Generation of chimeric monoclonal antibodies from mice that carry human immunoglobulin Cγ1 heavy or Cκ light chain gene segments

Pluschke, Gerd; Joss, Andrea; Marfurt, Jutta; Daubenberger, Claudia; Kashala, Oscar; Zwickl, Markus; Stief, A; Sansig, Gilles; Schläpfer, Beatrice S.; Linkert, Susanne; Putten, Herman van der; Hardman, Norman; Schröder, Markus

doi:10.1016/s0022-1759(98)00041-6

Cited by 15 publications

(12 citation statements)

References 16 publications

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“…The anthrosecontaining synthetic carbohydrates were prepared as described previously (20,22,23). Mice carrying human immunoglobulin C␥1 heavy and C light chain gene segments (16) were immunized with an anthrose-rhamnose disaccharide conjugated to keyhole limpet hemocyanin (KLH) and formulated in ImmunEasy adjuvant (Qiagen AG, Hombrechtikon, Switzerland). Mice received 3 doses of 40 g conjugate at 3-week intervals.…”

Section: Methodsmentioning

confidence: 99%

Anthrax Spore Detection by a Luminex Assay Based on Monoclonal Antibodies That Recognize Anthrose-Containing Oligosaccharides

Tamborrini

Holzer

Seeberger

et al. 2010

Clin Vaccine Immunol

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The similarity of endospore surface antigens between bacteria of the Bacillus cereus group complicates the development of selective antibody-based anthrax detection systems. The surface of B. anthracis endospores exposes a tetrasaccharide containing the monosaccharide anthrose. Anti-tetrasaccharide monoclonal antibodies (MAbs) and anti-anthrose-rhamnose disaccharide MAbs were produced and tested for their fine specificities in a direct spore enzyme-linked immunosorbent assay (ELISA) with inactivated spores of a broad spectrum of B. anthracis strains and related species of the Bacillus genus. Although the two sets of MAbs had different fine specificities, all of them recognized the tested B. anthracis strains and showed only a limited cross-reactivity with two B. cereus strains. The MAbs were further tested for their ability to be implemented in a highly sensitive and specific bead-based Luminex assay. This assay detected spores from different B. anthracis strains and two cross-reactive B. cereus strains, correlating with the results obtained in direct spore ELISA. The Luminex assay (detection limit 10 3 to 10 4 spores per ml) was much more sensitive than the corresponding sandwich ELISA. Although not strictly specific for B. anthracis spores, the developed Luminex assay represents a useful first-line screening tool for the detection of B. anthracis spores.

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Section: Methodsmentioning

confidence: 99%

Anthrax Spore Detection by a Luminex Assay Based on Monoclonal Antibodies That Recognize Anthrose-Containing Oligosaccharides

Tamborrini

Holzer

Seeberger

et al. 2010

Clin Vaccine Immunol

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“…The purified recombinant protein was identified as the expected D13 protein by matrix-assisted laser desorption ionization-time of flight mass spectrometry. D13-specific MAbs were generated from mice carrying human heavy and light immunoglobulin chain replacement mutations (18). After repeated immunization with the recombinant fragment of D13 delivered with MPLϩTDM as adjuvant, four anti-D13 MAbs were generated that reacted with the recombinant 17 kDa fragment in ELISA ( lysates of unsynchronized blood stage parasites one distinct band of ϳ100 kDa (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Hybridoma cell lines were generated from mice immunized essentially as described (18). A group of five mice was immunized subcutaneously three times with 50 g recombinant D13 protein isolated under denaturing conditions and formulated in MPLϩTDM adjuvant (Sigma Chemicals, St. Louis, Mo.).…”

Section: Identification Of Orf D13mentioning

confidence: 99%

Identification and Characterization of a Conserved, Stage-Specific Gene Product of Plasmodium falciparum Recognized by Parasite Growth Inhibitory Antibodies

et al. 2003

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We have identified a novel conserved protein of Plasmodium falciparum, designated D13, that is stagespecifically expressed in asexual blood stages of the parasite. The predicted open reading frame (ORF) D13 contains 863 amino acids with a calculated molecular mass of 99.7 kDa and displays a repeat region composed of pentapeptide motives. Northern blot analysis with lysates of synchronized blood stage parasites showed that D13 is highly expressed at the mRNA level during schizogony. The first N-terminal 138 amino acids of D13 were expressed in Escherichia coli and the purified protein was used to generate anti-D13 monoclonal antibodies (MAbs). Using total lysates of blood stage parasites and Western blot analysis, these MAbs stained one single band of ϳ100 kDa, corresponding to the predicted molecular mass of ORF D13. Western blot analysis demonstrated further that D13 is expressed during schizogony, declines rapidly in early ring stages and is undetectable in trophozoites. D13 protein is localized in individual merozoites in a distinct area, as demonstrated by indirect immunofluorescence analysis. After subcellular fractionation, D13 was confined to the pelleted fraction of the parasite lysate and its extraction by alkaline carbonate buffer treatment indicated that D13 is not a membrane-integral protein. Inclusion of certain anti-D13 MAbs into in vitro cultures of blood stage parasites resulted in considerable reduction in parasite growth. The N-terminal domain encompassing 158 amino acids is 94 and 95%, respectively, identical at the amino acid level between Plasmodium knowlesi, Plasmodium yoelii, and P. falciparum. In summary, we describe a novel stage-specifically expressed, highly conserved gene product of P. falciparum that is recognized by parasite growth inhibitory antibodies.

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“…Hybridomas were generated from mice immunized as described (36) with SPf66 or with His 6 rRAP-1 using PAI mouse myeloma cells as a fusion partner (38). Hybrids were selected in hypoxanthine-aminopterin-thymidine (HAT) medium, and cells that secreted MAbs specific for the 35.1 building block of SPf66 or for His 6 rRAP-1 , respectively, were identified by enzyme-linked immunosorbent assay (ELISA).…”

Section: Methodsmentioning

confidence: 99%

Rhoptry-Associated Protein 1-Binding Monoclonal Antibody Raised against a Heterologous Peptide Sequence InhibitsPlasmodium falciparumGrowth In Vitro

et al. 2001

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Generation of chimeric monoclonal antibodies from mice that carry human immunoglobulin Cγ1 heavy or Cκ light chain gene segments

Cited by 15 publications

References 16 publications

Anthrax Spore Detection by a Luminex Assay Based on Monoclonal Antibodies That Recognize Anthrose-Containing Oligosaccharides

Anthrax Spore Detection by a Luminex Assay Based on Monoclonal Antibodies That Recognize Anthrose-Containing Oligosaccharides

Identification and Characterization of a Conserved, Stage-Specific Gene Product of Plasmodium falciparum Recognized by Parasite Growth Inhibitory Antibodies

Rhoptry-Associated Protein 1-Binding Monoclonal Antibody Raised against a Heterologous Peptide Sequence InhibitsPlasmodium falciparumGrowth In Vitro

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