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Bordetella pertussis whole-cell vaccines (wP) caused a spectacular drop of global pertussis incidence, but since the replacement of wP with acellular pertussis vaccines (aP), pertussis has resurged in developed countries within 7 to 12 years of the change from wP to aP. In the mouse infection model, we examined whether addition of further protective antigens into the aP vaccine, such as type 2 and type 3 fimbriae (FIM2/3) with outer membrane lipooligosaccharide (LOS) and/or of the adenylate cyclase toxoid (dACT), which elicits antibodies neutralizing the CyaA toxin, could enhance the capacity of the aP vaccine to prevent colonization of the nasal mucosa by B. pertussis. The addition of the toxoid and of the opsonizing antibody-inducing agglutinogens modestly enhanced the already high capacity of intraperitoneally-administered aP vaccine to elicit sterilizing immunity, protecting mouse lungs from B. pertussis infection. At the same time, irrespective of FIM2/3 with LOS and dACT addition, the aP vaccination ablated the natural capacity of BALB/c mice to clear B. pertussis infection from the nasal cavity. While wP or sham-vaccinated animals cleared the nasal infection with similar kinetics within 7 weeks, administration of the aP vaccine promoted persistent colonization of mouse nasal mucosa by B. pertussis.
Jana Holubová; Ondřej Staněk; Ludmila Brázdilová; Jiří Mašín; Ladislav Bumba; Andrew R. Gorringe; Frances Alexander; Peter Šebo. Acellular Pertussis Vaccine Inhibits Bordetella pertussis Clearance from the Nasal Mucosa of Mice. Vaccines 2020, 8, 695 .
AMA StyleJana Holubová, Ondřej Staněk, Ludmila Brázdilová, Jiří Mašín, Ladislav Bumba, Andrew R. Gorringe, Frances Alexander, Peter Šebo. Acellular Pertussis Vaccine Inhibits Bordetella pertussis Clearance from the Nasal Mucosa of Mice. Vaccines. 2020; 8 (4):695.
Chicago/Turabian StyleJana Holubová; Ondřej Staněk; Ludmila Brázdilová; Jiří Mašín; Ladislav Bumba; Andrew R. Gorringe; Frances Alexander; Peter Šebo. 2020. "Acellular Pertussis Vaccine Inhibits Bordetella pertussis Clearance from the Nasal Mucosa of Mice." Vaccines 8, no. 4: 695.
Two distinct conformers of the adenylate cyclase toxin (CyaA) appear to accomplish its two parallel activities within target cell membrane. The translocating conformer would deliver the N-terminal adenylyl cyclase (AC) enzyme domain across plasma membrane into cytosol of cells, while the pore precursor conformer would assemble into oligomeric cation-selective pores and permeabilize cellular membrane. Both toxin activities then involve a membrane-interacting ‘AC-to-Hly-linking segment’ (residues 400 to 500). Here, we report the NMR structure of the corresponding CyaA411–490 polypeptide in dodecylphosphocholine micelles and show that it consists of two α-helices linked by an unrestrained loop. The N-terminal α-helix (Gly418 to His439) remained solvent accessible, while the C-terminal α-helix (His457 to Phe485) was fully enclosed within detergent micelles. CyaA411–490 weakly bound Ca2+ ions (apparent KD 2.6 mM) and permeabilized negatively charged lipid vesicles. At high concentrations (10 μM) the CyaA411–490 polypeptide formed stable conductance units in artificial lipid bilayers with applied voltage, suggesting its possible transmembrane orientation in the membrane-inserted toxin. Mutagenesis revealed that two clusters of negatively charged residues within the ‘AC-to-Hly-linking segment’ (Glu419 to Glu432 and Asp445 to Glu448) regulate the balance between the AC domain translocating and pore-forming capacities of CyaA in function of calcium concentration.
Anna Sukova; Ladislav Bumba; Pavel Srb; Vaclav Veverka; Ondrej Stanek; Jana Holubova; Josef Chmelik; Radovan Fiser; Peter Sebo; Jiri Masin. Negative charge of the AC-to-Hly linking segment modulates calcium-dependent membrane activities of Bordetella adenylate cyclase toxin. Biochimica et Biophysica Acta (BBA) - Biomembranes 2020, 1862, 183310 .
AMA StyleAnna Sukova, Ladislav Bumba, Pavel Srb, Vaclav Veverka, Ondrej Stanek, Jana Holubova, Josef Chmelik, Radovan Fiser, Peter Sebo, Jiri Masin. Negative charge of the AC-to-Hly linking segment modulates calcium-dependent membrane activities of Bordetella adenylate cyclase toxin. Biochimica et Biophysica Acta (BBA) - Biomembranes. 2020; 1862 (9):183310.
