Cross-reactivity of monoclonal antibodies against lipopolysaccharides of gram-negative bacteria

Jongh-Leuvenink, J. de; Bouter, A. S.; Marcelis, J. H.; Schellekens, J. F. P.; Verhoef, J.

doi:10.1007/bf02013970

Cited by 16 publications

(9 citation statements)

References 23 publications

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“…However, similar to our results, a MAb raised against S . Minnesota Re595 has been reported to bind to both Re‐ and Rb 2 ‐LPSs, but not to other R‐form LPSs [7]. (4) Binding of peptide 45 to S. Enteritidis LPS shows that its binding site is also expressed in this S‐form LPS.…”

Section: Resultsmentioning

confidence: 99%

“…Recent immunochemical studies of R‐LPS have shown that some core oligosaccharides expressed on specific R‐LPS are immunogenic to produce cross‐reactive antibodies. For example, a monoclonal antibody (MAb) raised against Salmonella Re mutant binds both Re‐LPS and Rb 2 ‐LPS [7], which showed not only the presence of a common carbohydrate epitope between the Re and its elongated Rb 2 ‐LPS but also implied the possibility of existence of common epitope(s) among R‐form of LPS.…”

Section: Introductionmentioning

confidence: 99%

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Selection of peptides that bind to the core oligosaccharide of R-form LPS from a phage-displayed heptapeptide library

Noda

Yamasaki

Hironaka

et al. 2001

FEMS Microbiology Letters

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To characterize common sites within the core oligosaccharide of the R-form lipopolysaccharide (LPS), we screened peptides from a phage-displayed heptapeptide library by using the most truncated form of R-LPS, Re-LPS (S. Typhimurium SL1165) as a ligand. After three rounds of biopanning/amplification and subsequent screening by phagemid enzyme-linked immunosorbent assay (ELISA), we selected three distinct clones that bind to the ligand LPS. We characterized the binding sites of the three clones by ELISA and thin-layer chromatography immunostaining and found that the three clones bind the two Re-LPSs (SL1165 and S. Minnesota Re595) and Rb2-LPS. In addition, one of the clones also bound to S-form LPS (S. Enteritidis). Current data show that those clones bind to common carbohydrate structure(s) expressed in the core oligosaccharides of those LPS samples.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Selection of peptides that bind to the core oligosaccharide of R-form LPS from a phage-displayed heptapeptide library

Noda

Yamasaki

Hironaka

et al. 2001

FEMS Microbiology Letters

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“…The polyclonal sera were able to react with all 16 bacteria strains with corresponding results in the three assays. This is not surprising as several Gram-negative bacteria share common antigens (de Jongh-Leuvenink 1986;Bogard et al 1987;Appelmelk et al 1988). Monoclonal antibody 6C11 formed a self-contained group as it reacted strongly with only one wild type strain of S .…”

Section: Discussionmentioning

confidence: 95%

Production and specificity of poly‐ and monoclonal antibodies raised against Shewanella putrefaciens

Fonnesbech¹,

Frøkiær²,

Gram³

et al. 1993

Journal of Applied Bacteriology

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Polyclonal antibodies were raised in rabbits and mice against Shewanella putrefaciens. Murine monoclonal antibodies were produced against the type strain (ATCC 8071) as well as wild type strains isolated from fish products. The specificities of four polyclonal and 12 monoclonal antibodies were tested by dot-blotting, an indirect and a competitive ELISA against 16 Gram-negative strains; including six strains of S. putrefaciens and one strain of Pseudomonas rubescens (NC 10695). All polyclonal antibodies reacted strongly with S. putrefaciens and with Ps. rubescens and cross-reacted with the nine other bacteria (Pseudomonas spp., Aeromonas spp. and Vibrio anguillarum). The monoclonal antibodies could be divided into three groups with different patterns of specificity. The largest group (8 monoclonal antibodies) reacted strongly with S. putrefaciens and with Ps. rubescens and showed only weak reactions with the other strains. The results confirm that Ps. rubescens should be classified as S. putrefaciens.

