Internalin must be on the bacterial surface to mediate entry of Listeria monocytogenes into epithelial cells.

Abstract:

:Entry of Listeria monocytogenes into cultured epithelial cells requires production of internalin, a protein with features characteristic of some Gram-positive bacterial surface proteins, in particular an LPXTG motif preceding a hydrophobic sequence and a few basic residues at its C-terminal end. By immunofluorescence and immunogold labelling, we show that in wild-type L. monocytogenes, internalin is present on the cell surface and has a polarized distribution similar to that of ActA, another surface protein of L. monocytogenes involved in actin assembly. Through a genetic analysis, we establish that the C-terminal region of internalin is necessary for cell-surface association, and that although internalin is partially released in the culture medium, its location on the bacterial surface is required to promote entry. Finally, using a 'domain-swapping' strategy-replacement of the cell wall anchor of IniA by the membrane anchor of ActA- we show that the reduced ability to adhere and enter cells of strains expressing IniA-ActA correlates with a lower amount of surface-exposed internalin. Taken together, these results suggest that internalin exposed on the bacterial surface mediates direct contact between the bacterium and the host cell.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Lebrun M,Mengaud J,Ohayon H,Nato F,Cossart P

doi

10.1111/j.1365-2958.1996.tb02566.x

subject

Has Abstract

pub_date

1996-08-01 00:00:00

pages

579-92

issue

3

eissn

0950-382X

issn

1365-2958

journal_volume

21

pub_type

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