Sculpture alcove, Kangaroo Point House, Kangaroo Point, Brisbane

Alcove to deck, as seen from garden.

Sculpture alcove, Kangaroo Point House, Kangaroo Point, Brisbane

Alcove to deck, with timber handrail in foreground.

Sculpture alcove, Kangaroo Point House, Kangaroo Point, Brisbane

Alcove to deck, as seen from garden.

Aboriginal Art Collection: Highlights from Australia's Public Museums and Galleries

Contents: Introduction SUSAN COCHRANE National Gallery of Australia, Canberra WALLY CARUANA National Museum of Australia, Canberra DAVID KAUS Museum and Art Gallery of the Northern Territory, Darwin MARGIE WEST Art Gallery of New South Wales, Sydney HETTI PERKINS AND KEN WATSON Museum of Contemporary Art, Sydney BERNICE MURPHY Queensland Art Gallery, Brisbane MARCO NEALE Queensland Museum, Brisbane RICHARD ROBINS National Gallery of Victoria, Melbourne JUDITH RYAN Museum Victoria, Melbourne GAYE SCULTHORPE Tasmanian Museum and Art Gallery, Hobart KIM AKERMAN AND DAVID HANSEN Art Gallery of Western Australia, Perth MICHAEL O'FERRALL AND BRENDA L. CROFT Western Australian Museum, Perth ROSS CHADWICK AND MANCE LOFGREN Art Gallery of South Australia, Adelaide JANE HYLTON South Australian Museum, Adelaide PHILIP A. CLARKE List of Plates Bibliography Editor's Acknowledgments Contributors Index

Receptor for Fc on the surfaces of schistosomes

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.