E-Cadherin Is the Receptor for Internalin, a Surface Protein Required for Entry of L. monocytogenes into Epithelial Cells

Mengaud, J; Ohayon, Hélène; Gounon, Pierre; Mège, René-Marc; Cossart, Pascale

doi:10.1016/s0092-8674(00)81070-3

Cited by 801 publications

(655 citation statements)

References 60 publications

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“…Thus, cellular processes regulated by this kinase appear to be induced upon interaction of these bacteria with a cellular receptor(s). These results are in accordance with previous data postulating a zipper type of entry of L. monocytogenes (Swanson and Baer, 1995;Mengaud et al, 1996a;Finlay and Cossart, 1997).…”

Section: Discussionsupporting

confidence: 93%

“…Finally, physical association of purified native InlB with the surface of two non-invasive strains, ⌬inl B2 and ⌬inlAB2, increased their ability to invade HUVECs by about 28-and 23-fold, respectively, more than the wild-type strain. Although the distribution of L. monocytogenes is centripetal in Caco-2 cells, with invasion taking place from the cell periphery (Mengaud et al, 1996a), in the case of HUVECs, it was not localized only to the cell periphery but also occurred throughout the surface of the infected cell.…”

Section: Discussionmentioning

confidence: 96%

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Internalin B is essential for adhesion and mediates the invasion of Listeria monocytogenes into human endothelial cells

Parida

Domann

Rohde

et al. 1998

Molecular Microbiology

162

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SummaryListeria monocytogenes causes rhombencephalitis in humans and animals and also affects the fetus in utero, causing disseminated sepsis. In both instances, the infection occurs by the crossing of endothelial cells lining a physiological barrier, the blood-brain barrier or the transplacental barrier. In this study, the ability of L. monocytogenes wild-type EGD to invade human umbilical vein endothelial cells (HUVECs) was evaluated using wild-type bacteria and isogenic Listeria mutants. Here, we show that invasion of HUVECs by L. monocytogenes is dependent on the expression of the internalin B gene product. This was demonstrated in several ways. First, L. monocytogenes strains lacking the inl B gene did not invade HUVECs. Secondly, avid invasion was obtained when a strain deleted for inlAB was complemented with a plasmid harbouring inl B only, whereas strains expressing inlA did not enter HUVECs. Thirdly, entry of wild-type EGD could be blocked effectively with antibodies to InlB. Fourthly, cell binding assays and flow cytometry with HUVECs showed binding of purified InlB, but not InlA, suggesting a tropism of InlB for this cell type. Finally, physical association of purified native InlB with the surface of non-invasive mutants dramatically increased their ability to invade HUVECs. In laser-scanning confocal microscopy, binding of InlB was observed as focal and localized patches on the cell surface of HUVECs. Qualitative examination of the entry process by scanning electron microscopy revealed that both wild-type EGD and a recombinant strain overexpressing only InlB enter HUVECs in a similar fashion. The entry process was polarized, involved single bacteria and occurred over the entire surface of endothelial cells.

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Section: Discussionsupporting

confidence: 93%

Section: Discussionmentioning

confidence: 96%

Internalin B is essential for adhesion and mediates the invasion of Listeria monocytogenes into human endothelial cells

Parida

Domann

Rohde

et al. 1998

Molecular Microbiology

162

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“…A similar mechanism has been described for Listeria monocytogenes, in which bacterial internalin A binds to E-cadherin on the cell surface (Mengaud et al, 1996). In both cases, the bacterium is not actively involved in the invasion process, but rather relies on signal transduction from the host cell receptor to the cytoskeleton.…”

Section: Introductionmentioning

confidence: 71%

Fibronectin-binding protein acts as Staphylococcus aureus invasin via fibronectin bridging to integrin alpha5beta1

Sinha¹,

François²,

Nüße³

et al. 1999

Cell Microbiol

515

563

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SummaryThe ability of Staphylococcus aureus to invade mammalian cells may explain its capacity to colonize mucosa and to persist in tissues after bacteraemia. To date, the underlying molecular mechanisms of cellular invasion by S. aureus are unknown, despite its high prevalence and dif®culties in treatment. Here, we show cellular invasion as a novel function for an S. aureus adhesin, previously implicated solely in attachment. S. aureus, but not S. epidermidis, invaded epithelial 293 cells in a temperature-and F-actindependent manner. Formaldehyde-®xed and live bacteria were equally invasive, suggesting that no active bacterial process was involved. All clinical S. aureus isolates analysed, but only a subset of laboratory strains, were invasive. Fibronectin-binding proteins (FnBPs) acted as S. aureus invasins, because: (i) FnBP deletion mutants of invasive laboratory strains lost invasiveness; (ii) expression of FnBPs in noninvasive strains conferred invasiveness; and (iii) the soluble isolated ®bronectin-binding domain of FnBP (D1±D4) completely blocked invasion. Integrin a 5 b 1 served as host cell receptor, which interacted with staphylococcal FnBPs through cellular or soluble ®bronectin. FnBP-de®cient mutants lost invasiveness for epithelial cells, endothelial cells and ®broblasts. Thus, ®bronectin-dependent bridging between S. aureus FnBPs and host cell integrin a 5 b 1 is a conserved mechanism for S. aureus invasion of human cells. This may prove useful in developing new therapeutic and vaccine strategies for S. aureus infections.

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“…The two major invasion proteins are internalin (InlA) and InlB. The receptor for InlA is E-cadherin [Mengaud et al, 1996], and the receptors for InlB are gC1qR/p32 (the receptor for the globular part of complement component C1q), Met/hepatocyte growth factor (HGF) receptor, and glycosaminoglycans [Braun et al, 2000;Shen et al, 2000;Jonquières et al, 2001].…”

Section: Bmentioning

confidence: 99%

Cytoskeleton rearrangements during Listeria infection: Clathrin and septins as new players in the game

Mostowy

Cossart

2009

Cell Motil. Cytoskeleton

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The study of an infection process can reveal how microbes exploit the host, and can illuminate unknown host cellular functions. Invasive pathogens have evolved efficient strategies to promote their internalization within normally non-phagocytic host cells. The so-called ''zippering'' bacteria present to host cell receptors molecules that mimic endogenous ligands, thereby inducing specific intracellular signaling cascades ultimately resulting in actin polymerization and uptake. Here we review how the bacterial pathogen Listeria monocytogenes enters into cells, and present a series of studies revealing that in addition to actin rearrangements this bacterium exploits the clathrin-mediated endocytosis machinery together with septins, a novel cytoskeleton element. The challenge is now to decipher how all of these components orchestrate themselves to permit entry into normally non-phagocytic cells. Cell Motil. Cytoskeleton 66: 816-823, 2009. '

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E-Cadherin Is the Receptor for Internalin, a Surface Protein Required for Entry of L. monocytogenes into Epithelial Cells

Cited by 801 publications

References 60 publications

Internalin B is essential for adhesion and mediates the invasion of Listeria monocytogenes into human endothelial cells

Internalin B is essential for adhesion and mediates the invasion of Listeria monocytogenes into human endothelial cells

Fibronectin-binding protein acts as Staphylococcus aureus invasin via fibronectin bridging to integrin alpha5beta1

Cytoskeleton rearrangements during Listeria infection: Clathrin and septins as new players in the game

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