Cultured mammalian cells attach to the invasin protein of Yersinia pseudotuberculosis.

Isberg, Ralph R.; Leong, John M.

doi:10.1073/pnas.85.18.6682

Cited by 82 publications

(60 citation statements)

References 35 publications

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“…The fibrinogen molecule contains two RGD sequences both on the Aa chain and an additional aIIb/3 binding site located at the carboxyl-terminus ofthe oy chain, which includes 12 amino acids, but does not contain the RGD sequence (42). This dodecapeptide and RGD containing peptides compete with each other for binding to aIIbA3 (43 (55,56). Specific binding of purified invasin to f1 chain paired to a chains 3, 4, 5, or 6 (57) suggests that attachment and entry into cells ofbacteria expressing invasin requires these integrins.…”

Section: Discussionmentioning

confidence: 99%

Kistrin, an integrin antagonist, blocks endocytosis of fibrinogen into guinea pig megakaryocyte and platelet alpha-granules.

Handagama¹,

Bainton²,

Jacques³

et al. 1993

J. Clin. Invest.

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Recent data indicate that megakaryocyte/platelet a-granule fibrinogen is endocytosed from plasma. Because fibrinogen is the major platelet protein present in high concentrations in a-granules, fibrinogen uptake into a-granules may occur via specific receptors. In that cells of the megakaryocyte/platelet lineage contain two integrins-am63 (GP IIb-Illa) and the vitronectin receptor (a'83)-that can bind fibrinogen, one or both of these receptors may mediate the endocytic uptake of fibrinogen. To test this hypothesis, we examined the effect of Kistrin, an RGD-containing protein purified from the venom of Agkistrodon rhodostoma that inhibits fibrinogen binding to human platelet receptors, on endocytosis of fibrinogen by megakaryocytes and platelets. Continuous intravenous infusion of kistrin into guinea pigs (200 ag/h) over a 24-h period inhibited collagen-induced platelet aggregation. When biotinylated fibrinogen was injected intravenously into animals receiving Kistrin, megakaryocytes failed to endocytose the labeled fibrinogen. Endocytosis of fibrinogen into platelets was also inhibited in these animals. In contrast, platelets and megakaryocytes obtained from shaminfused control animals contained the injected biotinylated fibrinogen. We conclude that, in addition to the well-known extracellular function of cell adhesion, integrins can also act as receptors that mediate endocytosis of exogenous proteins and incorporate them into regulated secretory granules. (J. Clin. Invest. 1993. 91:193-200.)

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Section: Discussionmentioning

confidence: 99%

Kistrin, an integrin antagonist, blocks endocytosis of fibrinogen into guinea pig megakaryocyte and platelet alpha-granules.

Handagama¹,

Bainton²,

Jacques³

et al. 1993

J. Clin. Invest.

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“…Filters were washed twice in PBS, and then incubated for 2 h at 378C in 5% CO 2 with freshly resuspended cells (either trypsinized or EDTA treated) diluted at 1.10 6 per ml in RPMI containing 0.5% BSA (Isberg and Leong, 1988). The filters were then washed twice with the same medium, fixed with 3% (w/v) paraformaldehyde, and then stained with amido black to visualize attached cells (Hayman et al, 1982).…”

Section: Western Immunoblottingmentioning

confidence: 99%

The microneme protein MIC3 of Toxoplasma gondii is a secretory adhesin that binds to both the surface of the host cells and the surface of the parasite

Lebrun²,

et al. 2000

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SummaryAssay of the adhesion of cultured cells on Toxoplasma gondii tachyzoite protein Western blots identified a major adhesive protein, that migrated at 90 kDa in non-reducing gels. This band comigrated with the previously described microneme protein MIC3. Cellular binding on Western blots was abolished by MIC3-specific monoclonal and polyclonal antibodies. The MIC3 protein affinity purified from tachyzoite lysates bound to the surface of putative host cells. In addition, T. gondii tachyzoites also bound to immobilized MIC3. Immunofluorescence analysis of T. gondii tachyzoite invasion showed that MIC3 was exocytosed and relocalized to the surface of the parasite during invasion. The cDNA encoding MIC3 and the corresponding gene have been cloned, allowing the determination of the complete coding sequence. The MIC3 sequence has been confirmed by affinity purification of the native protein and N-terminal sequencing. The deduced protein sequence contains five partially overlapping EGF-like domains and a chitin binding-like domain, which can be involved in protein±protein or protein± carbohydrate interactions. Taken together, these results suggest that MIC3 is a new microneme adhesin of T. gondii.

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“…Evidence for this property was obtained by demonstrating that membrane extracts containing invasin were able to support attachment ot mammalian cells to solid surfaces ( Fig. 1; Isberg and Leong, 1988). That the mammalian cells were directly attaching to invasin was shown by fractionating the extracts on polyacrylamide gels, transferring the proteins to nitrocellulose filters, and showing that the cells attached to a region of the filter replica that corresponded to the mobility of invasin.…”

Section: Entry Of Enteropathogenic Yersiniamentioning

confidence: 99%

“…The filter was then allowed to incubate in the presence of HEp-? cells before gltitaraldehyde fixation and scanning electron microscopy (Isberg and Leong, 1988). Note the spreading behaviour of cells attached to (he filtw Falkow.…”

Section: Entry Of Enteropathogenic Yersiniamentioning

confidence: 99%

“…That the mammalian cells were directly attaching to invasin was shown by fractionating the extracts on polyacrylamide gels, transferring the proteins to nitrocellulose filters, and showing that the cells attached to a region of the filter replica that corresponded to the mobility of invasin. This binding is apparently critical for the penetration process, because monoclonal antibodies that block such cellular attachment prevent E. coli strains which are expressing invasin from entering cultured cells (Isberg and Leong, 1988).…”

Section: Entry Of Enteropathogenic Yersiniamentioning

confidence: 99%

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Mammalian cell adhesion functions and cellular penetration of enteropathogenic Yersinia species

Isberg

1989

Molecular Microbiology

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SummaryThe entry of enteropathogenic Yersinia into cultured mammalian ceils has been studied in order to gain insight into the mechanism of bacterial penetration into host cells during infection. There exist at least three pathways for entry by Yersinia into mammalian cells, the most efficient of which is promoted by invasJn, the product of the invgene. Invasin is an outer membrane protein that attaches to a mammalian cell receptor, initiating the entry process. Several receptors that bind invasin have been identified, and each is a member of the VLA family of integrin cell adhesion molecules. The role of integrins in the entry process is discussed, as is the ability of invasin to stimulate uptake by binding to its integrin receptor.

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Cultured mammalian cells attach to the invasin protein of Yersinia pseudotuberculosis.

Cited by 82 publications

References 35 publications

Kistrin, an integrin antagonist, blocks endocytosis of fibrinogen into guinea pig megakaryocyte and platelet alpha-granules.

Kistrin, an integrin antagonist, blocks endocytosis of fibrinogen into guinea pig megakaryocyte and platelet alpha-granules.

The microneme protein MIC3 of Toxoplasma gondii is a secretory adhesin that binds to both the surface of the host cells and the surface of the parasite

Mammalian cell adhesion functions and cellular penetration of enteropathogenic Yersinia species

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