Photorhabdus luminescens Toxins ADP-Ribosylate Actin and RhoA to Force Actin Clustering

The bacterium Photorhabdus luminescens is mutualistically associated with entomopathogenetic nematodes. These nematodes invade insect larvae and release the bacteria from their intestine, which kills the insects through the action of toxin complexes. We elucidated the mode of action of two of these...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2010-02, Vol.327 (5969), p.1139-1142
Main Authors: Lang, Alexander E, Schmidt, Gudula, Schlosser, Andreas, Hey, Timothy D, Larrinua, Ignacio M, Sheets, Joel J, Mannherz, Hans G, Aktories, Klaus
Format: Article
Language:English
Subjects:
Actins
Actins - chemistry
Actins - metabolism
Adenosine Diphosphate Ribose - metabolism
ADP Ribose Transferases - chemistry
ADP Ribose Transferases - metabolism
Amino acids
Animals
Bacteria
Bacterial Toxins - chemistry
Bacterial Toxins - metabolism
Bacterial Toxins - pharmacology
Bacteriology
Biochemistry
Biological and medical sciences
Cell Line
Fundamental and applied biological sciences. Psychology
Glutamine - metabolism
HeLa Cells
Hemocytes
Hemocytes - immunology
Humans
Insect larvae
Microbiology
Miscellaneous
Moths
Nematoda
Nematodes
Phagocytosis - drug effects
Photorhabdus
Photorhabdus luminescens
Polymerization
Proteins
rhoA GTP-Binding Protein - metabolism
Signal Transduction
Stress Fibers - metabolism
Threonine - metabolism
Thymosin - metabolism
Thymosin - pharmacology
Toxicology
Toxins
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Summary:The bacterium Photorhabdus luminescens is mutualistically associated with entomopathogenetic nematodes. These nematodes invade insect larvae and release the bacteria from their intestine, which kills the insects through the action of toxin complexes. We elucidated the mode of action of two of these insecticidal toxins from P. luminescens. We identified the biologically active components TccC3 and TccC5 as adenosine diphosphate (ADP)-ribosyltransferases, which modify unusual amino acids. TccC3 ADP-ribosylated threonine-148 of actin, resulting in actin polymerization. TccC5 ADP-ribosylated Rho guanosine triphosphatase proteins at glutamine-61 and glutamine-63, inducing their activation. The concerted action of both toxins inhibited phagocytosis of target insect cells and induced extensive intracellular polymerization and clustering of actin. Several human pathogenic bacteria produce related toxins.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1184557