Diatoms are unicellular microalgae encased in a siliceous cell wall, or frustule. Pennate diatoms, which possess bilateral symmetry, attach to the substratum at a slit in the frustule called the raphe. These diatoms not only adhere, but glide across surfaces whilst maintaining their attachment, secreting a sticky mucilage that forms a trail behind the gliding cells. We have raised monoclonal antibodies to the major cell surface proteoglycans of the marine raphid diatom Stauroneis decipiens Hustedt. The antibody StF.H4 binds to the cell surface, in the raphe and to adhesive trails and inhibits the ability of living diatoms to adhere to the substratum and to glide. Moreover, StF.H4 binds to a periodate-insensitive epitope on four frustule-associated proteoglycans (relative molecular masses 87, 112, and > 200 kDa). Another monoclonal antibody, StF.D5, binds to a carbohydrate epitope on the same set of proteoglycans, although the antibody binds only to the outer surface of the frustule and does not inhibit cell motility and adhesion.
A basic, hydroxyproline-rich glycoprotein (molecular mass 120 kDa) has been purified from the styles of Nicotiana alata. An antibody, specific for the protein backbone (molecular mass 78 kDa) of the glycoprotein, was used to demonstrate that the glycoprotein is a soluble, style-specific component and that related molecules are present in the styles of other solanaceous species. Linkage analysis of the carbohydrate portion of the glycoprotein, together with antibody binding studies, indicates that the glycoprotein contains both extensin-like and arabinogalactan-protein (AGP)-like side chains. Furthermore, the AGP-like side-chains contain a style-specific epitope that is also present on AGPs from N. alata styles and glycoconjugates from the styles of other members of the Solanaceae. The abundance of this 120 kDa glycoprotein, its location in the extracellular matrix of the transmitting tract and its conservation in several species within the Solanaceae suggests a role in pistil function.
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