Methods published for the purification of P.II proteins from Neisseria gonorrhoea have been modified to allow the purification of class 5 proteins from Neisseria meningitidis serogroup A bacteria. The five class 5 protein electrophoretic variants detected within an epidemic in the Gambia (a, b, c, d, and e) and three other variants (f, g, and h) found within other isolates of the same clone in West Africa have been purified with yields of 6-28 mg. The NH2-terminal amino acid sequence for variant c differs from those of the other class 5 proteins, whereas the latter are very similar to the sequence predicted for two class 5 proteins from DNA analyses of serogroup C meningococci and determined for 8 P.II proteins from gonococci. Numerous other regulatory, chemical, and serological differences were found between the c protein and the other class 5 proteins such that we recommend that the class 5 proteins be subdivided into two subclasses. mAbs have been isolated that distinguish between these two protein subclasses and Western blotting with these antibodies enabled us to conclude that both protein subclasses were found in bacteria isolated from different epidemics and pandemics of the last 50 yr.
Article|
August 01 1988
Purification and characterization of eight class 5 outer membrane protein variants from a clone of Neisseria meningitidis serogroup A.
M Achtman,
M Achtman
Max-Planck Institut für Molekulare Genetik, Berlin, Federal Republic of Germany.
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M Neibert,
M Neibert
Max-Planck Institut für Molekulare Genetik, Berlin, Federal Republic of Germany.
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B A Crowe,
B A Crowe
Max-Planck Institut für Molekulare Genetik, Berlin, Federal Republic of Germany.
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W Strittmatter,
W Strittmatter
Max-Planck Institut für Molekulare Genetik, Berlin, Federal Republic of Germany.
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B Kusecek,
B Kusecek
Max-Planck Institut für Molekulare Genetik, Berlin, Federal Republic of Germany.
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E Weyse,
E Weyse
Max-Planck Institut für Molekulare Genetik, Berlin, Federal Republic of Germany.
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M J Walsh,
M J Walsh
Max-Planck Institut für Molekulare Genetik, Berlin, Federal Republic of Germany.
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B Slawig,
B Slawig
Max-Planck Institut für Molekulare Genetik, Berlin, Federal Republic of Germany.
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G Morelli,
G Morelli
Max-Planck Institut für Molekulare Genetik, Berlin, Federal Republic of Germany.
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A Moll
A Moll
Max-Planck Institut für Molekulare Genetik, Berlin, Federal Republic of Germany.
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M Achtman
Max-Planck Institut für Molekulare Genetik, Berlin, Federal Republic of Germany.
M Neibert
Max-Planck Institut für Molekulare Genetik, Berlin, Federal Republic of Germany.
B A Crowe
Max-Planck Institut für Molekulare Genetik, Berlin, Federal Republic of Germany.
W Strittmatter
Max-Planck Institut für Molekulare Genetik, Berlin, Federal Republic of Germany.
B Kusecek
Max-Planck Institut für Molekulare Genetik, Berlin, Federal Republic of Germany.
E Weyse
Max-Planck Institut für Molekulare Genetik, Berlin, Federal Republic of Germany.
M J Walsh
Max-Planck Institut für Molekulare Genetik, Berlin, Federal Republic of Germany.
B Slawig
Max-Planck Institut für Molekulare Genetik, Berlin, Federal Republic of Germany.
G Morelli
Max-Planck Institut für Molekulare Genetik, Berlin, Federal Republic of Germany.
A Moll
Max-Planck Institut für Molekulare Genetik, Berlin, Federal Republic of Germany.
Online Issn: 1540-9538
Print Issn: 0022-1007
J Exp Med (1988) 168 (2): 507–525.
Citation
M Achtman, M Neibert, B A Crowe, W Strittmatter, B Kusecek, E Weyse, M J Walsh, B Slawig, G Morelli, A Moll; Purification and characterization of eight class 5 outer membrane protein variants from a clone of Neisseria meningitidis serogroup A.. J Exp Med 1 August 1988; 168 (2): 507–525. doi: https://doi.org/10.1084/jem.168.2.507
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