H. Lomholt et M. Kilian, ANTIGENIC RELATIONSHIPS AMONG IMMUNOGLOBULIN A1 PROTEASES FROM HAEMOPHILUS, NEISSERIA, AND STREPTOCOCCUS SPECIES, Infection and immunity, 62(8), 1994, pp. 3178-3183
To investigate the antigenic variation and relationships of immunoglob
ulin Al (IgA1) proteases among different species and genera, we examin
ed a comprehensive collection of serine type and metallo-type IgA1 pro
teases and corresponding antisera in enzyme neutralization assays. Sha
ring of neutralizing epitopes of metallo-type IgA1 proteases from Stre
ptococcus pneumoniae, Streptococcus sanguis, Streptococcus mitis, and
Streptococcus oralis and of serine type IgA1 proteases from Haemophilu
s and pathogenic Neisseria species was extremely limited. A number of
limited to strong cross-reactions in such epitopes were found among se
rine type IgA1 proteases released by members of the genera Haemophilus
and Neisseria, reflecting the common origin of their iga gene. Howeve
r, the relatively limited prevalence of shared ''neutralizing'' epitop
es of IgA1 proteases from the two genera indicates that they rarely in
duce immunity to each other. In contrast, extensive sharing of neutral
izing epitopes was found between N. meningitidis and N. gonorrhoeae Ig
A1 proteases, making them potentially attractive vaccine components. A
mong metallo-type IgA1 proteases, several pneumococcal proteases were
found to induce neutralizing antibodies to IgA1 proteases of oral stre
ptococci whereas the opposite was not the case.