Chicago/Turabian StyleAnna Sukova; Ladislav Bumba; Pavel Srb; Vaclav Veverka; Ondrej Stanek; Jana Holubova; Josef Chmelik; Radovan Fiser; Peter Sebo; Jiri Masin. 2020. "Negative charge of the AC-to-Hly linking segment modulates calcium-dependent membrane activities of Bordetella adenylate cyclase toxin." Biochimica et Biophysica Acta (BBA) - Biomembranes 1862, no. 9: 183310.
Cytolytic leukotoxins of the repeat in toxin (RTX) family are large proteins excreted by gram-negative bacterial pathogens through the type 1 secretion system (T1SS). Due to low yields and poor stability in cultures of the original pathogens, it is useful to purify recombinant fatty-acylated RTX cytolysins from inclusion bodies produced in E. coli. Such preparations are, however, typically contaminated by high amounts of E. coli lipopolysaccharide (LPS or endotoxin). We report a simple procedure for purification of large amounts of biologically active and endotoxin-free RTX toxins. It is based on the common feature of RTX cytolysins that are T1SS-excreted as unfolded polypeptides and fold into a biologically active toxin only upon binding of calcium ions outside of the bacterial cell. Mimicking this process, the RTX proteins are solubilized from inclusion bodies with buffered 8 M urea, bound onto a suitable chromatographic medium under denaturing conditions and the contaminating LPS is removed through extensive on-column washes with buffers containing 6 to 8 M urea and 1% Triton X-100 or Triton X-114. Extensive on-column rinsing with 8 M urea buffer removes residual detergent and the eluted highly active RTX protein preparations then contain only trace amounts of LPS. The procedure is exemplified using four prototypic RTX cytolysins, the Bordetella pertussis CyaA and the hemolysins of Escherichia coli (HlyA), Kingella kingae (RtxA), and Actinobacillus pleuropneumoniae (ApxIA).
Ondrej Stanek; Jiri Masin; Radim Osicka; David Jurnecka; Adriana Osickova; Peter Sebo. Rapid Purification of Endotoxin-Free RTX Toxins. Toxins 2019, 11, 336 .
AMA StyleOndrej Stanek, Jiri Masin, Radim Osicka, David Jurnecka, Adriana Osickova, Peter Sebo. Rapid Purification of Endotoxin-Free RTX Toxins. Toxins. 2019; 11 (6):336.
Chicago/Turabian StyleOndrej Stanek; Jiri Masin; Radim Osicka; David Jurnecka; Adriana Osickova; Peter Sebo. 2019. "Rapid Purification of Endotoxin-Free RTX Toxins." Toxins 11, no. 6: 336.
The adenylate cyclase toxin-hemolysin (CyaA, ACT or AC-Hly) of pathogenic Bordetellae delivers its adenylyl cyclase (AC) enzyme domain into the cytosol of host cells and catalyzes uncontrolled conversion of cellular ATP to cAMP. In parallel, the toxin forms small cation-selective pores that permeabilize target cell membrane and account for the hemolytic activity of CyaA on erythrocytes. The pore-forming domain of CyaA is predicted to consist of five transmembrane α-helices, of which the helices I, III, IV and V have previously been characterized. We examined here the α-helix II that is predicted to form between residues 529 to 549. Substitution of the glycine 531 residue by a proline selectively reduced the hemolytic capacity but did not affect the AC translocating activity of the CyaA-G531P toxin. In contrast, CyaA toxins with alanine 538 or 546 replaced by diverse residues were selectively impaired in the capacity to translocate the AC domain across cell membrane but remained fully hemolytic. Such toxins, however, formed pores in planar asolectin bilayer membranes with a very low frequency and with at least two different conducting states. The helix-breaking substitution of alanine 538 by a proline residue abolished the voltage-activated increase of membrane activity of CyaA in asolectin bilayers. These results reveal that the predicted α-helix comprising the residues 529 to 549 plays a key role in CyaA penetration into the target plasma membrane and pore-forming activity of the toxin.
Jana Roderova; Adriana Osickova; Anna Sukova; Gabriela Mikusova; Radovan Fiser; Peter Sebo; Radim Osicka; Jiri Masin. Residues 529 to 549 participate in membrane penetration and pore-forming activity of the Bordetella adenylate cyclase toxin. Scientific Reports 2019, 9, 5758 .
AMA StyleJana Roderova, Adriana Osickova, Anna Sukova, Gabriela Mikusova, Radovan Fiser, Peter Sebo, Radim Osicka, Jiri Masin. Residues 529 to 549 participate in membrane penetration and pore-forming activity of the Bordetella adenylate cyclase toxin. Scientific Reports. 2019; 9 (1):5758.
