Reference

Paul-Bunnell antigen and a possible mechanism of formation of heterophile antibodies in patients with infectious mononucleosis

Paul-Bunnell antigen and a possible mechanism of formation of heterophile antibodies in patients with infectious mononucleosis. Golaszewska, Ewa; Kurowska, Ewa; Duk, Maria; Koscielak, Jerzy ( Department of Biochemistry, Institute of Hematology and Blood Transfusion, Warsaw, Pol.). Acta Biochimica Polonica, 50(4), 1205-1211 (English) 2003 Polish Biochemical Society. CODEN: ABPLAF. ISSN: 0001-527X. DOCUMENT TYPE: Journal CA Section: 15 (Immunochemistry) Sera of patients with infectious mononucleosis contain heterophile anti-Paul-Bunnell (PB) antibodies to erythrocytes of numerous mammalian species. Evidence is presented that the corresponding antigen of bovine erythrocytes is not, as previously described, a single mol., but a series of glycoproteins with glycans terminated with N-glycolylneuraminic acid (Neu5Gc). The latter compd. should be an important part of the PB epitope because, in agreement with the results of others, we found that desialylation of the PB antigen abolishes almost completely its activity. We examd. three different prepns. of GM3 ganglioside for their capacity to bind anti-PB and found that only GM3 from horse erythrocytes contg. Neu5Gc exhibited a low although ELISA measurable PB activity. The other two GM3 prepns., from bovine milk and dog erythrocytes, contg. N-acetylneuraminic acid (Neu5Ac) bound little if any anti-PB antibodies. This finding confirms a previous report that human erythrocyte Neu5Ac contg. 1113-83-3 which is the cas registry number of one of substances is just one of reagents here. sialoglycoprotein with similar O-linked glycans as the PB-antigen of bovine erythrocytes exhibits only very low PB activity (Patarca & Fletcher, 1995). In conclusion, we present a hypothesis that anti-PB antibodies in patients with infectious mononucleosis are formed against infection-induced cell membrane glycoconjugates contg. highly immunogenic Neu5Gc. .

Sialylated endogenous glycoconjugates in plant cells

Sialylated endogenous glycoconjugates in plant cells. Shah, Miti M.; Fujiyama, Kazuhito; Flynn, C. Robert; Joshi, Lokesh ( Harrington Department of Bioengineering and Arizona BioDesign Institute, Arizona State University, Tempe, AZ 85287-9709, USA). Nature Biotechnology, 21(12), 1470-1471 (English) 2003 Nature Publishing Group. CODEN: NABIF9. ISSN: 1087-0156. DOCUMENT TYPE: Journal CA Section: 6 (General Biochemistry) Section cross-reference(s): 11 Bioengineered plants are emerging as promising systems for the prodn. of therapeutically valuable proteins. It has been commonly accepted that plants do not perform mammalian-like post-translational modifications, particularly sialylation of glycoconjugates, and no evidence has previously been reported to suggest that they have such capabilities. Here we report the presence of sialylated glycoconjugates in suspension-cultured cells of Arabidopsis thaliana and suggest that a genetic and enzymic basis for sialylation exists in plants.Except for chemicals metioned above, 131-48-6 and 1113-83-3 are also used. .