prof. Ing. Peter Šebo, CSc.

Vedoucí laboratoře

Publication

cAMP signaling of Bordetella adenylate cyclase toxin blocks M-CSF triggered upregulation of iron acquisition receptors on differentiating CD14+ monocytes.

Modification of the RTX domain cap by acyl chains of adapted length rules the formation of functional hemolysin pores.

Deciphering the early innate immune response to bordetella pertussis infection

UNCOVERING THE DIFFERENCES BETWEEN RESPIRATORY PATHOGEN-INDUCED T-CELLS

Delivery of Mycobacterium tuberculosis epitopes by Bordetella pertussis adenylate cyclase toxoid expands HLA-E-restricted cytotoxic CD8+ T cells

Toll-like receptor 4 and CD11b expressed on microglia coordinate eradication of Candida albicans cerebral mycosis

The adenylate cyclase toxin RTX domain follows a series templated folding mechanism with implications for toxin activity

BopN is a Gatekeeper of the Bordetella Type III Secretion System

A conserved tryptophan in the acylated segment of RTX toxins controls their ?inf2/inf integrin–independent cell penetration

A multifaceted role of filamentous hemagglutinin in the virulence of pathogenic bordetella species

Prior exposure to B. pertussis shapes the mucosal antibody response to acellular pertussis booster vaccination

The Fim and FhaB adhesins play a crucial role in nasal cavity infection and Bordetella pertussis transmission in a novel mouse catarrhal infection model

Filamentous Hemagglutinin of Bordetella pertussis Does Not Interact with the ?2 Integrin CD11b/CD18

Pertussis toxin suppresses dendritic cell-mediated delivery of B. pertussis into lung-draining lymph nodes

Modeling the catarrhal stage of Bordetella pertussis upper respiratory tract infections in mice

Selective enhancement of the cell-permeabilizing activity of adenylate cyclase toxin does not increase virulence of bordetella pertussis

Different roles of conserved tyrosine residues of the acylated domains in folding and activity of RTX toxins

Bordetella Adenylate Cyclase Toxin Elicits Airway Mucin Secretion through Activation of the cAMP Response Element Binding Protein

Almost half of the RTX domain is dispensable for complement receptor 3 binding and cell-invasive activity of the Bordetella adenylate cyclase toxin

Bacterial RTX toxins and host immunity

Simultaneous Determination of Antibodies to Pertussis Toxin and Adenylate Cyclase Toxin Improves Serological Diagnosis of Pertussis

Acellular Pertussis Vaccine Inhibits Bordetella pertussis Clearance from the Nasal Mucosa of Mice

Production of Highly Active Recombinant Dermonecrotic Toxin ofBordetella Pertussis

Adenylate Cyclase Toxin Tinkering With Monocyte-Macrophage Differentiation

Continuous Assembly of beta-Roll Structures Is Implicated in the Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins

Acyltransferase-mediated selection of the length of the fatty acyl chain and of the acylation site governs activation of bacterial RTX toxins

Cytotoxicity of the effector protein BteA was attenuated in Bordetella pertussis by insertion of an alanine residue

Retargeting from the CR3 to the LFA-1 receptor uncovers the adenylyl cyclase enzyme?translocating segment ofBordetellaadenylate cyclase toxin

Overcoming Waning Immunity in Pertussis Vaccines: Workshop of the National Institute of Allergy and Infectious Diseases

Negative charge of the AC-to-Hly linking segment modulates calcium-dependent membrane activities of Bordetella adenylate cyclase toxin

Structural Basis of Ca2+-Dependent Self-Processing Activity of Repeat-in-Toxin Proteins

Distinct Spatiotemporal Distribution of Bacterial Toxin-Produced Cellular cAMP Differentially Inhibits Opsonophagocytic Signaling

Bordetella Adenylate Cyclase Toxin Inhibits Monocyte-to-Macrophage Transition and Dedifferentiates Human Alveolar Macrophages into Monocyte-like Cells

Rapid Purification of Endotoxin-Free RTX Toxins

PERISCOPE: road towards effective control of pertussis

Residues 529 to 549 participate in membrane penetration and pore-forming activity of the Bordetella adenylate cyclase toxin