Chicago/Turabian StyleJana Roderova; Adriana Osickova; Anna Sukova; Gabriela Mikusova; Radovan Fiser; Peter Sebo; Radim Osicka; Jiri Masin. 2019. "Residues 529 to 549 participate in membrane penetration and pore-forming activity of the Bordetella adenylate cyclase toxin." Scientific Reports 9, no. 1: 5758.
The adenylate cyclase toxin-hemolysin (CyaA, ACT, or AC-Hly) plays a crucial role in virulence and airway colonization capacity of the whooping cough agent Bordetella pertussis. The toxin penetrates target cell membranes and exhibits three distinct biological activities. A population of CyaA conformers forms small cation-selective pores that permeabilize the cell membrane for potassium efflux, which can provoke colloid-osmotic (oncotic) cell lysis. The other two activities are due to CyaA conformers that transiently form calcium influx conduits in the target cell membrane and translocate the adenylate cyclase (AC) enzyme into cytosol of cells. A fourth putative biological activity has recently been reported; an intrinsic phospholipase A (PLA) activity was claimed to be associated with the CyaA polypeptide and be involved in the mechanism of translocation of the AC enzyme polypeptide across cell membrane lipid bilayer. However, the conclusions drawn by the authors contradicted their own results and we show them to be erroneous. We demonstrate that highly purified CyaA is devoid of any detectable phospholipase A1 activity and that contrary to the published claims, the two putative conserved phospholipase A catalytic residues, namely the Ser606 and Asp1079 residues, are not involved in the process of membrane translocation of the AC domain of CyaA across target membranes.
Ladislav Bumba; Jiri Masin; Adriana Osickova; Radim Osicka; Peter Sebo. Bordetella Pertussis Adenylate Cyclase Toxin Does Not Possess a Phospholipase A Activity; Serine 606 and Aspartate 1079 Residues Are Not Involved in Target Cell Delivery of the Adenylyl Cyclase Enzyme Domain. Toxins 2018, 10, 245 .
AMA StyleLadislav Bumba, Jiri Masin, Adriana Osickova, Radim Osicka, Peter Sebo. Bordetella Pertussis Adenylate Cyclase Toxin Does Not Possess a Phospholipase A Activity; Serine 606 and Aspartate 1079 Residues Are Not Involved in Target Cell Delivery of the Adenylyl Cyclase Enzyme Domain. Toxins. 2018; 10 (6):245.
Chicago/Turabian StyleLadislav Bumba; Jiri Masin; Adriana Osickova; Radim Osicka; Peter Sebo. 2018. "Bordetella Pertussis Adenylate Cyclase Toxin Does Not Possess a Phospholipase A Activity; Serine 606 and Aspartate 1079 Residues Are Not Involved in Target Cell Delivery of the Adenylyl Cyclase Enzyme Domain." Toxins 10, no. 6: 245.
Bordetellae, pathogenic to mammals, produce an immunomodulatory adenylate cyclase toxin–hemolysin (CyaA, ACT or AC-Hly) that enables them to overcome the innate immune defense of the host. CyaA subverts host phagocytic cells by an orchestrated action of its functional domains, where an extremely catalytically active adenylyl cyclase enzyme is delivered into phagocyte cytosol by a pore-forming repeat-in-toxin (RTX) cytolysin moiety. By targeting sentinel cells expressing the complement receptor 3, known as the CD11b/CD18 (αMβ2) integrin, CyaA compromises the bactericidal functions of host phagocytes and supports infection of host airways by Bordetellae. Here, we review the state of knowledge on structural and functional aspects of CyaA toxin action, placing particular emphasis on signaling mechanisms by which the toxin-produced 3′,5′-cyclic adenosine monophosphate (cAMP) subverts the physiology of phagocytic cells.
Jakub Novak; Ondrej Cerny; Adriana Osickova; Irena Linhartova; Jiri Masin; Ladislav Bumba; Peter Sebo; Radim Osicka. Structure–Function Relationships Underlying the Capacity of Bordetella Adenylate Cyclase Toxin to Disarm Host Phagocytes. Toxins 2017, 9, 300 .
AMA StyleJakub Novak, Ondrej Cerny, Adriana Osickova, Irena Linhartova, Jiri Masin, Ladislav Bumba, Peter Sebo, Radim Osicka. Structure–Function Relationships Underlying the Capacity of Bordetella Adenylate Cyclase Toxin to Disarm Host Phagocytes. Toxins. 2017; 9 (10):300.
