Receptor-mediated uptake of Legionella pneumophila by Acanthamoeba castellanii and Naegleria lovaniensis

Investigation of the attachment and uptake of Legionella pneumophila by Acanthamoeba castellanii and Naegleria lovaniensis, as these are two critical steps in the subsequent bacterial survival in both amoeba hosts. Initially, the mode of Legionella uptake was examined using inhibitors of microfilament-dependent and receptor-mediated uptake phagocytosis. Secondly, the minimum saccharide structure to interfere with L. pneumophila uptake was determined by means of selected saccharides. Bacterial attachment and uptake by each of the amoeba species occurred through a receptor-mediated endocytosis, which required de novo synthesis of host proteins. Legionella pneumophila showed a high affinity to the α1-3 d-mannobiose domain of the mannose-binding receptor located on A. castellanii. In contrast, L. pneumophila bacteria had a high affinity for the GalNAcβ1-4Gal domain of the N-acetyl- d-galactosamine receptor of N. lovaniensis. Our data pointed to a remarkable adaptation of L. pneumophila to invade different amoeba hosts, as the uptake by both amoeba species is mediated by two different receptor families. The fact that L. pneumophila is taken up by two different amoeba species using different receptor families adds further complexity to the host-parasite interaction process, as 14 amoeba species are known to be appropriate Legionella hosts.