Naslov
Purification and partial characterization of a lectin protein complex, the clathrilectin, from the calcareous sponge Clathrina clathrus

Autori
Gardères, Johan ; Domart-Coulon, Isabelle ; Marie, Arul ; Hamer, Bojan ; Batel, Renato ; Müller, Werner E.G. ; Bourguet-Kondracki, Marie-Lise

Izvornik
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology (1096-4959) 200 (2016); 17-27

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
Porifera ; Clathrina clathrus ; lectin ; N-acetyl-glucosamine ; cell aggregation ; proteomics

Sažetak
Carbohydrate-binding proteins were purified from the marine calcareous sponge Clathrina clathrus via affinity chromatography on lactose and N-acetyl glucosamine- agarose resins. Proteomic analysis of acrylamide gel separated protein subunits obtained in reducing conditions pointed out several candidates for lectins. Based on amino- acid sequence similarity, two peptides displayed homology with the jack bean lectin Concanavalin A, 
 including a conserved domain shared by proteins in the L-type lectin superfamily. An N-acetyl glucosamine - binding protein complex, named clathrilectin, was further purified via gel filtration chromatography, bioguided with a diagnostic rabbit erythrocyte haemagglutination assay, and its activity was found to be calcium dependent. Clathrilectin, a protein complex of 3, 200 kDa estimated by gel filtration, is composed of monomers with apparent molecular masses of 208 and 180 kDa estimated on 10% SDS- PAGE. Nine internal peptides were identified using proteomic analyses, and compared to protein libraries from the demosponge Amphimedon queenslandica and a calcareous sponge Sycon sp. from the Adriatic Sea. The clathrilectin is the first lectin isolated from a calcareous sponge and displays homologies with predicted sponge proteins potentially involved in cell aggregation and interaction with bacteria.

Izvorni jezik
Engleski

Znanstvena područja
Geologija

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