Chicago/Turabian StyleJakub Novak; Ondrej Cerny; Adriana Osickova; Irena Linhartova; Jiri Masin; Ladislav Bumba; Peter Sebo; Radim Osicka. 2017. "Structure–Function Relationships Underlying the Capacity of Bordetella Adenylate Cyclase Toxin to Disarm Host Phagocytes." Toxins 9, no. 10: 300.
The adenylate cyclase toxin-hemolysin (CyaA, ACT or AC-Hly) translocates its adenylate cyclase (AC) enzyme domain into target cells in a step that depends on membrane cholesterol content. We thus examined what role in toxin activities is played by the five putative cholesterol recognition amino acid consensus (CRAC) motifs predicted in CyaA hemolysin moiety. CRAC-disrupting phenylalanine substitutions had no impact on toxin activities and these were not inhibited by free cholesterol, showing that the putative CRAC motifs are not involved in cholesterol binding. However, helix-breaking proline substitutions in these segments uncovered a structural role of the Y632, Y658, Y725 and Y738 residues in AC domain delivery and pore formation by CyaA. Substitutions of Y940 of the fifth motif, conserved in the acylated domains of related RTX toxins, did not impact on fatty-acylation of CyaA by CyaC and the CyaA-Y940F mutant was intact for toxin activities on erythrocytes and myeloid cells. However, the Y940A or Y940P substitutions disrupted the capacity of CyaA to insert into artificial lipid bilayers or target cell membranes. The aromatic ring of tyrosine 940 side chain thus appears to play a key structural role in molecular interactions that initiate CyaA penetration into target membranes.
Jiri Masin; Jana Roderova; Adriana Osickova; Petr Novak; Ladislav Bumba; Radovan Fiser; Peter Sebo; Radim Osicka. The conserved tyrosine residue 940 plays a key structural role in membrane interaction of Bordetella adenylate cyclase toxin. Scientific Reports 2017, 7, 1 -14.
AMA StyleJiri Masin, Jana Roderova, Adriana Osickova, Petr Novak, Ladislav Bumba, Radovan Fiser, Peter Sebo, Radim Osicka. The conserved tyrosine residue 940 plays a key structural role in membrane interaction of Bordetella adenylate cyclase toxin. Scientific Reports. 2017; 7 (1):1-14.
Chicago/Turabian StyleJiri Masin; Jana Roderova; Adriana Osickova; Petr Novak; Ladislav Bumba; Radovan Fiser; Peter Sebo; Radim Osicka. 2017. "The conserved tyrosine residue 940 plays a key structural role in membrane interaction of Bordetella adenylate cyclase toxin." Scientific Reports 7, no. 1: 1-14.
The whooping cough agent, Bordetella pertussis, secretes an adenylate cyclase toxin-hemolysin (CyaA) that plays a crucial role in host respiratory tract colonization. CyaA targets CR3-expressing cells and disrupts their bactericidal functions by delivering into their cytosol an adenylate cyclase enzyme that converts intracellular ATP to cAMP. In parallel, the hydrophobic domain of CyaA forms cation-selective pores that permeabilize cell membrane. The invasive AC and pore-forming domains of CyaA are linked by a segment that is unique in the RTX cytolysin family. We used mass spectrometry and circular dichroism to show that the linker segment forms α-helical structures that penetrate into lipid bilayer. Replacement of the positively charged arginine residues, proposed to be involved in target membrane destabilization by the linker segment, reduced the capacity of the toxin to translocate the AC domain across cell membrane. Substitutions of negatively charged residues then revealed that two clusters of negative charges within the linker segment control the size and the propensity of CyaA pore formation, thereby restricting the cell-permeabilizing capacity of CyaA. The ‘AC to Hly-linking segment’ thus appears to account for the smaller size and modest cell-permeabilizing capacity of CyaA pores, as compared to typical RTX hemolysins.
Jiri Masin; Adriana Osickova; Anna Sukova; Radovan Fiser; Petr Halada; Ladislav Bumba; Irena Linhartova; Radim Osicka; Peter Sebo. Negatively charged residues of the segment linking the enzyme and cytolysin moieties restrict the membrane-permeabilizing capacity of adenylate cyclase toxin. Scientific Reports 2016, 6, 29137 .
AMA StyleJiri Masin, Adriana Osickova, Anna Sukova, Radovan Fiser, Petr Halada, Ladislav Bumba, Irena Linhartova, Radim Osicka, Peter Sebo. Negatively charged residues of the segment linking the enzyme and cytolysin moieties restrict the membrane-permeabilizing capacity of adenylate cyclase toxin. Scientific Reports. 2016; 6 (1):29137.
