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Neisseria gonorrhoeae lipooligosaccharide glycan epitopes recognized by bactericidal IgG antibodies elicited by the meningococcal group B-directed vaccine, MenB-4C
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Neisseria gonorrhoeae lipooligosaccharide glycan epitopes recognized by bactericidal IgG antibodies elicited by the meningococcal group B-directed vaccine, MenB-4C
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Neisseria gonorrhoeae lipooligosaccharide glycan epitopes recognized by bactericidal IgG antibodies elicited by the meningococcal group B-directed vaccine, MenB-4C
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Journal Article
Neisseria gonorrhoeae lipooligosaccharide glycan epitopes recognized by bactericidal IgG antibodies elicited by the meningococcal group B-directed vaccine, MenB-4C
2024
Overview
Outer membrane vesicles (OMVs) of
in the group B-directed vaccine MenB-4C (Bexsero
) protect against infections with
. The immunological basis for protection remains unclear.
OMV vaccines generate human antibodies to
and
lipooligosaccharide (LOS/endotoxin), but the structural specificity of these LOS antibodies is not defined.
Ten paired human sera obtained pre- and post-MenB-4C immunization were used in Western blots to probe
and
LOS. Post-MenB-4C sera (7v5, 19v5, and 17v5), representing individual human variability in LOS recognition, were then used to interrogate structurally defined LOSs of
and
strains and mutants and studied in bactericidal assays.
Post-MenB-4C sera recognized both
and
LOS species, ~10% of total IgG to gonococcal OMV antigens.
and
LOSs were broadly recognized by post-IgG antibodies, but with individual variability for LOS structures. Deep truncation of LOS, specifically a
K mutant without
-,
-, or
-chain glycosylation, eliminated LOS recognition by all post-vaccine sera. Serum 7v5 IgG antibodies recognized the unsialyated L1
-chain, and a 3-PEA-HepII or 6-PEA-HepII was part of the conformational epitope. Replacing the 3-PEA on HepII with a 3-Glc blocked 7v5 IgG antibody recognition of
and
LOSs. Serum 19v5 recognized lactoneotetrose (LNT) or L1 LOS-expressing
or
with a minimal
-chain structure of Gal-Glc-HepI (L8), a 3-PEA-HepII or 6-PEA-HepII was again part of the conformational epitope and a 3-Glc-HepII blocked 19v5 antibody binding. Serum 17v5 LOS antibodies recognized LNT or L1
-chains with a minimal HepI structure of three sugars and no requirement for HepII modifications. These LOS antibodies contributed to the serum bactericidal activity against
. The MenB-4C vaccination elicits bactericidal IgG antibodies to
conformational epitopes involving HepI and HepII glycosylated LOS structures shared between
and
LOS structures should be considered in next-generation gonococcal vaccine design.
