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Immunogenicity and evolutionary variability of epitopes within IgA1 protease from serogroup A Neisseria meningitidis
Author(s) -
Morelli Giovanna,
Valle Jesus,
Lammel Claudia J.,
Pohlner Johannes,
Müller Kerstin,
Blake Milan,
Brooks Geo. F.,
Meyer Thomas F.,
Koumaré Brehima,
Brieske Norbert,
Achtman Mark
Publication year - 1994
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1994.tb00299.x
Subject(s) - epitope , neisseria meningitidis , immunogenicity , biology , virology , monoclonal antibody , neisseria , protease , microbiology and biotechnology , epitope mapping , antibody , neisseria gonorrhoeae , enzyme , immunology , bacteria , genetics , biochemistry
Summary 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.