Receptor for Fc on the surfaces of schistosomes

Loukas, Alex, Jones, Malcolm K., King, Lynette T., Brindley, Paul J. and McManus, Donald P. (2001) Receptor for Fc on the surfaces of schistosomes. Infection And Immunity, 69 6: 3646-3651. doi:10.1128/IAI.69.6.3646-3651.2001

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Author Loukas, Alex
Jones, Malcolm K.
King, Lynette T.
Brindley, Paul J.
McManus, Donald P.
Title Receptor for Fc on the surfaces of schistosomes
Journal name Infection And Immunity
ISSN 1098-5522
1070-6313
Publication date 2001-05
Sub-type Article (original research)
DOI 10.1128/IAI.69.6.3646-3651.2001
Open Access Status File (Publisher version)
Volume 69
Issue 6
Start page 3646
End page 3651
Total pages 6
Place of publication Washington, DC, United States
Publisher American Society of Microbiology
Collection year 2001
Language eng
Abstract Schistosoma mansoni masks its surface with adsorbed host proteins including erythrocyte antigens, immunoglobulins, major histocompatibility complex class I, and beta (2)-microglobulin (beta (2)m), presumably as a means of avoiding host immune responses, How this is accomplished has not been explained. To identify surface receptors for host proteins, we biotinylated the tegument of live S, mansoni adults and mechanically transformed schistosomula and then removed the parasite surface with detergent, Incubation of biotinylated schistosome surface extracts witt l human immunoglobulin G (IgG) Fc-Sepharose resulted in purification of a 97-kDa protein that was subsequently identified as paramyosin (Pmy), using antiserum specific for recombinant Pmy, Fc also bound recombinant S. mansoni Pmy and native S. japonicum Pmy, Antiserum to Pmy decreased the binding of Pmy to Fc-Sepharose, and no proteins bound after removal of Pmy from extracts. Fluoresceinated human Fe bound to the surface, vestigial penetration glands, and nascent oral cavity of mechanically transformed schistosomula, and rabbit anti-Pmy Fab fragments ablated the binding of Fc to the schistosome surface, Pmy coprecipitated with host IgG from parasite surface extracts, indicating that complexes formed on the parasite surface as well as in vitro. Binding of Pmy to Fe was not inhibited by soluble protein A, suggesting that Pmy does not bind to the region between the CH2 and CH3 domains used by many other Fc-binding proteins. beta (2)m did not bind to the schistosome Fc receptor (Pmy), a finding that contradicts reports from earlier workers but did bind to a heteromultimer of labeled schistosomula surface proteins, This is the first report of the molecular identity of a schistosome Fc receptor; moreover it demonstrates an additional aspect of the unusual and multifunctional properties of Pmy from schistosomes and other parasitic flatworms.
Keyword Immunology
Infectious Diseases
Monoclonal Ige Antibody
Taenia-solium
Antigen-b
Japonicum Paramyosin
Nucleotide-sequence
Vaccine Candidate
Mansoni
Protein
Purification
Acquisition
Q-Index Code C1

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Medicine Publications
 
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Created: Tue, 14 Aug 2007, 14:54:18 EST