Endocytosis from coated pits of Shiga toxin: a glycolipid-binding protein from Shigella dysenteriae 1.

Sandvig, Kirsten; Olsnes, Sjur; Brown, J E; Petersen, Ole W.; Deurs, Bo van

doi:10.1083/jcb.108.4.1331

Cited by 245 publications

(168 citation statements)

References 48 publications

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“…Using Shiga toxin coupled to horse radish peroxidase, it has been shown that an important fraction of this protein is transported to lysosomes (41,42). We have observed in our experiments a fragment that may correspond to a degradation product of B-Glyc-KDEL (Fig.…”

Section: Discussionsupporting

confidence: 51%

“…At this time, some B-Glyc-KDEL was already detectable in the ER (not shown). The presence of B-Glyc-KDEL in coated pits and vesicles suggests that the protein entered the cells through the clathrindependent pathway, as documented previously for Shiga toxin (41,42). After 2 h at 37°C, the ER became heavily labeled (Fig.…”

Section: Fig 4 Colocalization Of B-glyc-kdel and B-glyc-kdelgl Withmentioning

confidence: 56%

“…In addition, retrograde transport may target B-Glyc-KDEL to subcompartments of the ER which do not contain oligosaccharyltransferase activity. Diffusion of Bfragment in the ER might then be slowed by interaction with Sandvig and co-workers have shown by electron microscopic studies that Shiga toxin can be internalized via clathrin-coated pits and detected in endosomes, the Golgi apparatus, and the ER (17,18,41,42). It was thus assumed that Shiga toxin passes to the ER via the Golgi apparatus.…”

Section: Discussionmentioning

confidence: 99%

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Retrograde Transport of KDEL-bearing B-fragment of Shiga Toxin

Johannes¹,

Tenza

Antony

et al. 1997

Journal of Biological Chemistry

187

254

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To investigate retrograde transport along the biosynthetic/secretory pathway, we have constructed a recombinant Shiga toxin B-fragment carrying an N-glycosylation site and a KDEL retrieval motif at its carboxyl terminus (B-Glyc-KDEL). After incubation with HeLa cells, B-Glyc-KDEL was progressively glycosylated in the endoplasmic reticulum (ER) and remained stably associated with this compartment. B-fragment with a nonfunctional KDEL sequence (B-Glyc-KDELGL) was glycosylated with about the same kinetics as B-Glyc-KDEL but localized at steady state to the Golgi apparatus. Morphological studies showed that B-Glyc-KDEL was delivered from the plasma membrane, via endosomes and the cisternae of the Golgi apparatus, to the ER. Moreover, the addition of a sulfation site allowed us to show that B-Glyc-KDEL on transit to the ER entered the Golgi apparatus through the trans-Golgi network. Transport of B-Glyc-KDEL to the ER was slowed down by nocodazole, indicating that microtubules are important for the retrograde pathway. Our results document the existence of a continuous pathway from the plasma membrane to the endoplasmic reticulum via the Golgi apparatus and show that a fully folded exogenous protein arriving in the endoplasmic reticulum via this pathway can undergo N-glycosylation.

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Section: Discussionsupporting

confidence: 51%

Section: Fig 4 Colocalization Of B-glyc-kdel and B-glyc-kdelgl Withmentioning

confidence: 56%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Retrograde Transport of KDEL-bearing B-fragment of Shiga Toxin

Johannes¹,

Tenza

Antony

et al. 1997

Journal of Biological Chemistry

187

254

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“…A number of the protein toxins are produced by bacteria and are important for severe diseases caused by these organisms. This is, for instance, the case for diphtheria toxin, although vaccination of the population has helped to control this disease, and for pseudomonas toxin, tetanus toxin, botulinum toxin, and Shiga toxin [14]. Shiga toxin is not only produced by Shigella dysenteriae, which is the infective agent in dysenteria, but Shiga-like toxins are also produced by E. coli, giving rise to infections and disease and being a serious health problem in several countries [1,2].…”

