RNDr. David Jurnečka, Ph.D.

Postdoktorand

Publikace

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

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

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

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

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

Rapid Purification of Endotoxin-Free RTX Toxins