Chicago/Turabian StyleJiri Masin; Adriana Osickova; Anna Sukova; Radovan Fiser; Petr Halada; Ladislav Bumba; Irena Linhartova; Radim Osicka; Peter Sebo. 2016. "Negatively charged residues of the segment linking the enzyme and cytolysin moieties restrict the membrane-permeabilizing capacity of adenylate cyclase toxin." Scientific Reports 6, no. 1: 29137.
The adenylate cyclase toxin-hemolysin (CyaA, ACT or AC-Hly) is a key virulence factor of the whooping cough agent Bordetella pertussis. CyaA targets myeloid phagocytes expressing the complement receptor 3 (CR3, known as αMβ2 integrin CD11b/CD18 or Mac-1) and translocates by a poorly understood mechanism directly across the cytoplasmic membrane into cell cytosol of phagocytes an adenylyl cyclase(AC) enzyme. This binds intracellular calmodulin and catalyzes unregulated conversion of cytosolic ATP into cAMP. Among other effects, this yields activation of the tyrosine phosphatase SHP-1, BimEL accumulation and phagocyte apoptosis induction. In parallel, CyaA acts as a cytolysin that forms cation-selective pores in target membranes. Direct penetration of CyaA into the cytosol of professional antigen-presenting cells allows the use of an enzymatically inactive CyaA toxoid as a tool for delivery of passenger antigens into the cytosolic pathway of processing and MHC class I-restricted presentation, which can be exploited for induction of antigen-specific CD8+ cytotoxic T-lymphocyte immune responses.
Jiri Masin; Radim Osicka; Ladislav Bumba; Peter Sebo. Bordetellaadenylate cyclase toxin: a unique combination of a pore-forming moiety with a cell-invading adenylate cyclase enzyme. Pathogens and Disease 2015, 73, ftv075 .
AMA StyleJiri Masin, Radim Osicka, Ladislav Bumba, Peter Sebo. Bordetellaadenylate cyclase toxin: a unique combination of a pore-forming moiety with a cell-invading adenylate cyclase enzyme. Pathogens and Disease. 2015; 73 (8):ftv075.
Chicago/Turabian StyleJiri Masin; Radim Osicka; Ladislav Bumba; Peter Sebo. 2015. "Bordetellaadenylate cyclase toxin: a unique combination of a pore-forming moiety with a cell-invading adenylate cyclase enzyme." Pathogens and Disease 73, no. 8: ftv075.
The aim of this study was to compare two methods for quantification of changes in intracellular potassium concentration (decrease from ∼140 to ∼20mM) due to the action of a pore-forming toxin, the adenylate cyclase toxin (CyaA) from the pathogenic bacterium Bordetella pertussis. CyaA was incubated with stably transfected K1 Chinese hamster ovary cells expressing the toxin receptor CD11b/CD18 and the decrease in potassium concentration in the cells was followed by inductively coupled plasma mass spectrometry (ICP-MS). It is shown that this method is superior in terms of sensitivity, accuracy, and temporal resolution over the method employing the potassium-binding benzofuran isophthalate-acetoxymethyl ester fluorescent indicator. The ICP-MS procedure was found to be a reliable and straightforward analytical approach enabling kinetic studies of CyaA action at physiologically relevant toxin concentrations (<1000ng/ml) in biological microsamples.
Tomas Wald; Inga Petry-Podgorska; Radovan Fiser; Tomas Matousek; Jiri Dedina; Radim Osicka; Peter Sebo; Jiri Masin. Quantification of potassium levels in cells treated with Bordetella adenylate cyclase toxin. Analytical Biochemistry 2014, 450, 57 -62.
AMA StyleTomas Wald, Inga Petry-Podgorska, Radovan Fiser, Tomas Matousek, Jiri Dedina, Radim Osicka, Peter Sebo, Jiri Masin. Quantification of potassium levels in cells treated with Bordetella adenylate cyclase toxin. Analytical Biochemistry. 2014; 450 ():57-62.
Chicago/Turabian StyleTomas Wald; Inga Petry-Podgorska; Radovan Fiser; Tomas Matousek; Jiri Dedina; Radim Osicka; Peter Sebo; Jiri Masin. 2014. "Quantification of potassium levels in cells treated with Bordetella adenylate cyclase toxin." Analytical Biochemistry 450, no. : 57-62.
