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2003 | 50 | 4 |

Tytuł artykułu

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

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
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 molecule, but a series of glycoproteins with glycans termi­nated with .-glycolylneuraminic acid (Neu5Gc). The latter compound 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 examined three different preparations of GM3 ganglioside for their capacity to bind anti-PB and found that only GM3 from horse erythrocytes containing Neu5Gc exhibited a low although ELISA measurable PB activity. The other two GM3 prepa­rations, from bovine milk and dog erythrocytes, containing .-acetylneuraminic acid (Neu5Ac) bound little if any anti-PB antibodies. This finding confirms a previous re­port that human erythrocyte Neu5Ac containing sialoglycoprotein with similar O-linked glycans as the PB-antigen of bovine erythrocytes exhibits only very low PB activity (Patarca & Fletcher, 1995, Crit Rev Oncogen., 6: 305). In conclusion, we present a hypothesis that anti-PB antibodies in patients with infectious mononucleosis are formed against infection-induced cell membrane glycoconjugates containing highly immunogenic Neu5Gc.

Wydawca

-

Rocznik

Tom

50

Numer

4

Opis fizyczny

p.1205-1211,fig.,ref.

Twórcy

  • Institute of Hematology and Blood Transfusion, Chocimska 5, 00-957 Warsaw, Poland
autor
autor
autor

Bibliografia

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  • Chou HH, Hayakawa T, Diaz S, Krings M, Indriaty E, Leakey M, Paabo S, Satta Y, Takahata N, Varki A. (2002) Inactivation of CMP-N-acetylneuraminic acid hydroxylase occurred prior to brain expansion during human evolution. Proc Natl Acad Sci US A.; 99: 11736-41.
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  • Fletcher MA, Caldwell KE, Latif Z. (1982) Immunochemical studies of infectious mononucleosis. IX. Heterophile antigen asociated with a glycoprotein from the bovine erythrocyte membrane. Vox Sang.; 43: 57-70.
  • Hanganutziu M. (1924) Hemagglutinines Heterogenetiques apres injectior de serum de cheval. CRSocBiol (Paris).; 91: 1457.
  • Higashi H, Naiki M, Matuo S, Okouchi K. (1977) Antigen of "serum sickness" type of heterophile antibodies in human sera: identification as gangliosides with N-glycolylneuraminic acid. Biochem Biophys Res Commun.; 79: 388-95.
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  • Merrick JM, Zadarlik K, Milgrom F. (1978) Characterization of the Hanganutziu-Deicher (serum-sickness) antigen as gangliosides containing N-glycolyl-neuraminic acid. Int Arch Allergy Appl Immunol.; 57: 477-80.
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  • Muchmore EA, Milewski M, Varki A, Diaz S. (1989) Biosynthesis of N-glycolylneuraminic acid. The primary site of hydroxylation of N-acetylneuraminic acid is the cytosolic sugar nucleotide pool. J Biol Chem.; 264: 20216-23.
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  • Patarca R, Fletcher MA. (1995) Structure and pathophysiology of the erythrocyte membrane-associated Paul-Bunnell heterophile antibody determinant in Epstein-Barr virus-associated disease. Crit Rev Oncog.; 6: 305-26.
  • Shaw L, Schauer R. (1988) The biosynthesis of N-glycolylneuraminic acid occurs by hydroxylation of the CMP-glycoside of N-acetylneuraminic acid. Biol Chem Hoppe Seyler.; 369: 477-86.
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Bibliografia

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