Structure and immunochemistry of meningococcal lipopolysaccharides

Jennings, Harold J.; Beurret, Michel; Gamian, Andrzej; Michon, Francis

doi:10.1007/bf00415511

Cited by 45 publications

(32 citation statements)

References 11 publications

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“…Jennings and co-workers used nuclear magnetic resonance to study acid-released OS of LOS and reported that the terminal tetrasaccharide of the nonreducing end of the LOS of an L2 strain (17,26), an L3, 7, 9 strain (29), and an L5 strain (42) is composed of lacto-N-neotetraose (Gal1-4GlcNAcP1-, 3GalP1--4Glc). Also consistent with this structure are a common structure deduced by fast-atom-bombardment spectrometry analysis of acid-released OS of meningococcal strains 891 (L4) and M981 (L5) (10) and part of the preliminary structure described for the L3 LOS in this study (Fig.…”

Section: Resultsmentioning

confidence: 99%

Endogenous sialylation of the lipooligosaccharides of Neisseria meningitidis

et al. 1991

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Monoclonal antibodies (MAb) 3F11 and 06B4 recognize epitopes that are conserved on gonococcal lipooligosaccharides (LOS), present on some meningococcal LOS, and conserved on human erythrocytes. LOS of some group B and C prototype meningococcal LOS strains (LOS serotypes Ll to L8) treated with neuraminidase showed increased expression of the 3F11 and 06B4 MAb-defined epitopes. Neuraminidasetreated LOS separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and silver stained showed a shift in migration from a component with a mass of approximately 4.8 kDa to a component with a mass of between 4.5 and 4.6 kDa. The same strains grown in medium with excess CMP-N-acetylneuraminic acid had LOS that shifted in migration to a slightly higher component (mass, approximately 4.8 kDa). Chemical analysis of the neuraminidase-digested products from one LOS indicated it contained approximately 1.5% sialic acid. Covalent linkage between sialic acid and the LOS was confirmed by analysis of de-O-acylated and dephosphorylated LOS by liquid secondary ion mass spectrometry. These studies show that some meningococci contain sialic acid in their LOS, that the sialic acid is cleaved and lost in conventional acetic acid hydrolysis, and that the sialic acid alters the expression of MAb-defined epitopes. Recent studies have shown that when gonococci are grown in the presence of CMP-N-acetylneuraminic acid (CMP-NANA), sialic acid is incorporated into the LOS component of 4.5 kDa that binds MAbs 3F11 and 06B4 (36, 44). The sialylated component no longer binds the MAbs (4, 36). Treatment of the LOS with neuraminidase restores these epitopes, both on organisms grown in vitro (36) and on organisms in vivo in urethral exudates (4). Although the 3F11 and 06B4 epitopes are of similar specificity and are both expressed on gonococcal LOS (37), the 06B4 epitope is expressed much better than is the 3F11 epitope on meningococcal LOS of group B and C strains (30, 35 Bacterial strains. The prototype group B and C meningococcal LOS strains (38, 62) have been described previously. The surface glycolipids (lipooligosaccharides [LOS]) of

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Section: Resultsmentioning

confidence: 99%

Endogenous sialylation of the lipooligosaccharides of Neisseria meningitidis

et al. 1991

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“…Structural Similarities between LOS and Blood Group Antigens. Jennings and colleagues (7)(8)(9) have reported the structure of three meningococcal strains of different LOS serotype ( Table 1). LNnT (GalOl-4G1cNAca1-3Ga1(31-4Glc) is the nonreducing terminus of the oligosaccharides of each of these strains (7)(8)(9).…”

Section: Resultsmentioning

confidence: 99%

“…Jennings and colleagues (7)(8)(9) have reported the structure of three meningococcal strains of different LOS serotype ( Table 1). LNnT (GalOl-4G1cNAca1-3Ga1(31-4Glc) is the nonreducing terminus of the oligosaccharides of each of these strains (7)(8)(9). Since LNnT is also the terminal tetrasaccharide of the major blood group antigen precursor, nLc4Cer (Table I), this structural similarity led us to test for immunochemical similarity between human cells and LOS.…”

Section: Resultsmentioning

confidence: 99%

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.

Mandrell

Griffiss

Macher

1988

The Journal of Experimental Medicine

253

167

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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.

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“…A variety of biochemical and biophysical techniques have been used for LOS structural determination: these include methylation analysis, specific degradations (e.g., mild acid hydrolysis) and high-pH anion-exchange chromatography of underivatised oligosaccharides with reverse-phase high performance liquid chromatography; pulsed amperometric detection (HPAE-PAD) of oligosaccharides (OS), fluorophore-assisted carbohydrate electrophoresis monosaccharide composition analysis; 1D 500-MHz 1 H-NMR as well as nuclear Overhauser effect experiments; 2D NMR methods [double quantum filtered COSY (DQF-COSY), delayed COSY (D-COSY), homonuclear Hartmann-Hahn spectroscopy (HOHAHA) and pure-absorption 2D NOE NMR]; mass spectrometry techniques (positive ion fast atom bombardment; Fourier transform ion cyclotron resonance mass spectrometry (FTICR-MS); electrospray ionization, collision-induced dissociation, and multiple step) [164,165,166,167,168,169,170,171,172,173,174]. Structural information on LOS has been recorded for meningococci [168,172,174,175,176,177], gonococci [178,179] and several commensals ( N. canis , N. perflava , N. subflava , N. flava , N. cinerea , N. flavescens , N. caviae , N. sicca ) [180,181,182]. …”

Section: Neisseria Surface Structures Involved In Adhesionmentioning

confidence: 99%

The Biology of Neisseria Adhesins

Hung

Christodoulides

2013

Biology

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Members of the genus Neisseria include pathogens causing important human diseases such as meningitis, septicaemia, gonorrhoea and pelvic inflammatory disease syndrome. Neisseriae are found on the exposed epithelia of the upper respiratory tract and the urogenital tract. Colonisation of these exposed epithelia is dependent on a repertoire of diverse bacterial molecules, extending not only from the surface of the bacteria but also found within the outer membrane. During invasive disease, pathogenic Neisseriae also interact with immune effector cells, vascular endothelia and the meninges. Neisseria adhesion involves the interplay of these multiple surface factors and in this review we discuss the structure and function of these important molecules and the nature of the host cell receptors and mechanisms involved in their recognition. We also describe the current status for recently identified Neisseria adhesins. Understanding the biology of Neisseria adhesins has an impact not only on the development of new vaccines but also in revealing fundamental knowledge about human biology.

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Structure and immunochemistry of meningococcal lipopolysaccharides

Cited by 45 publications

References 11 publications

Endogenous sialylation of the lipooligosaccharides of Neisseria meningitidis

Endogenous sialylation of the lipooligosaccharides of Neisseria meningitidis

The Biology of Neisseria Adhesins

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