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Assessment of snapper (Pagrus auratus) natural IgM binding to bromelain treated sheep erythrocytes
journal contribution
posted on 2023-05-16, 16:12 authored by Morrison, RN, Alan Lyons, Barbara NowakBarbara Nowak, Hayball, JDNormal snapper (Pagrus auratus Bloch and Schneider) serum was examined for natural IgM that binds to protease (bromelain) treated sheep erythrocytes (BrSRBC) in a model assay system that has been used to appraise natural IgM of various mammals. Normal snapper serum lysed BrSRBC while haemolysis was abrogated by heat inactivation of serum and in divalent cation-deficient conditions, indicative of classical complement mediated lysis. In addition, heat inactivated normal snapper serum agglutinated BrSRBC while phosphatidylcholine (PtC) liposomes partially inhibited both haemolysis and agglutination. Inhibition of haemolysis and agglutination may have been mediated by an interaction between immunoglobulin (Ig) and PtC as protein A purified snapper Ig bound to PtC liposomes. However it is not known if this binding was PtC specific nor if the binding was initiated by either the Fab and/or Fc domains of snapper Ig. BrSRBC plaque forming cells (PFC) were detected in the peritoneal cavity, spleen, head kidney and peripheral blood of normal snapper. The greatest proportion of BrSRBC PFC per B cell was within the peritoneal cavity followed by the spleen, peripheral blood and head kidney. Together, these data suggest that normal snapper serum may contain natural Ig that binds BrSRBC, activating the classical complement cascade. © 2004 Elsevier Ltd. All rights reserved.
History
Publication title
Fish and Shellfish ImmunologyVolume
18Pagination
91-99ISSN
1050-4648Department/School
Institute for Marine and Antarctic StudiesPublisher
Academic Press Ltd Elsevier Science LtdPlace of publication
24-28 Oval Rd, London, England, Nw1 7DxRepository Status
- Restricted