Neutralizing monoclonal antibodies against listeriolysin: mapping of epitopes involved in pore formation.
Six different mouse monoclonal antibodies (MAbs) and a specific rabbit polygonal antibody were raised against listeriolysin. Four of the MAbs also recognized seeligeriolysin, and five cross-reacted with ivanolysin. The hemolytic activity could be neutralized by the polygonal antibody as well as by five of the MAbs. None of the neutralizing antibodies interfered with the binding of listeriolysin to the cellular membrane. The epitopes recognized by the MAbs were localized by using overlapping synthetic peptides between positions 59 and 279, a region hitherto not implicated in mediating hemolytic activity.
Darji
A
A
Department of Cell Biology and Immunology, National Research Centre for Biotechnology, Braunschweig, Germany.
Niebuhr
K
K
Hense
M
M
Wehland
J
J
Chakraborty
T
T
Weiss
S
S
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D001427:Bacterial Toxins; D018604:Epitope Mapping; D006360:Heat-Shock Proteins / Q000276:immunology* / Q000633:toxicity; D006460:Hemolysin Proteins / Q000276:immunology*; D006461:Hemolysis; D051379:Mice; D008969:Molecular Sequence Data; D011817:Rabbits
D000911:Antibodies, Monoclonal; D001427:Bacterial Toxins; D006360:Heat-Shock Proteins; D006460:Hemolysin Proteins; C038705:hlyA protein, Listeria monocytogenes