A large subgroup of the r epeat in t o x in (RTX) family of leukotoxins of Gram-negative pathogens consists of pore-forming hemolysins. These can permeabilize mammalian erythrocytes (RBCs) and provoke their colloid osmotic lysis (hemolytic activity). Recently, ATP leakage through pannexin channels and P2X receptor-mediated opening of cellular calcium and potassium channels were implicated in cell permeabilization by pore-forming toxins. In the study described here, we examined the role played by purinergic signaling in the cytolytic action of two RTX toxins that form pores of different sizes. The cytolytic potency of ApxIA hemolysin of Actinobacillus pleuropneumoniae , which forms pores about 2.4 nm wide, was clearly reduced in the presence of P2X 7 receptor antagonists or an ATP scavenger, such as pyridoxalphosphate-6-azophenyl-2′,4′-disulfonic acid (PPADS), Brilliant Blue G, ATP oxidized sodium salt, or hexokinase. In contrast, antagonists of purinergic signaling had no impact on the hemolytic potency of the adenylate cyclase toxin-hemolysin (CyaA) of Bordetella pertussis , which forms pores of 0.6 to 0.8 nm in diameter. Moreover, the conductance of pores formed by ApxIA increased with the toxin concentration, while the conductance of the CyaA single pore units was constant at various toxin concentrations. However, the P2X 7 receptor antagonist PPADS inhibited in a concentration-dependent manner the exacerbated hemolytic activity of a CyaA-ΔN489 construct (lacking 489 N-terminal residues of CyaA), which exhibited a strongly enhanced pore-forming propensity (>20-fold) and also formed severalfold larger conductance units in planar lipid bilayers than intact CyaA. These results point to a pore size threshold of purinergic amplification involvement in cell permeabilization by pore-forming RTX toxins.
Jiri Masin; Radovan Fiser; Irena Linhartova; Radim Osicka; Ladislav Bumba; Erik L. Hewlett; Roland Benz; Peter Sebo. Differences in Purinergic Amplification of Osmotic Cell Lysis by the Pore-Forming RTX Toxins Bordetella pertussis CyaA and Actinobacillus pleuropneumoniae ApxIA: the Role of Pore Size. Infection and Immunity 2013, 81, 4571 -4582.
AMA StyleJiri Masin, Radovan Fiser, Irena Linhartova, Radim Osicka, Ladislav Bumba, Erik L. Hewlett, Roland Benz, Peter Sebo. Differences in Purinergic Amplification of Osmotic Cell Lysis by the Pore-Forming RTX Toxins Bordetella pertussis CyaA and Actinobacillus pleuropneumoniae ApxIA: the Role of Pore Size. Infection and Immunity. 2013; 81 (12):4571-4582.
Chicago/Turabian StyleJiri Masin; Radovan Fiser; Irena Linhartova; Radim Osicka; Ladislav Bumba; Erik L. Hewlett; Roland Benz; Peter Sebo. 2013. "Differences in Purinergic Amplification of Osmotic Cell Lysis by the Pore-Forming RTX Toxins Bordetella pertussis CyaA and Actinobacillus pleuropneumoniae ApxIA: the Role of Pore Size." Infection and Immunity 81, no. 12: 4571-4582.
K. Ravi Acharya; Martin A. Acquadro; Klaus Aktories; Joseph E. Alouf; Ralf Arnold; Aurélie Babon; Steffen Backert; Matthew D. Baker; Joseph T. Barbieri; Ajit K. Basak; Darrin J. Bast; Stephen J. Billington; Stephanie Bohnert; Patrice Boquet; Gary E. Borodic; Volkmar Braun; Amy E. Bryant; Karen Carniol; Christophe Carnoy; Alexandre Chenal; Ambrose Cole; Didier A. Colin; John Collier; Timothy L. Cover; Mauro Dalla Serra; Joyce C.S. De Azavedo; Kartrin Deinhardt; Ulrich Dobrindt; Jocelyne M. D'souza; Daniel Dubreuil; Susanne C. Feil; Gilles Flateau; Bénédicte Fournier; Augusto A. Franco; Dara W. Frank; John D. Fraser; Joachim Frey; Teresa Frisan; Antoine Galmiche; Michel Gauthier; Kara S. Giddings; Daniel Gillet; Michael S. Gilmore; Werner Goebel; Per Einar Granum; Laure Gurcel; Jörg Hacker; Ralf Hertle; Timothy R. Hirst; Mangfei Ho; Randall K. Holmes; Jan