Lipooligosaccharides (LOS) of Neisseria gonorrhoeae and Neisseria meningitidis have components that are immunochemically similar to precursors of human blood group antigens. Carbohydrate sequence specificity of the mouse monoclonal antibodies that recognize crossreacting antigens on LOS and human erythrocytes.

Abstract

We have used mouse mAbs, 3F11 and 06B4, that are specific for highly conserved epitopes of Neisseria gonorrhoeae lipooligosaccharides (LOS) to identify immunochemically similar structures on human erythrocytes. mAb 3F11 agglutinated erythrocytes from all randomly selected adult humans, while mAb 06B4 agglutinated only 80% of the same specimens. The antibodies had an activity with erythrocytes similar to human cold agglutinins in that agglutination occurred at 4 degrees C and decreased with increasing incubation temperature. Human infant erythrocytes were agglutinated less well, but enzymatic treatment of either infant or adult cells resulted in an increase in expression of the 3F11- and 06B4-defined epitopes. Both antibodies bound to a series of neutral glycosphingolipids from human erythrocytes and neutrophils that have a type 2 (Gal beta 1----4GlcNAc) or N-acetyllactosamine structure. Neither antibody bound to glycosphingolipids from human meconium, which have a type 1 (Gal beta 1----3GlcNAc) structure. The antibodies were unable to bind to N-acetyl-lactosamine glycosphingolipids with a nonreducing terminal sialic acid or a Gala1----3Gal disaccharide. Antibody binding also was blocked by the presence of fucose linked to the penultimate glucosamine residue of N-acetyllactosamine glycosphingolipids. Although both antibodies bound to linear and branched-chain N-acetyllactosamine glycosphingolipids, 3F11 had a higher affinity for branched structures than did 06B4. The activity of 3F11 with human adult and infant treated and untreated erythrocytes with N-acetyllactosamine glycosphingolipids, and with LOS was very similar, if not identical, in specificity to 1B2, an mAb prepared from mice inoculated with a linear N-acetyllactosamine glycosphingolipid.

Identification of Novel Glycosyltransferases Required for Assembly of the Pasteurella multocida A:1 Lipopolysaccharide and Their Involvement in Virulence

“…which mimics paragloboside and other glycosphingolipids expressed in mammalian tissues (22,23). The glycosyltransferases required for the assembly of this trisaccharide in H. influenzae were identified when genes from the lsg locus were expressed in E. coli (24).…”

Endogenous sialylation of the lipooligosaccharides of Neisseria meningitidis

“…Many gonococcal and meningococcal strains contain LOS that bind monoclonal antibodies (MAbs) 3F11 and 06B4, usually to a 4.5-kDa LOS component. The shared epitopes defined by MAbs 3F11 and 06B4 (35) are conserved on gonococcal LOS (3,4,37) but variably expressed on LOS of meningococci (31, 35), Neisseria lactamica (30), and Haemophilus ducreyi (9). These MAbs also have been used to show that certain LOS components are immunochemically similar to molecules present in human erythrocytes and in other human cells (35).…”

Expression of sialic acid and polysialic acid in serogroup B Neisseria meningitidis: divergent transcription of biosynthesis and transport operons through a common promoter region

“…Sialic acid is also expressed in group B meningococci as N-acetylneuraminic acid (NANA), which is added to the terminal galactose of the lipooligosaccharide (LOS) ␣-chain paragloboside (30,31). The (␣2 3 3) linkage of NANA to LOS (52) is accomplished by an as-yet-undefined LOS sialyltransferase pathway which utilizes endogenous or exogenous CMP-NANA as the sialic acid substrate (32,34).…”