Lipooligosaccharides: The Principal Glycolipids of the Neisserial Outer Membrane

Griffiss, J M; Schneider, Herman; Mandrell, Robert E.; Yamasaki, Ryohei; Jarvis, Gary A.; Kim, J J; Gibson, Brad; Hamadeh, R M; Apicella, M A

doi:10.1093/cid/10.supplement_2.s287

Cited by 113 publications

(71 citation statements)

References 31 publications

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“…These occur commonly in non-enteric Gram-negative bacteria, such as those that colonise the mucosal surfaces of the upper respiratory tract [39]. The LOS of M. catarrhalis consists of lipid A plus a core polysaccharide and one oligosaccharide [40].…”

Section: Discussionmentioning

confidence: 99%

The IgD-binding domain of the Moraxella IgD-binding protein MID (MID962-1200) activates human B cells in the presence of T cell cytokines

Nordström

Jendholm

Samuelsson

et al. 2005

Journal of Leukocyte Biology

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Moraxella catarrhalis immunoglobulin D (IgD)‐binding protein (MID) is an outer membrane protein with specific affinity for soluble and cell‐bound human IgD. Here, we demonstrate that mutated M. catarrhalis strains devoid of MID show a 75% decreased activation of human B cells as compared with wild‐type bacteria. In contrast to MID‐expressing Moraxella, the MID‐deficient Moraxella mutants did not bind to human CD19+ IgD+ B cells. The smallest MID fragment with preserved IgD‐binding capacity comprises 238 amino acids (MID962‐1200). To prove the specificity of MID962‐1200 for IgD, a Chinese hamster ovary (CHO) cell line expressing membrane‐anchored human IgD was manufactured. MID962‐1200 bound strongly to the recombinant IgD on CHO cells. Moreover, MID962‐1200 stimulated peripheral blood lymphocyte (PBL) proliferation 5‐ and 15‐fold at 0.1 and 1.0 μg/ml, respectively. This activation could be blocked completely by antibodies directed against the CD40 ligand (CD154). MID962‐1200 also activated purified B cells in the presence of interleukin (IL)‐2 or IL‐4. An increased IL‐6 production was seen after stimulation with MID962‐1200, as revealed by a human cytokine protein array. MID962‐1200 fused to green fluorescent protein (GFP) bound to human B cells and activated PBL to the same degree as MID962‐1200. Taken together, MID is the only IgD‐binding protein in Moraxella. Furthermore, the novel T cell‐independent antigen MID962‐1200 may, together with MID962‐1200–GFP, be considered as promising reagents in the study of IgD‐dependent B cell activation.

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Section: Discussionmentioning

confidence: 99%

The IgD-binding domain of the Moraxella IgD-binding protein MID (MID962-1200) activates human B cells in the presence of T cell cytokines

Nordström

Jendholm

Samuelsson

et al. 2005

Journal of Leukocyte Biology

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“…The molecular mass of meningococcal LPS varies within certain limits (3.2-7.1 kD) owing to heterogeneity in size of the carbohydrate chain depending on strain, i.e., immunotype, and to microheterogeneity ofthe LPS related to growth conditions (51)(52)(53). For calculations in this study, we have chosen a molecular mass of 5.0 kD.…”

Section: Introductionmentioning

confidence: 99%

Meningococcal endotoxin in lethal septic shock plasma studied by gas chromatography, mass-spectrometry, ultracentrifugation, and electron microscopy.

Brandtzæg

Bryn²,

Kierulf³

et al. 1992

J. Clin. Invest.

129

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We have compared gas chromatography and mass spectrometry (GC-MS) analysis with the Limulus amebocyte lysate (LAL) assay to quantify native meningococcal lipopolysaccharides (LPS) in five patient plasmas containing > 5 ,gg/liter by LAL. 3-Hydroxy launric acid (3-OH-12:0) was used as a specific lipid A marker of neisserial LPS. The quantitative LAL results were confirmed by GC-MS (r = 0.98, P = 0.006). Seven patient plasmas were centrifuged at 103,000 g and the sedimentation behavior of native LPS compared with reference plasma proteins and with apo Al and apo B100 representing high and low density lipoproteins. After 15 min ofcentrifugation, 84±2% (mean±SE) of the recovered LPS were found in the lower onethird of the centrifuged volume, whereas 6±1% remained in the upper one-third volume, indicating that meningococcal endotoxin circulates as complexes with high sedimentation coefficients. Bacterial outer membrane fragments were detected in the bottom fractions of three patient plasmas examined by means of electron microscopy. In three patient plasmas ultracentrifuged for 60 min at 103,000 g, the levels of apo Al and apo B100 revealed minor changes, whereas only 1±1% of the recovered LPS remained in the upper one-third and 91±2% were found in the lower one-third volume. Few bioreactive LPS appear to be complexed with high and low density lipoproteins in meningococcal septic shock plasma. (J. Clin. Invest. 1992.

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“…The surface glycolipids (lipooligosaccharides [LOS]) of Neisseria gonorrhoeae and Neisseria meninigitidis are composed of multiple components that are antigenically and chemically distinct (21,37). Many gonococcal and meningococcal strains contain LOS that bind monoclonal antibodies (MAbs) 3F11 and 06B4, usually to a 4.5-kDa LOS component.…”

mentioning

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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Lipooligosaccharides: The Principal Glycolipids of the Neisserial Outer Membrane

Cited by 113 publications

References 31 publications

The IgD-binding domain of the Moraxella IgD-binding protein MID (MID962-1200) activates human B cells in the presence of T cell cytokines

The IgD-binding domain of the Moraxella IgD-binding protein MID (MID962-1200) activates human B cells in the presence of T cell cytokines

Meningococcal endotoxin in lethal septic shock plasma studied by gas chromatography, mass-spectrometry, ultracentrifugation, and electron microscopy.

Endogenous sialylation of the lipooligosaccharides of Neisseria meningitidis

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