Platelet-activating factor receptor initiates contact of Acinetobacter baumannii expressing phosphorylcholine with host cells.
Adhesion is an initial and important step in Acinetobacter baumannii causing infections. However, the exact molecular mechanism of such a step between A. baumannii and the host cells remains unclear. Here, we demonstrated that the phosphorylcholine (ChoP)-containing outer membrane protein of A. baumannii binds to A549 cells through platelet-activating factor receptor (PAFR), resulting in activation of G protein and intracellular calcium. Upon A. baumannii expressing ChoP binding to PAFR, clathrin and β-arrestins, proteins involved in the direction of the vacuolar movement, are activated during invasion of A. baumannii. PAFR antagonism restricts the dissemination of A. baumannii in the pneumonia model. These results define a role for PAFR in A. baumannii interaction with host cells and suggest a mechanism for the entry of A. baumannii into the cytoplasm of host cells.
Clinic Unit of Infectious Diseases, Microbiology and Preventive Medicine, Institute of Biomedicine of Seville (IBiS), University Hospital Virgen del Rocío/CSIC/University of Seville, 41013 Seville, Spain. y_smani@hotmail.com
Younes
Y
Smani
Fernando
F
Docobo-Pérez
Rafael
R
López-Rojas
Juan
J
Domínguez-Herrera
José
J
Ibáñez-Martínez
Jerónimo
J
Pachón
D040981:Acinetobacter baumannii / Q000378:metabolism*; D019390:Arrestins / Q000378:metabolism; D001422:Bacterial Adhesion; D002460:Cell Line; D002966:Clathrin / Q000378:metabolism; D019204:GTP-Binding Proteins / Q000378:metabolism; D006801:Humans; D010767:Phosphorylcholine / Q000378:metabolism*; D010980:Platelet Membrane Glycoproteins / Q000378:metabolism*; D043562:Receptors, G-Protein-Coupled / Q000378:metabolism*; D000071557:beta-Arrestins
D019390:Arrestins; D002966:Clathrin; D010980:Platelet Membrane Glycoproteins; D043562:Receptors, G-Protein-Coupled; D000071557:beta-Arrestins; C039351:platelet activating factor receptor; D010767:Phosphorylcholine; D019204:GTP-Binding Proteins