Validation parameters for a novel biosensor assay which simultaneously measures serum concentrations of a humanized monoclonal antibody and detects induced antibodies

Wong, Robbie L; Mytych, Daniel T.; Jacobs, Sheila J.; Bordens, Ronald; Swanson, Steven J.

doi:10.1016/s0022-1759(97)00140-3

Cited by 54 publications

(23 citation statements)

References 7 publications

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“…Ideally it should be possible to carry out 50 or more regeneration cycles on a given immobilized surface, and ligand-binding capacity should be maintained within 20% of positive control values (Wong et al, 1997). Regeneration studies were carried out on the scFv anti-AFB 1 antibody for binding to an immobilized AFB 1 -BSA conjugate surface.…”

Section: Discussionmentioning

confidence: 99%

“…They recommend minimal acceptance limits of 20% (25% at the limits of quantification) for precision profiles. Wong et al (1997) describe the validation of an assay using BIAcore 2000 for the detection and quantification of humanized MAb in mouse serum. They examined and number of variables within the assay including degrees of precision, accuracy, specificity and sensitivity.…”

Section: Discussionmentioning

confidence: 99%

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Production and Characterization of Murine Single Chain Fv Antibodies to Aflatoxin B 1 Derived From a Pre-immunized Antibody Phage Display Library System

Daly

Dillon

Manning

et al. 2002

Food and Agricultural Immunology

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Production and Characterization of Murine Single Chain Fv Antibodies to Aflatoxin B 1 Derived From a Pre-immunized Antibody Phage Display Library System

Daly

Dillon

Manning

et al. 2002

Food and Agricultural Immunology

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“…The sample was placed in an UltraFree-4 centrifugal filter unit containing a 5K NMWL membrane (Millipore, Bedford, MA) and centrifuged in an Eppendorf 5810R tabletop centrifuge (Eppendorf AG, Hamburg, Germany) at 4,000 rpm until concentrated. The concentrated srCEACAM1 was then diluted 1:2 in buffer containing 1 mg carboxymethyl dextran/ml (55), and a 15-l sample was assayed at a flow rate of 10 l/min across each of the four flow cells, to which one of the four region peptides had been bound. The interaction between these proteins was evaluated in real time and reported in resonance units, as we have described previously (39,41).…”

Section: Methodsmentioning

confidence: 99%

A Carcinoembryonic Antigen-Related Cell Adhesion Molecule 1 Homologue Plays a Pivotal Role in Nontypeable Haemophilus influenzae Colonization of the Chinchilla Nasopharynx via the Outer Membrane Protein P5-Homologous Adhesin

et al. 2008

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In vitro studies suggest an important role for CEACAM1 (carcinoembryonic antigen-related cell adhesion molecule 1) in infection by multiple gram-negative bacteria. However, in vivo evidence supporting this role is lacking, largely because the bacterial adhesins involved in this host-microbe association do not bind to murine-derived CEACAM1. One of several adhesins expressed by nontypeable Haemophilus influenzae (NTHI), the outer membrane protein P5-homologous adhesin (or P5), is essential for colonization of the chinchilla nasopharynx and infection of the middle ear. Here we reveal that NTHI P5 binds to the chinchilla homologue of CEACAM1 and that rabbit anti-human carcinoembryonic antigen blocks NTHI colonization of the chinchilla nasopharynx, providing the first demonstration of a role for CEACAM receptor binding by any bacterial pathogen in vivo.The carcinoembryonic antigen-related cellular adhesion molecules (CEACAMs) are a subset of the immunoglobulin superfamily that mediate intercellular binding by homophilic and heterophilic interactions which influence a variety of normal and pathogenic processes, cellular growth, differentiation, and activation (reviewed in references 13, 16, 25, and 35). In vitro studies from several laboratories have now clearly established that adhesins expressed by a variety of important human-restricted bacterial pathogens bind specific members of the CEACAM family. For example, the evolutionarily unrelated colony opacity-associated (Opa) family of adhesins expressed by pathogenic and commensal Neisseria spp. (8, 10-12, 14, 15, 51-53), the Haemophilus influenzae outer membrane protein (OMP) P5 (20), and the Moraxella catarrhalis ubiquitous surface protein UspA1 (21) each bind CEACAMs. This interaction appears to mediate both attachment and engulfment of the bound bacteria by CEACAM-expressing epithelia (52, 54), endothelia (33, 34), and phagocytes (10,14,29,46,47,52). In the context of the epithelia, polarized monolayers of epithelia express CEACAM1, CEACAM5, and CEACAM6 on the apical surface and at cell-cell junctions (49, 54). Bacterial binding to these receptors is sufficient to mediate apical adherence and transcellular transcytosis across the monolayers, allowing the bacteria to emerge in the subepithelial spaces (54). Bacterial binding to CEACAM1 also causes the direct suppression of immune cell activity due to the coinhibitory function of CEACAM1 (9). While these studies suggest an essential role for CEACAM binding in host colonization and persistence, the exquisite specificity of the protein-protein interactions mediated by each of these adhesins has so far prevented their contribution to infection from being addressed in vivo.We previously demonstrated that nontypeable H. influenzae (NTHI) effectively colonizes the upper respiratory tract (URT) of chinchillas and that when this rodent host is also coinfected with a common human URT virus, NTHI can induce culturepositive otitis media (or middle ear infection) via a process that closely reflects the disease course in human...

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“…After saturation of unreacted binding sites with ethanolamine, the obtained immobilization level was 9622 relative response units (RUs). Control lanes included Herceptin (19,999 RUs immobilized) and an ethanolamine treated lane. Samples and standards were analyzed in randomized order (except for the pre-qualification experiment) by injecting 40 L at a flow rate of 10 L/min.…”

Section: Spr Assay Set-upmentioning

confidence: 99%

Qualification and application of a surface plasmon resonance-based assay for monitoring potential HAHA responses induced after passive administration of a humanized anti Lewis-Y antibody

Szolar¹,

Stranner²,

Zinoecker³

et al. 2006

Journal of Pharmaceutical and Biomedical Analysis

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Validation parameters for a novel biosensor assay which simultaneously measures serum concentrations of a humanized monoclonal antibody and detects induced antibodies

Cited by 54 publications

References 7 publications

Production and Characterization of Murine Single Chain Fv Antibodies to Aflatoxin B 1 Derived From a Pre-immunized Antibody Phage Display Library System

Production and Characterization of Murine Single Chain Fv Antibodies to Aflatoxin B 1 Derived From a Pre-immunized Antibody Phage Display Library System

A Carcinoembryonic Antigen-Related Cell Adhesion Molecule 1 Homologue Plays a Pivotal Role in Nontypeable Haemophilus influenzae Colonization of the Chinchilla Nasopharynx via the Outer Membrane Protein P5-Homologous Adhesin

Qualification and application of a surface plasmon resonance-based assay for monitoring potential HAHA responses induced after passive administration of a humanized anti Lewis-Y antibody

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