EFFECT OF SIALYLATION OF LIPOPOLYSACCHARIDE OF NEISSERIA-GONORRHOEAE ON RECOGNITION AND COMPLEMENT-MEDIATED KILLING BY MONOCLONAL-ANTIBODIES DIRECTED AGAINST DIFFERENT OUTER-MEMBRANE ANTIGENS
H. Delapaz et al., EFFECT OF SIALYLATION OF LIPOPOLYSACCHARIDE OF NEISSERIA-GONORRHOEAE ON RECOGNITION AND COMPLEMENT-MEDIATED KILLING BY MONOCLONAL-ANTIBODIES DIRECTED AGAINST DIFFERENT OUTER-MEMBRANE ANTIGENS, Microbiology, 141, 1995, pp. 913-920
Growth of gonococci in the presence of CMP-N-acetylneuraminic acid (CM
P-NANA) has previously been shown to induce resistance to the bacteric
idal effect of normal human serum and is accompanied by sialylation of
the gonococcal lipopolysaccharide (LPS). We have used monoclonal anti
bodies (mAbs) to compare the effect of LPS sialylation on recognition
of gonococci and complement-mediated killing by antibodies directed ei
ther against LPS or against defined epitopes on outer-membrane protein
PI, Despite differences in binding to sialylated LPS on Western blots
, all three mAbs directed against LPS showed considerably reduced bind
ing to gonococci grown in the presence of CMP-NANA and a concomitant r
eduction in ability to promote complement-mediated killing, In contras
t, mAbs directed against previously defined epitopes on a surface expo
sed loop of PI showed little difference in binding between sialylated
and non-sialylated gonococci and promoted killing of the sialylated go
nococci, Similarly a mAb directed against an epitope on a loop of the
outer-membrane Rmp protein, which had previously been shown to block k
illing by antibodies directed against other surface antigens, also exe
rted a blocking effect with sialylated gonococci, Thus in the present
study the continued biological effect of mAbs was correlated with the
ability of the antibody to recognize surface-exposed epitopes on sialy
lated gonococci, Despite the presence of the sialylation which is like
ly to occur in vivo, it should be possible to induce complement-mediat
ed killing by focusing the immune response to those surface-exposed ep
itopes which are least susceptible to the potential inhibitory effect
of LPS sialylation.