Section: Introductionmentioning

confidence: 99%

Endocytosis and intracellular sorting of ricin and Shiga toxin

Sandvig

Deurs

1994

FEBS Letters

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AkstraetRicin and Shiga toxin belong to a group of protein toxins with targets in the cytosol. These toxins consist of one moiety that binds the toxin molecule to cell surface receptors, and another enzymatically active moiety that enters the cytosol after endocytic uptake of the toxin. The toxins are of current interest in relation to disease and the construction of immunotoxins. Moreover, they have proven useful to investigate mechanisms of endocytosis and to follow intracellular pathways of transport. Some of the recent results obtained with ricin and Shiga toxin are discussed.

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“…L'attachement du pentamère de sous-unités B induit l'entrée de la sous-unité A dans la cellule [128]. La toxine est internalisée par voie endocytosique et les vésicules formées, contenant la toxine, fusionnent avec des lysosomes.…”

Section: Arrêt De La Synthèse Protéiqueunclassified

Les récepteurs des entérotoxines bactériennes

Rousset

2000

Vet. Res.

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-Bacterial enterotoxin receptors. Enteric bacterial toxins display a great diversity in their structure, molecular weight and mechanism of action. The interaction of enterotoxins with the intestinal mucosa either leads to a direct effect on the cell membrane or an effect on signal transduction within eukaryotic cells. However, before a toxin can affect a cell, it must after its secretion by a microorganism, recognise and bind to a specific surface molecule, its receptor. Membrane receptors of bacterial enterotoxins have been identified as protein, glycoprotein or glycolipid in nature. The chemical nature of the molecules acting as receptors is crucial and during evolution they have been carefully selected. Some toxins, after their interaction with a receptor molecule, will transduce a signal across the cell membrane while remaining at the cell surface. Other toxins, after this initial binding step with a receptor, will be internalised. Others can form pores leading to leakage of cellular components and cell lysis. Receptors that have been identified often comprise a saccharidic chain that is directly involved in the recognition and binding of the toxin. Today, models explaining toxin-receptor interactions are more complex, including multistep events. This review summarises the knowledge of the interactions between bacterial toxins and membrane receptors present on intestinal mucosa. receptor / intestine / enterotoxin / binding epitope / glycosphingolipidRésumé -Les toxines bactériennes entériques présentent une grande diversité autant dans leur structure que dans leur poids moléculaire et leur mécanisme d'action. L'interaction des entérotoxines avec la muqueuse intestinale conduit soit à un effet direct sur la paroi cellulaire de la cellule hôte, soit à un dérèglement des voies de signalisation de celle-ci. Toutefois, avant même d'affecter la cellule cible, la toxine sécrétée par le micro-organisme devra reconnaître et s'attacher à une molécule présente à la surface cellulaire, son récepteur. Les récepteurs membranaires des entérotoxines bactériennes peuvent être de nature protéique, glycoprotéique ou glycolipidique. La nature chimique de ces récepteurs, sur laquelle repose la spécificité, est primordiale et au cours de l'évolution ceuxci ont été soigneusement sélectionnés. Certaines toxines, une fois en contact avec leur récepteur, envoient un signal à l'intérieur de la cellule tout en demeurant à la surface alors que d'autres toxines sont internalisées. Enfin, certaines toxines bactériennes peuvent former des pores dans la membrane Vet. Res. 31 (2000)

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Endocytosis from coated pits of Shiga toxin: a glycolipid-binding protein from Shigella dysenteriae 1.

Abstract: Abstract. Evidence is presented that endocytosis is involved in the transport to the cytosol of the cytotoxin from Shigella dysenteriae 1, Shiga toxin, which acts

Cited by 245 publications

References 48 publications

Retrograde Transport of KDEL-bearing B-fragment of Shiga Toxin

Retrograde Transport of KDEL-bearing B-fragment of Shiga Toxin

Endocytosis and intracellular sorting of ricin and Shiga toxin

Les récepteurs des entérotoxines bactériennes

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