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Immunogenicity and evolutionary variability of epitopes within IgA1 protease from serogroup A Neisseria meningitidis
Authors:Giovanna Morelli,Jesus del,Valle, Claudia J. Lammel,Johannes Pohlner,Kerstin Mü  ller,Milan Blake,Geo. F. Brooks,Thomas F. Meyer,Brehima Koumaré  ,Norbert Brieske,Mark Achtman
Affiliation:Max-Planck Institut für molekulare Genetik, Ihnestrasse 73, D-14195 Berlin, Germany.;Department of Laboratory Medicine, University of California, San Francisco, California, USA.;3Max-Planck Institut fur Biologie, Abteilung Infektionsbiologie, Spemannstrasse 34, D-72076 Tubingen, Germany.;Laboratory of Bacteriology and Immunology, The Rockefeller University, New York, New York, USA.;Institut Nationale de Recherche en SantéPublique, Bamako, Mali
Abstract:Five murine epitopes were defined and mapped within IgA1 protease produced by Neisseria meningitidis. Epitopes 1 and 2 were present in IgA1 protease from all strains, and from Neisseria gonorrhoeae. Epitopes 3 through to 5 varied between subgroups of serogroup A meningococci. but have remained constant over decades within the subgroups, except for epitope 4, which changed between 1983 and 1987 during the spread of subgroup III meningococci from Asia to Africa. Binding of monoclonal antibodies to epitopes 1, 4 and 5 neutralized enzymatic function. Human sera containing antibodies to lgA1 protease as a result of natural infection inhibited binding of monoclonal antibodies to epitope 4 but not to the other epitopes.
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