01501nas a2200193   4500008004100000020001400041245015100055210006900206260000800275300001200283490000800295520087100303100001701174700002101191700001701212700001601229700001601245856004601261       1994                        eng d  a0301-556400aTISSUE TREATMENT FOR WHOLE-MOUNT INTERNAL LECTIN STAINING IN THE NEMATODES CAENORHABDITIS-ELEGANS, PANAGROLAIMUS-SUPERBUS AND ACROBELOIDES-MAXIMUS0 aTISSUE TREATMENT FOR WHOLEMOUNT INTERNAL LECTIN STAINING IN THE   cJun  a379-3840 v1013 aFour different fixation schemes, using ten fluorescent-labelled lectins, were investigated for whole mount internal staining of three rhabditid nematodes: Caenorhabditis elegans, Panagrolaimus superbus and Acrobeloides maximus. Acetone-only fixation was found to give strong and reproducible staining, which could be prevented either by periodate treatment of the organisms or by specific inhibitory sugars of the lectins under investigation. Whereas the use of either phosphate or TRIS buffers had no effect on the staining pattern or the fluorescence intensity, the incubation time as well as the in cubation temperature affected the staining reaction. The best results were obtained upon overnight incubation at 4 degrees C: the lectin staining could be inhibited in all cases, except for the intestinal brush border of C. elegans by the lectin of Lens culinaris.1 aBorgonie, G.1 aVanDriessche, E.1 aLink, C., D.1 aDeWaele, D.1 aCoomans, A.  uhttps://nematodes.myspecies.info/node/29201393nas a2200193   4500008004100000020001400041245012600055210006900181300001200250490000700262520078200269100001701051700002101068700001701089700001501106700001601121700001601137856004601153       1997                        eng d  a1164-557100aInternal lectin binding patterns in the nematodes Caenorhabditis elegans, Panagrolaimus superbus and Acrobeloides maximus0 aInternal lectin binding patterns in the nematodes Caenorhabditis  a173-1860 v203 aUsing ten different lectins, the binding patterns were studied in three free-living rhabditid nematodes : Caenorhabditis elegans, Panagrolaimus superbus, and Acrobeloides maximus. Although all the nematode tissues showed binding by one or more of the lectins used, considerable differences were noticed between the three nematode species. Yolk, four of the coelomocytes, and the oocytes bind most often with the lectins used. Although the intestinal brush border interacts with a lot of foreign materials, it stained only with few lectins. The lectin binding pattern of the yolk indicated that, at the time of incorporation of the yolk in embryos or shortly thereafter, a processing of the yolk occurs resulting in changes in lectin-binding characteristics of the yolk protein.1 aBorgonie, G.1 aVanDriessche, E.1 aLink, C., D.1 aClaeys, M.1 aDeWaele, D.1 aCoomans, A.  uhttps://nematodes.myspecies.info/node/24501654nas a2200169   4500008004100000020001400041245009100055210006900146300001200215490000600227520114000233100001701373700001701390700001501407700001601422856004601438       2003                        eng d  a1388-554500aLysosomal and pseudocoelom routing protects Caenorhabditis elegans from ricin toxicity0 aLysosomal and pseudocoelom routing protects Caenorhabditis elega  a339-3500 v53 aThe resistance of the nematode Caenorhabditis elegans towards the highly potent toxin ricin has been studied. Incubation of C. elegans in ricin did not affect life span or progeny production. However, micro-injection of the ricin A-chain into the distal, syncitial gonad caused degeneration and sterility in test specimens, confirming that C. elegans ribosomes are sensitive. Using transmission electron microscopy, it was observed that ricin is effectively internalised into the intestinal cells. When pre-labelled with bold. the toxin reached only the lysosomes. When native toxin was used, the toxin was either routed to the lysosomes or underwent transcytosis to the pseudocoelomatic cavity and incorporation into embryos. None of the ricin reached either the trans Golgi network or the Golgi apparatus. considered essential for toxicity. The observed oral non-toxicity is therefore due to alternate sorting of the toxin. a mechanism not previously observed. The data indicate that, although ricin can opportunistically bind to, and be internalised by, cell surface receptors. these receptors are not sufficient to elicit toxicity.1 aBorgonie, G.1 aLink, C., D.1 aClaeys, M.1 aCoomans, A.  uhttps://nematodes.myspecies.info/node/186