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

journal contribution
posted on 2023-05-16, 14:01 authored by Cook, MT, Hayball, PJ, Birdseye, L, Bagley, C, Barbara NowakBarbara Nowak, Hayball, JD
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 200kDa consisting of non-covalently bound subunits of 26 and 23kDa. 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. © 2003 Elsevier Science Ltd. All rights reserved.

History

Publication title

Developmental and Comparative Immunology

Volume

27

Issue

6-7

Pagination

579-588

ISSN

0145-305X

Department/School

Institute for Marine and Antarctic Studies

Publisher

Pergamon-Elsevier Science Ltd

Place of publication

Oxford, England

Repository Status

  • Restricted

Socio-economic Objectives

Fisheries - aquaculture not elsewhere classified

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