Newspaper
Language:English
Published: Pergamon-Elsevier Science Ltd 2003
Subjects:
Animals
Fishes
C-Reactive Protein
Serum Amyloid P-Component
Up-Regulation
Amino Acid Sequence
Multigene Family
Molecular Sequence Data
Complement System Proteins
Laurie
Mathew
Nowak
Atlantic salmon
Online Access:http://hdl.handle.net/2440/9397
https://doi.org/10.1016/S0145-305X(03)00034-X
Description
Summary:Pentraxin-like molecules have been isolated from a number of fish species. However, little is known about the function of these proteins in the teleosts. In this study we report the isolation and characterization of a pentraxin-like molecule from the serum of snapper (Pagrus auratus) that has the ability to activate complement. This pentraxin-like protein was isolated from serum by calcium-dependent binding to agarose. SDS-PAGE analysis demonstrated an oligomeric protein of approximately 200k Da consisting of non-covalently bound subunits of 26 and 23 kDa. Protein sequencing revealed significant (50%) sequence identity with pentraxins from both Atlantic salmon (S. salar) and rainbow trout (O. mykiss). However, polyclonal antibodies raised against snapper pentraxin did not recognise salmon or trout pentraxin in Western blot analysis. Following LPS injection, snapper pentraxin levels increased 2-fold before gradually returning to basal levels. Most significantly, the isolated pentraxin initiated complement-mediated lysis of ligand-coated sheep erythrocytes in a dose-dependent fashion. In view of the similarity between the known fish pentraxins, and their similarity to mammalian serum amyloid P-components we conclude that the isolated protein may be a snapper pentraxin homologue. Cook, Mathew T; Hayball, Peter J; Birdseye, Laurie; Bagley, Christopher; Nowak, Barbara F; Hayball, John D

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