Holmgren; Yasuhiko Horiguchi; Ioan Iacovache; Ken-Ichi Imanishi; Ludger Johannes; Arthur E. Johnson; Eric A. Johnson; B. Helen Jost; Ingo Just; Hidehito Kato; Wolfgang König; Brigitte König; Lizeth Lacharme; Shamez N. Ladhani; Christophe Lamaze; Nadine Lemaitre; Emmanuel Lemichez; Stephen Leppla; Didier Lereclus; George Liu; Camille Locht; Albrecht Ludwig; Jacques Mahillon; Anthony W. Maresso; Vega Masignani; Jiri Masin; Mark McClain; Bruce McClane; Eisuke Mekada; Jody Melton; Gianfranco† Menestrina; André Ménez; Nathalie Michelet; Tim J. Mitchell; Shin-Ichi Miyoshi; Tohru Miyoshi-Akiyama; Jordi Molgo; Henri Monteil; Lionel Mourey; Heide Müller-Alouf; Victor Nizet; Tobias Ölschläger; Sjur Olsnes; Diana Marra Oram; Michael W. Parker; Aurélie Perier; Mariagrazia Pizza; Galina Polekhina; Michel R. Popoff; Bernard Poulain; Gilles Prévost; Thomas Proft; Rino Rappuoli; Julian I. Rood; Jamie Rossjohn; Maha Rupnik; Kowthar Y. Salim; Sara Salinas; Maria Sandkvist; Kirsten Sandvig; Giampetro Schiavo; Mariela Scortti; Maria E. Scott; Cynthia L. Sears; Peter Sebo; Sumio Shinoda; Michel Simonet; Leonard A. Smith; Radek Stachowiak; Dennis L. Stevens; Bradley G. Stiles; Ann-Mari Svennerholm; Julian Tang; Monica Thelestam; Richard W. Titball; Rodney K. Tweten; Takehiko Uchiyama; F. Gisou Van Der Goot; José A. Vásquez-Boland; Jørgen Wesche; Brenda Anne Wilson; Shaoguang Wu. Contributors. The Comprehensive Sourcebook of Bacterial Protein Toxins 2006, 1 .
AMA StyleK. Ravi Acharya, Martin A. Acquadro, Klaus Aktories, Joseph E. Alouf, Ralf Arnold, Aurélie Babon, Steffen Backert, Matthew D. Baker, Joseph T. Barbieri, Ajit K. Basak, Darrin J. Bast, Stephen J. Billington, Stephanie Bohnert, Patrice Boquet, Gary E. Borodic, Volkmar Braun, Amy E. Bryant, Karen Carniol, Christophe Carnoy, Alexandre Chenal, Ambrose Cole, Didier A. Colin, John Collier, Timothy L. Cover, Mauro Dalla Serra, Joyce C.S. De Azavedo, Kartrin Deinhardt, Ulrich Dobrindt, Jocelyne M. D'souza, Daniel Dubreuil, Susanne C. Feil, Gilles Flateau, Bénédicte Fournier, Augusto A. Franco, Dara W. Frank, John D. Fraser, Joachim Frey, Teresa Frisan, Antoine Galmiche, Michel Gauthier, Kara S. Giddings, Daniel Gillet, Michael S. Gilmore, Werner Goebel, Per Einar Granum, Laure Gurcel, Jörg Hacker, Ralf Hertle, Timothy R. Hirst, Mangfei Ho, Randall K. Holmes, Jan Holmgren, Yasuhiko Horiguchi, Ioan Iacovache, Ken-Ichi Imanishi, Ludger Johannes, Arthur E. Johnson, Eric A. Johnson, B. Helen Jost, Ingo Just, Hidehito Kato, Wolfgang König, Brigitte König, Lizeth Lacharme, Shamez N. Ladhani, Christophe Lamaze, Nadine Lemaitre, Emmanuel Lemichez, Stephen Leppla, Didier Lereclus, George Liu, Camille Locht, Albrecht Ludwig, Jacques Mahillon, Anthony W. Maresso, Vega Masignani, Jiri Masin, Mark McClain, Bruce McClane, Eisuke Mekada, Jody Melton, Gianfranco† Menestrina, André Ménez, Nathalie Michelet, Tim J. Mitchell, Shin-Ichi Miyoshi, Tohru Miyoshi-Akiyama, Jordi Molgo, Henri Monteil, Lionel Mourey, Heide Müller-Alouf, Victor Nizet, Tobias Ölschläger, Sjur Olsnes, Diana Marra Oram, Michael W. Parker, Aurélie Perier, Mariagrazia Pizza, Galina Polekhina, Michel R. Popoff, Bernard Poulain, Gilles Prévost, Thomas Proft, Rino Rappuoli, Julian I. Rood, Jamie Rossjohn, Maha Rupnik, Kowthar Y. Salim, Sara Salinas, Maria Sandkvist, Kirsten Sandvig, Giampetro Schiavo, Mariela Scortti, Maria E. Scott, Cynthia L. Sears, Peter Sebo, Sumio Shinoda, Michel Simonet, Leonard A. Smith, Radek Stachowiak, Dennis L. Stevens, Bradley G. Stiles, Ann-Mari Svennerholm, Julian Tang, Monica Thelestam, Richard W. Titball, Rodney K. Tweten, Takehiko Uchiyama, F. Gisou Van Der Goot, José A. Vásquez-Boland, Jørgen Wesche, Brenda Anne Wilson, Shaoguang Wu. Contributors. The Comprehensive Sourcebook of Bacterial Protein Toxins. 2006; ():1.
