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Choleragen (Cholera Toxin): A Bacterial Lectin

Choleragen (cholera toxin) agglutinated erythrocytes and liposomes containing the toxin receptor, galactosyl-N-acetylgalactosaminyl-(N-acetylneuraminyl)-galactos ylceramide (ganglioside GM1). Cells that had been exposed to GM1 were agglutinated, but agglutination was not observed when cells had been... Full description

Journal Title: Proceedings of the National Academy of Sciences of the United States of America 1 April 1979, Vol.76(4), pp.1673-1676
Main Author: Richards, Roberta L.
Other Authors: Moss, Joel , Alving, Carl R. , Fishman, Peter H. , Brady, Roscoe O.
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 00278424
Link: https://www.jstor.org/stable/69574
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recordid: jstor_archive_2369574
title: Choleragen (Cholera Toxin): A Bacterial Lectin
format: Article
creator:
  • Richards, Roberta L.
  • Moss, Joel
  • Alving, Carl R.
  • Fishman, Peter H.
  • Brady, Roscoe O.
subjects:
  • Applied sciences -- Materials science -- Materials
  • Health sciences -- Medical sciences -- Immunology
  • Biological sciences -- Biology -- Physiology
  • Biological sciences -- Biochemistry -- Biomolecules
  • Physical sciences -- Chemistry -- Chemical compounds
  • Physical sciences -- Chemistry -- Chemical compounds
  • Biological sciences -- Biochemistry -- Chemical compounds
  • Physical sciences -- Chemistry -- Biomolecules
  • Biological sciences -- Biochemistry -- Biomolecules
  • Biological sciences -- Biochemistry -- Biomolecules
ispartof: Proceedings of the National Academy of Sciences of the United States of America, 1 April 1979, Vol.76(4), pp.1673-1676
description: Choleragen (cholera toxin) agglutinated erythrocytes and liposomes containing the toxin receptor, galactosyl-N-acetylgalactosaminyl-(N-acetylneuraminyl)-galactos ylceramide (ganglioside GM1). Cells that had been exposed to GM1 were agglutinated, but agglutination was not observed when cells had been exposed to other gangliosides (GM2, GM3, GD1a, GD1b). Choleragen-dependent agglutination of liposomes was slightly less specific, because liposomes containing either GM1 or GD1b, but neither GM2, GD1a, nor GM3 were agglutinated. The oligosaccharide isolated from GM1 inhibited both the agglutination of cells and liposomes containing GM1 and the binding of choleragen to liposomes containing GM1. Galactose and sialic acid were less effective inhibitors of liposomal agglutination and did not inhibit cellular agglutination or binding of choleragen to liposomes. Liposomal agglutination was dependent on choleragen concentration and occurred with the B but not the A protomer of choleragen. These results suggest that choleragen, through its binding to the oligosaccharide portion of a glycolipid, exhibits lectinlike activity, which results in agglutination of liposomes and erythrocytes.
language: eng
source:
identifier: ISSN: 00278424
fulltext: fulltext
issn:
  • 0027-8424
  • 00278424
url: Link


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titleCholeragen (Cholera Toxin): A Bacterial Lectin
creatorRichards, Roberta L. ; Moss, Joel ; Alving, Carl R. ; Fishman, Peter H. ; Brady, Roscoe O.
ispartofProceedings of the National Academy of Sciences of the United States of America, 1 April 1979, Vol.76(4), pp.1673-1676
identifierISSN: 00278424
subjectApplied sciences -- Materials science -- Materials ; Health sciences -- Medical sciences -- Immunology ; Biological sciences -- Biology -- Physiology ; Biological sciences -- Biochemistry -- Biomolecules ; Physical sciences -- Chemistry -- Chemical compounds ; Physical sciences -- Chemistry -- Chemical compounds ; Biological sciences -- Biochemistry -- Chemical compounds ; Physical sciences -- Chemistry -- Biomolecules ; Biological sciences -- Biochemistry -- Biomolecules ; Biological sciences -- Biochemistry -- Biomolecules
descriptionCholeragen (cholera toxin) agglutinated erythrocytes and liposomes containing the toxin receptor, galactosyl-N-acetylgalactosaminyl-(N-acetylneuraminyl)-galactos ylceramide (ganglioside GM1). Cells that had been exposed to GM1 were agglutinated, but agglutination was not observed when cells had been exposed to other gangliosides (GM2, GM3, GD1a, GD1b). Choleragen-dependent agglutination of liposomes was slightly less specific, because liposomes containing either GM1 or GD1b, but neither GM2, GD1a, nor GM3 were agglutinated. The oligosaccharide isolated from GM1 inhibited both the agglutination of cells and liposomes containing GM1 and the binding of choleragen to liposomes containing GM1. Galactose and sialic acid were less effective inhibitors of liposomal agglutination and did not inhibit cellular agglutination or binding of choleragen to liposomes. Liposomal agglutination was dependent on choleragen concentration and occurred with the B but not the A protomer of choleragen. These results suggest that choleragen, through its binding to the oligosaccharide portion of a glycolipid, exhibits lectinlike activity, which results in agglutination of liposomes and erythrocytes.
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abstractCholeragen (cholera toxin) agglutinated erythrocytes and liposomes containing the toxin receptor, galactosyl-N-acetylgalactosaminyl-(N-acetylneuraminyl)-galactos ylceramide (ganglioside GM1). Cells that had been exposed to GM1 were agglutinated, but agglutination was not observed when cells had been exposed to other gangliosides (GM2, GM3, GD1a, GD1b). Choleragen-dependent agglutination of liposomes was slightly less specific, because liposomes containing either GM1 or GD1b, but neither GM2, GD1a, nor GM3 were agglutinated. The oligosaccharide isolated from GM1 inhibited both the agglutination of cells and liposomes containing GM1 and the binding of choleragen to liposomes containing GM1. Galactose and sialic acid were less effective inhibitors of liposomal agglutination and did not inhibit cellular agglutination or binding of choleragen to liposomes. Liposomal agglutination was dependent on choleragen concentration and occurred with the B but not the A protomer of choleragen. These results suggest that choleragen, through its binding to the oligosaccharide portion of a glycolipid, exhibits lectinlike activity, which results in agglutination of liposomes and erythrocytes.
pubNational Academy of Sciences of the United States of America
doi10.1073/pnas.76.4.1673
eissn10916490
date1979-04-01