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.
journal_name
Proc Natl Acad Sci U S Aauthors
Belyi Y,Niggeweg R,Opitz B,Vogelsgesang M,Hippenstiel S,Wilm M,Aktories Kdoi
10.1073/pnas.0601562103subject
Has Abstractpub_date
2006-11-07 00:00:00pages
16953-8issue
45eissn
0027-8424issn
1091-6490pii
0601562103journal_volume
103pub_type
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