title: Plasticity of listeriolysin O pores and its regulation by pH and unique histidine [corrected].
abstract: Pore formation of cellular membranes is an ancient mechanism of bacterial pathogenesis that allows efficient damaging of target cells. Several mechanisms have been described, however, relatively little is known about the assembly and properties of pores. Listeriolysin O (LLO) is a pH-regulated cholesterol-dependent cytolysin from the intracellular pathogen Listeria monocytogenes, which forms transmembrane β-barrel pores. Here we report that the assembly of LLO pores is rapid and efficient irrespective of pH. While pore diameters at the membrane surface are comparable at either pH 5.5 or 7.4, the distribution of pore conductances is significantly pH-dependent. This is directed by the unique residue H311, which is also important for the conformational stability of the LLO monomer and the rate of pore formation. The functional pores exhibit variations in height profiles and can reconfigure significantly by merging to other full pores or arcs. Our results indicate significant plasticity of large β-barrel pores, controlled by environmental cues like pH.
authors: Laboratory for Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.
authors: Marjetka
authors: M
authors: Podobnik
authors: Istituto di Biofisica, Consiglio Nazionale delle Ricerche &Fondazione Bruno Kessler, via alla Cascata 56/C, 38123 Trento, Italy.
authors: Marta
authors: M
authors: Marchioretto
authors: Istituto di Biofisica, Consiglio Nazionale delle Ricerche &Fondazione Bruno Kessler, via alla Cascata 56/C, 38123 Trento, Italy.
authors: Manuela
authors: M
authors: Zanetti
authors: Department of Biology, Biotechnical Faculty, University of Ljubljana, Večna pot 111, 1000 Ljubljana, Slovenia.
authors: Andrej
authors: A
authors: Bavdek
authors: Laboratory for Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.
authors: Matic
authors: M
authors: Kisovec
authors: Laboratory for Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.
authors: Miša Mojca
authors: MM
authors: Cajnko
authors: Istituto di Biofisica, Consiglio Nazionale delle Ricerche &Fondazione Bruno Kessler, via alla Cascata 56/C, 38123 Trento, Italy.
authors: Lorenzo
authors: L
authors: Lunelli
authors: Istituto di Biofisica, Consiglio Nazionale delle Ricerche &Fondazione Bruno Kessler, via alla Cascata 56/C, 38123 Trento, Italy.
authors: Mauro
authors: M
authors: Dalla Serra
authors: 1] Laboratory for Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia [2] Department of Biology, Biotechnical Faculty, University of Ljubljana, Večna pot 111, 1000 Ljubljana, Slovenia.
authors: Gregor
authors: G
authors: Anderluh
mesh_terms: D000595:Amino Acid Sequence; D001427:Bacterial Toxins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006460:Hemolysin Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006639:Histidine / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008089:Listeria monocytogenes / Q000472:pathogenicity / Q000502:physiology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D066329:Protein Aggregates; D011487:Protein Conformation; D055503:Protein Multimerization; D055550:Protein Stability; D016415:Sequence Alignment
chemical_list: D001427:Bacterial Toxins; D006360:Heat-Shock Proteins; D006460:Hemolysin Proteins; D066329:Protein Aggregates; D006639:Histidine; C038705:hlyA protein, Listeria monocytogenes