Protective efficacy of IgA monoclonal antibodies to O and H antigens in a mouse model of intranasal challenge with Salmonella enterica serotype Enteritidis.

Protective properties of immunoglobulin A (IgA) monoclonal antibodies (MAbs) directed against O and H antigens of Salmonella enterica serotype Enteritidis (S. enteritidis) were evaluated in a model of generalized infection after intranasal (i.n.

Bacterial lipopolysaccharide induces proliferation of IL-6-dependent plasmacytoma cells by MAPK pathway activation.

Mouse plasmacytomas are appropriate models to study the biology of human multiple myeloma (MM). Growth of murine interleukin-6 (IL-6)-dependent hybridoma/plasmacytoma lines can be stimulated by bacterial lipopolysaccharides (LPS). However, the molecular mechanisms of this phenomenon are still not elucidated.

Monoclonal antibody against O:5 Salmonella antigen cross-reacts with unidentified lipopolysaccharide epitope of Salmonella serogroup O:8 (C(2)-C(3)).

Monoclonal antibody (MAb) 8aC10 against Salmonella O:5 antigen was obtained after immunization of BALB/c mice with live attenuated mutant of Salmonella typhimurium. Antigen specificity of the MAb was characterized by ELISA, immunoblotting, passive hemagglutination (PHA), passive hemolysis and agglutination tests. In ELISA, PHA and immunoblotting the MAb reacted only with lipopolysaccharides (LPS) of Salmonella strains from group O:4 (B), expressing O:5 antigen.

Cross-reactive monoclonal antibodies raised against the lipopolysaccharide antigen of Salmonella minnesota Re chemotype: diagnostic relevance.

Three cross-reactive monoclonal antibodies (MAbs) of IgM and IgG2b isotype were generated in two separate fusions after immunization of BALB/c mice with heat killed Salmonella minnesota R595 of Re chemotype and acid-treated bacteria, coated with Re lipopolysaccharide (LPS) antigen. The specificity of the MAbs was demonstrated as the Re LPS antigen. The activity and cross-reactivity against purified elementary bodies of Chlamydia trachomatis and various S- and R-LPS antigens of other Gram-negative bacteria were characterized in enzyme-linked immunosorbent assay, passive hemolysis assay, immunoblot and immunofluorescence with the available chlamydial strains.

Production and characterization of monoclonal immunoglobulin A antibodies directed against Salmonella H:g,m flagellar antigen.

Hybridomas were generated after intragastral immunization of BALB/c mice with live Salmonella suberu and subsequent fusion between isolated spleen lymphoblasts and myeloma cells. Three monoclonal antibodies (MAbs) of immunoglobulin A (IgA) isotype were selected and characterized. All of them were found to recognize the H:g epitope in enzyme-linked immunosorbent assay and immunoblotting but did not react with all H:g-expressing strains in slide agglutination test.

Monoclonal antibody of IgG isotype against a cross-reactive lipopolysaccharide epitope of Chlamydia and Salmonella Re chemotype enhances infectivity in L-929 fibroblast cells.

A murine monoclonal antibody (MAb) 202D7 of IgG3 isotype recognizes a lipopolysaccharide (LPS) epitope of Chlamydia spp. and cross-reacts with the Re chemotype LPS of Salmonella and Escherichia coli. The antibody exhibits strong complement activating properties and stimulates phagocytosis of Salmonella enterica serovar Minnesota Re mutant by murine macrophages.

Lipopolysaccharide-specific but not anti-flagellar immunoglobulin A monoclonal antibodies prevent Salmonella enterica serotype enteritidis invasion and replication within HEp-2 cell monolayers.

The protective potential of immunoglobulin A (IgA) monoclonal antibodies (MAbs) directed against O and H antigens of Salmonella enterica serotype Enteritidis to prevent bacterial adhesion to and invasion of HEp-2 cells was evaluated. Although anti-flagellar IgA MAbs showed strong agglutinating capacities, they did not protect cell monolayers. In contrast, IgA MAbs specific for the O:9 epitope of Salmonella lipopolysaccharide antigen alone prevented S.