A reference procedure to study chemiluminescence induced in polymorphonuclear leukocytes by Neisseria meningitidis

Fredlund, Hans; Olcén, Per; Danielsson, Dan

doi:10.1111/j.1699-0463.1988.tb00966.x

Cited by 22 publications

(36 citation statements)

References 15 publications

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“…Glycosphingolipids from Human Neutrophils-Neutrophil leukocytes were isolated from pooled outdated human blood from healthy donors (blood group A) by Ficoll-Paque (Pharmacia, Uppsala, Sweden) centrifugation as described by Bøyum (20), with minor modifications (21).…”

Section: Methodsmentioning

confidence: 99%

Carbohydrate Binding Specificity of the Neutrophil-activating Protein of Helicobacter pylori

Teneberg¹,

Miller‐Podraza²,

Lampert³

et al. 1997

Journal of Biological Chemistry

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116

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The possible interaction of the neutrophil-activating protein of Helicobacter pylori with target cell glycoconjugates was investigated by the binding of 125 I-labeled recombinant protein to glycosphingolipids from human neutrophils in solid phase assays. Thereby, a distinct binding of the neutrophil-activating protein to four bands in the acid glycosphingolipid fraction from human neutrophils was detected, whereas no binding to the non-acid glycosphingolipids or polyglycosyl ceramides from these cells was obtained. When using glycosphingolipids not present in the cell membrane of human neutrophils, it was found that the neutrophilactivating protein also bound to sulfated glycosphingolipids as sulfatide and sulfated gangliotetraosyl ceramide. Comparison of the binding preferences of the protein to reference glycosphingolipids from other sources suggested that in human granulocytes, the neutrophil-activating protein of H. pylori preferentially recognizes glycoconjugates with a terminally unsubstituted NeuAc␣3Gal␤4GlcNAc␤3Gal␤4GlcNAc␤ sequence.

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Section: Methodsmentioning

confidence: 99%

Carbohydrate Binding Specificity of the Neutrophil-activating Protein of Helicobacter pylori

Teneberg¹,

Miller‐Podraza²,

Lampert³

et al. 1997

Journal of Biological Chemistry

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116

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“…A pooled normal human serum from 10 healthy blood donors of blood group AB+ Rh+ was used for the studies [14]. This serum (30 ml) was depleted of Clq and factor D by chromatography on Bio-Rex 70 (Mesh size 200-400.…”

Section: Serum Antibodies and Complement Proteins Pooled Norma! Humamentioning

confidence: 99%

“…A Staphylococcus epidermidis strain (strain 1.-9 from our strain collection) was included as a control in each CL experiment as described previously (14). Meningococci were scrogrouped and serotyped by co-agglutination [16].…”

Section: Bacteria Anti Culture Conditionsmentioning

confidence: 99%

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Serum Bactericidal Activity and Induction of Chemiluminescence of Polymorphonuclear Leukocytes: Complement Activation Pathway Requirements in Defense against Neisseria meningitidis

Fredlund

Sjöholm

Selander

et al. 1993

Int Arch Allergy Immunol

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Serum bactericidal activity and chemiluminescence (CL) responses of polymorphonuclear leukocytes (PMNL) to pathogenic Neisseria meningitidis serogroups B and W-135 and to nonpathogenic serogroup 29E were examined with pooled normal human serum depleted of the complement proteins C1q, factor D, properdin and C5. Purified C1q, factor D, properdin and C5 were added alone or in combination. For investigation of serogroup W-135 meningococci, a C1q, factor D and properdin-depleted postvaccination serum with high concentrations of anticapsular antibodies was also used. Serogroup B and W-135 cultured to log phase were resistant to the bactericidal activity of pooled normal human serum but were efficiently killed through the classical pathway alone when the bacteria were cultured to stationary phase. Nonpathogenic serogroup 29E meningococci in log or stationary growth phases were efficiently killed in serum, predominantly through the classical pathway. Serogroup W-135 meningococci grown to log phase were resistant to classical pathway-mediated bactericidal activity in postvaccination serum but were killed on addition of alternative pathway proteins. Stationary phase serogroup W-135 meningococci were killed through both pathways in the postvaccination serum. In the pooled normal human serum CL responses of PMNL were consistently more pronounced with fully reconstituted C1q, factor D, properdin, C5-depleted serum than with serum reconstituted with C1q, factor D and properdin suggesting contribution of actions related to terminal components. In the absence of C1q, serogroup W-135 meningococci in postvaccination serum induced a significant but delayed alternative pathway-mediated CL response. CL responses induced by serum-opsonized meningococci, in contrast to serum bactericidal activity, were not influenced by culture conditions. The findings suggest that phagocytic mechanisms may be of critical importance for resistance to pathogenic meningococci in nonvaccinated adults.

