Bacterial effectors manipulate membranes

Science ◽  
2021 ◽  
Vol 372 (6545) ◽  
pp. 929.5-930
Author(s):  
Stella M. Hurtley
Keyword(s):  
Bacterial Effectors

scholarly journals Host–pathogen interplay and the evolution of bacterial effectors

2007 ◽  
Vol 0 (0) ◽  
pp. 071127144819001-??? ◽  
Author(s):  
John Stavrinides ◽  
Honour C. McCann ◽  
David S. Guttman
Keyword(s):  
Host Pathogen ◽  
Bacterial Effectors

scholarly journals Exploitation of conserved eukaryotic host cell farnesylation machinery by an F-box effector of Legionella pneumophila

2010 ◽  
Vol 207 (8) ◽  
pp. 1713-1726 ◽  
Author(s):  
Christopher T.D. Price ◽  
Tasneem Al-Quadan ◽  
Marina Santic ◽  
Snake C. Jones ◽  
Yousef Abu Kwaik
Keyword(s):  
Legionella Pneumophila ◽  
Biological Function ◽  
Host Cells ◽  
Dependent Manner ◽  
Protein Farnesyltransferase ◽  
Type Iv ◽  
Eukaryotic Proteins ◽  
Bacterial Effectors

Farnesylation involves covalent linkage of eukaryotic proteins to a lipid moiety to anchor them into membranes, which is essential for the biological function of Ras and other proteins. A large cadre of bacterial effectors is injected into host cells by intravacuolar pathogens through elaborate type III–VII translocation machineries, and many of these effectors are incorporated into the pathogen-containing vacuolar membrane by unknown mechanisms. The Dot/Icm type IV secretion system of Legionella pneumophila injects into host cells the F-box effector Ankyrin B (AnkB), which functions as platforms for the docking of polyubiquitinated proteins to the Legionella-containing vacuole (LCV) to enable intravacuolar proliferation in macrophages and amoeba. We show that farnesylation of AnkB is indispensable for its anchoring to the cytosolic face of the LCV membrane, for its biological function within macrophages and Dictyostelium discoideum, and for intrapulmonary proliferation in mice. Remarkably, the protein farnesyltransferase, RCE-1 (Ras-converting enzyme-1), and isoprenyl cysteine carboxyl methyltransferase host farnesylation enzymes are recruited to the LCV in a Dot/Icm-dependent manner and are essential for the biological function of AnkB. In conclusion, this study shows novel localized recruitment of the host farnesylation machinery and its anchoring of an F-box effector to the LCV membrane, and this is essential for biological function in vitro and in vivo.

Cyclomodulins: bacterial effectors that modulate the eukaryotic cell cycle

2005 ◽  
Vol 13 (3) ◽  
pp. 103-110 ◽  
Author(s):  
Jean-Philippe Nougayrède ◽  
Frédéric Taieb ◽  
Jean De Rycke ◽  
Eric Oswald
Keyword(s):  
Cell Cycle ◽  
Eukaryotic Cell ◽  
Bacterial Effectors

scholarly journals Deciphering the mode of action and host recognition of bacterial type III effectors

2010 ◽  
Vol 37 (10) ◽  
pp. 926 ◽  
Author(s):  
Selena Gimenez-Ibanez ◽  
Dagmar R. Hann ◽  
John P. Rathjen
Keyword(s):  
Mode Of Action ◽  
Pathogenic Bacteria ◽  
Plant Immunity ◽  
Plant Defence ◽  
Host Recognition ◽  
Type Iii Effectors ◽  
Host Cytoplasm ◽  
Host Plasma Membrane ◽  
Defence Responses ◽  
Bacterial Effectors

Plant pathogenic bacteria adhere to cell walls and remain external to the cell throughout the pathogenic lifecycle, where they elicit host immunity through host plasma membrane localised receptors. To be successful pathogens, bacteria must suppress these defence responses, which they do by secreting a suite of virulence effector molecules into the host cytoplasm. However, effectors themselves can act as elicitors after perception by intracellular host immune receptors, thus, re-activating plant immunity. Bacterial effectors generally target host molecules through specific molecular activities to defeat plant defence responses. Although effectors can be used as tools to elucidate components of plant immunity, only a handful of these molecular targets are known and much remains to be learnt about effector strategies for bacterial pathogenicity. This review highlights recent advances in our understanding of the mode of action of bacterial effectors, which in the future will lead to improvements in agriculture.

scholarly journals A family of T6SS antibacterial effectors related to L,D-transpeptidases targets the Peptidoglycan

2020 ◽  
Vol 2 (7A) ◽  
Author(s):  
Stephanie Sibinelli de Sousa ◽  
Julia Takuno Hespanhol ◽  
Bruno Matsuyama ◽  
Stephane Mesnage ◽  
Gianlucca Nicastro ◽  
...  
Keyword(s):  
Cell Envelope ◽  
Point Mutations ◽  
Time Lapse ◽  
Secretion Systems ◽  
Bacterial Antagonism ◽  
New Family ◽  
Type Vi Secretion ◽  
Altered Cell ◽  
Bacterial Effectors ◽  
Insight Into

Type VI secretion systems (T6SSs) are contractile nanomachines widely used by bacteria to intoxicate competitors. Salmonella Typhimurium encodes a T6SS within the Salmonella pathogenicity island 6 (SPI-6) that is used during competition against species of the gut microbiota. We characterized a new SPI-6 T6SS antibacterial effector named Tlde1 (type VI L,D-transpeptidase effector 1). Tlde1 is toxic in target-cell periplasm and its toxicity is neutralized by co-expression with immunity protein Tldi1 (type VI L,D-transpeptidase immunity 1). Time-lapse microscopy revealed that intoxicated cells display altered cell division and lose cell envelope integrity. Bioinformatics analysis showed that Tlde1 is evolutionarily related to L,D-transpeptidases. Point mutations on conserved histidine121 and cysteine131 residues eliminated toxicity. Co-incubation of purified recombinant Tlde1 and peptidoglycan tetrapeptides showed that Tlde1 displays both L,D-carboxypeptidase activity by cleaving GM-tetrapeptides between meso-diaminopimelic acid3 and D-alanine4, and L,D-transpeptidase exchange activity by replacing D-alanine4 for a non-canonical D-amino acid. Tlde1 constitutes a new family of T6SS effectors widespread in Proteobacteria. This work increases our knowledge about the bacterial effectors used in interbacterial competitions and provides molecular insight into a new mechanism of bacterial antagonism.

Post-translational Mechanisms of Host Subversion by Bacterial Effectors

2017 ◽  
Vol 23 (12) ◽  
pp. 1088-1102 ◽  
Author(s):  
Nichollas E. Scott ◽  
Elizabeth L. Hartland
Keyword(s):  
Bacterial Effectors ◽  
Translational Mechanisms
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