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“…With the help of monoclonal antibodies (MAb) reactive with different antigenic determinants, it may then be possible to define the epitope that has the capacity to induce cross-protective antibodies in animals and humans. We have produced several MAb against the R mutants E. coli J5 and Salmonella typhimurium (5). These antibodies were characterized in this study and may, in the future, help to compare the reactivity and specificity of protective and nonprotective MAb.…”

mentioning

confidence: 99%

“…MAb. MAb 4-7B5 (immunoglobulin M [IgM]), MAb 4-9A1 (IgG3), and MAb 4-6A1 (IgGl) against E. coli J5 LPS and anti-Re LPS MAb 8-2C1 (IgM) were obtained as described previously (5). The specific anti-J5 LPS MAb BA7 (IgG3) was a gift of B. J. Appelmelk (Free University of Amsterdam, The Netherlands).…”

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confidence: 99%

Characterization of anti-core glycolipid monoclonal antibodies with chemically defined lipopolysaccharides

1990

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Five anti-core glycolipid monoclonal antibodies (MAb) (four against Escherichia coli J5 lipopolysaccharide [LPS] and one against the Re core glycolipid of Salmonella typhimurium) were characterized using LPS from several rough and smooth strains and derivatives of E. coli J5 LPS, obtained by N acetylation and hydrolysis.The MAb against E. coli J5 were not or only weakly cross-reactive with clinical isolates, whereas the anti-Re MAb was highly cross-reactive. The MAb differed in their reaction pattern with E. coli J5 LPS. MAb 4-7B5 (immunoglobulin M) and MAb 4-6A1 (immunoglobulin Gl) cross-reacted with LPS of Salmonella minnesota R5 and S. typhimurium Ra and Rc and little with Re and lipid A. The dominant binding site of these MAb was located in the glucose-heptose-heptose region and was independent of phosphate substitution. The MAb 4-9A1 reacted with the terminal part of the core region (glucose-heptose) and was dependent on phosphate substitution of the LPS. The MAb BA7 (immunoglobulin G3) was E. coli J5 LPS specific and reacted with the glucosaminyl-heptose disaccharide. Antibody 8-2C1 was directed against the common parts of LPS, 3deoxy-D-manno-octulosonic acid, and lipid A, which are not (or only weakly) recognized by the four anti-J5 LPS MAb. Thus, MAb that are not cross-reactive can be directed against at least three different antigenic determinants present on the core oligosaccharide of E. coli J5 LPS. * Corresponding author. 421MATERIALS AND METHODS Bacteria, LPS isolation, and chemical modifications of E. coli J5 LPS. Serratia marcescens, Enterobacter cloacae, Klebsiella pneumoniae, Pseudomonas aeruginosa, E. coli 0135K+, Proteus mirabilis, and Morganella morganii were isolated from the blood of patients with septic shock caused by gram-negative bacteria. Bacteria were grown on Isosensitest agar (Oxoid, United Kingdom) plates (18 h, 37°C). After harvesting, they were washed twice with phosphatebuffered saline (PBS) and heat killed in PBS for 1 h at 100°C.LPS. LPS of the R strains S. minnesota R5 (RcP-), E. coli J5 (RcP+), and S. typhimurium Ra, Rc (RcP+), and Re were isolated as described previously (7,8). They were dissolved in distilled water (5 mg/ml), ultrasonicated (5 min), adjusted to pH 7 with triethylamine, and kept at -20°C. Lipid A, obtained from H. Brade, was isolated from the E. coli Re mutant strain F515 by acetate buffer hydrolysis (0.1 M, pH 4.4, 1 h, 100°C) (4). Hydrolysis of E. coli J5 LPS. Sequential hydrolysis of LPS (20 mg/ml) was started with 20 mM acetate buffer (pH 4.4) for 3 h at 70°C. After dialysis against distilled water, dialysate 1 was concentrated by evaporation, and the remainder was further hydrolyzed with 0.1 M acetate buffer (pH 4.4) for 1 h at 100°C. After dialysis, dialysate 2 was obtained as described above. A part of the remainder (65%) was further hydrolyzed with 0.1 M HCl for 1 h at 100°C. The other 35% was termed J5 LPS-ACB (yield, 78%). Dialysate 3 was obtained as described above after 0.1 M HCl hydrolysis. This remainder was termed J5 LPS-HCI (yield, 31.4%).Af...

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Cross-reactivity of monoclonal antibodies against lipopolysaccharides of gram-negative bacteria

Cited by 16 publications

References 23 publications

Selection of peptides that bind to the core oligosaccharide of R-form LPS from a phage-displayed heptapeptide library

Selection of peptides that bind to the core oligosaccharide of R-form LPS from a phage-displayed heptapeptide library

Production and specificity of poly‐ and monoclonal antibodies raised against Shewanella putrefaciens

Characterization of anti-core glycolipid monoclonal antibodies with chemically defined lipopolysaccharides

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