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“…meningitidis is efficiently phagocytosed by polymorphonuclear (PMN) cells (5,8,10), and antibodies specific for group A and C polysaccharides are bactericidal in the presence of peripheral blood polymorphonuclear leukocytes and complement (19). Monocytes can also phagocytose Neisseria species (12,13,16,23).…”

mentioning

confidence: 99%

Opsonophagocytosis of Fluorescent Polystyrene Beads Coupled to Neisseria meningitidis Serogroup A, C, Y, or W135 Polysaccharide Correlates with Serum Bactericidal Activity

Martinez

Pilishvili

Barnard

et al. 2002

Clin Vaccine Immunol

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We developed a polysaccharide-specific flow cytometric opsonophagocytic assay (OPA) for the simultaneous measurement of functional antibody to Neisseria meningitidis serogroups A, C, Y, and W135. OPA titers significantly correlated with serum bactericidal assay titers for all serogroups tested (mean r ‫؍‬ 0.96; P < 0.001). OPA could be used in meningococcal vaccine evaluation.Meningococcal disease continues to be a significant cause of morbidity and mortality in the United States and worldwide (3). The primary mechanism of protection from disease is through antibody-and complement-dependent bactericidal activity (9). Antibodies to capsular polysaccharides of groups A and C of Neisseria meningitidis have been shown to confer protection from meningococcal disease (1,7).N. meningitidis is efficiently phagocytosed by polymorphonuclear (PMN) cells (5,8,10), and antibodies specific for group A and C polysaccharides are bactericidal in the presence of peripheral blood polymorphonuclear leukocytes and complement (19). Monocytes can also phagocytose Neisseria species (12,13,16,23). The relative importance of opsonophagocytic killing as a defense mechanism against N. meningitidis has been previously demonstrated (2,4,18,20,22). Opsonophagocytic assays (OPA) offer several advantages over the standard serum bactericidal assay (SBA). OPA for other pathogens such as Streptococcus pneumoniae have been developed which are semi-automated, use noninfectious targets, provide useful laboratory correlates of protection, and can be multiplexed (14).This report describes a patent-pending multiplexed flow cytometric OPA for measurement of antibody-and complementdependent cell-mediated antimeningococcal activity against serogroups A, C, Y, and W135. Postvaccination sera were collected 1 month after immunization with a quadrivalent meningococcal vaccine (Menomune; Connaught Laboratories, Philadelphia, Pa). Sera from nonimmunized adults (n ϭ 15) and postvaccination adults (n ϭ 12) were obtained through the Emory University Donor Services, Atlanta, Ga., and used as quality controls (15). Sera were stored at Ϫ70°C and heat inactivated at 56°C for 30 min just before being tested, to inactivate endogenous complement activity. We compare this flow OPA technique to a previously standardized SBA (15).(Part of this study was presented at the 11th International Pathogenic Neisseria Conference, Nice, France, 1998.) Homologous capsular polysaccharide from meningococcal serogroups A, C, Y, and W135 (Connaught Laboratories) at a concentration of 1 mg/ml was oxidized by the addition of 218 l of a 0.046 M sodium periodate solution for 30 min, protected from light, at room temperature. The reaction was stopped by the addition of 0.1 ml of glycerol per ml of reaction solution. The polysaccharide solutions were then dialyzed overnight against 0.1 M sodium bicarbonate buffer (pH 8.0).Aliquots (100 l) from the commercial preparation of 1-m-diameter carboxylate-modified FluroSpheres (Molecular Probes, Eugene, Oreg.) were coupled with each oxidized meningoc...

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A reference procedure to study chemiluminescence induced in polymorphonuclear leukocytes by Neisseria meningitidis

Cited by 22 publications

References 15 publications

Carbohydrate Binding Specificity of the Neutrophil-activating Protein of Helicobacter pylori

Carbohydrate Binding Specificity of the Neutrophil-activating Protein of Helicobacter pylori

Serum Bactericidal Activity and Induction of Chemiluminescence of Polymorphonuclear Leukocytes: Complement Activation Pathway Requirements in Defense against <i>Neisseria meningitidi</i><i>s</i>

Opsonophagocytosis of Fluorescent Polystyrene Beads Coupled to Neisseria meningitidis Serogroup A, C, Y, or W135 Polysaccharide Correlates with Serum Bactericidal Activity

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