Chicago/Turabian StyleK. Ravi Acharya; Martin A. Acquadro; Klaus Aktories; Joseph E. Alouf; Ralf Arnold; Aurélie Babon; Steffen Backert; Matthew D. Baker; Joseph T. Barbieri; Ajit K. Basak; Darrin J. Bast; Stephen J. Billington; Stephanie Bohnert; Patrice Boquet; Gary E. Borodic; Volkmar Braun; Amy E. Bryant; Karen Carniol; Christophe Carnoy; Alexandre Chenal; Ambrose Cole; Didier A. Colin; John Collier; Timothy L. Cover; Mauro Dalla Serra; Joyce C.S. De Azavedo; Kartrin Deinhardt; Ulrich Dobrindt; Jocelyne M. D'souza; Daniel Dubreuil; Susanne C. Feil; Gilles Flateau; Bénédicte Fournier; Augusto A. Franco; Dara W. Frank; John D. Fraser; Joachim Frey; Teresa Frisan; Antoine Galmiche; Michel Gauthier; Kara S. Giddings; Daniel Gillet; Michael S. Gilmore; Werner Goebel; Per Einar Granum; Laure Gurcel; Jörg Hacker; Ralf Hertle; Timothy R. Hirst; Mangfei Ho; Randall K. Holmes; Jan Holmgren; Yasuhiko Horiguchi; Ioan Iacovache; Ken-Ichi Imanishi; Ludger Johannes; Arthur E. Johnson; Eric A. Johnson; B. Helen Jost; Ingo Just; Hidehito Kato; Wolfgang König; Brigitte König; Lizeth Lacharme; Shamez N. Ladhani; Christophe Lamaze; Nadine Lemaitre; Emmanuel Lemichez; Stephen Leppla; Didier Lereclus; George Liu; Camille Locht; Albrecht Ludwig; Jacques Mahillon; Anthony W. Maresso; Vega Masignani; Jiri Masin; Mark McClain; Bruce McClane; Eisuke Mekada; Jody Melton; Gianfranco† Menestrina; André Ménez; Nathalie Michelet; Tim J. Mitchell; Shin-Ichi Miyoshi; Tohru Miyoshi-Akiyama; Jordi Molgo; Henri Monteil; Lionel Mourey; Heide Müller-Alouf; Victor Nizet; Tobias Ölschläger; Sjur Olsnes; Diana Marra Oram; Michael W. Parker; Aurélie Perier; Mariagrazia Pizza; Galina Polekhina; Michel R. Popoff; Bernard Poulain; Gilles Prévost; Thomas Proft; Rino Rappuoli; Julian I. Rood; Jamie Rossjohn; Maha Rupnik; Kowthar Y. Salim; Sara Salinas; Maria Sandkvist; Kirsten Sandvig; Giampetro Schiavo; Mariela Scortti; Maria E. Scott; Cynthia L. Sears; Peter Sebo; Sumio Shinoda; Michel Simonet; Leonard A. Smith; Radek Stachowiak; Dennis L. Stevens; Bradley G. Stiles; Ann-Mari Svennerholm; Julian Tang; Monica Thelestam; Richard W. Titball; Rodney K. Tweten; Takehiko Uchiyama; F. Gisou Van Der Goot; José A. Vásquez-Boland; Jørgen Wesche; Brenda Anne Wilson; Shaoguang Wu. 2006. "Contributors." The Comprehensive Sourcebook of Bacterial Protein Toxins , no. : 1.
Jirí Masín; Ivo Konopásek; Jaroslava Svobodová; Peter Sebo. Different structural requirements for adenylate cyclase toxin interactions with erythrocyte and liposome membranes. Biochimica et Biophysica Acta 2004, 1660, 1 .
AMA StyleJirí Masín, Ivo Konopásek, Jaroslava Svobodová, Peter Sebo. Different structural requirements for adenylate cyclase toxin interactions with erythrocyte and liposome membranes. Biochimica et Biophysica Acta. 2004; 1660 (1):1.
Chicago/Turabian StyleJirí Masín; Ivo Konopásek; Jaroslava Svobodová; Peter Sebo. 2004. "Different structural requirements for adenylate cyclase toxin interactions with erythrocyte and liposome membranes." Biochimica et Biophysica Acta 1660, no. 1: 1.