Legionella pneumophila glucosyltransferase inhibits host elongation factor 1A.

Abstract:

:Legionella pneumophila, the causal agent of Legionnaires' disease, is an intracellular parasite and invades and proliferates within different eukaryotic cells, including human alveolar macrophages. After several 100-fold multiplication within host cells, the pathogens are released for new invasion by induction of apoptosis or necrosis. Here we report that L. pneumophila produces a glucosyltransferase, which selectively modifies an approximately 50-kDa mammalian protein by using UDP-glucose as a cosubstrate. MS analysis identified the protein substrate as the mammalian elongation factor (EF)1A. Legionella glucosyltransferase modifies its eukaryotic protein substrate at serine-53, which is located in the GTPase domain of the EF. Glucosylation of EF1A results in inhibition of eukaryotic protein synthesis and death of target cells. Our findings show a mode of inhibition of protein synthesis by microbial pathogens and offer a perspective for understanding of the host-pathogen interaction of L. pneumophila.

authors

Belyi Y,Niggeweg R,Opitz B,Vogelsgesang M,Hippenstiel S,Wilm M,Aktories K

doi

10.1073/pnas.0601562103

subject

Has Abstract

pub_date

2006-11-07 00:00:00

pages

16953-8

issue

45

eissn

0027-8424

issn

1091-6490

pii

0601562103

journal_volume

103

pub_type

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