The rapid determination of binding constants for antiviral antibodies by a radioimmunoassay. An analysis of the interaction between hybridoma proteins and influenza virus

Frankel, Mark; Gerhard, Walter

doi:10.1016/0161-5890(79)90051-8

Cited by 185 publications

(63 citation statements)

References 12 publications

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“…The solid-phase radioimmunoassay system employed was adapted from that previously described by Frankel and Gerhard (48) and later modified by Mandrell and Zollinger (49), except that LPS (or lipid A) was the solid-phase antigen used to coat the wells of flexible polyvinyl microtiter plates (overnight incubation at 4VC at an appropriate LPS concentration, as indicated below). Serial dilutions of mAb, prepared by ammonium sulfate precipitation of hybridoma tissue culture supernatant obtained under serum-free conditions, were incubated overnight at room temperature in LPS-coated microtiter plates.…”

Section: Methodsmentioning

confidence: 99%

Human monoclonal antibodies that recognize conserved epitopes in the core-lipid A region of lipopolysaccharides.

Pollack¹,

Raubitschek²,

Larrick³

1987

J. Clin. Invest.

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Section: Methodsmentioning

confidence: 99%

Human monoclonal antibodies that recognize conserved epitopes in the core-lipid A region of lipopolysaccharides.

Pollack¹,

Raubitschek²,

Larrick³

1987

J. Clin. Invest.

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“…The avidity constant of radiolabeled NHS76/PEP 2 was determined by a fixed-cell RIA developed in our laboratory (29), using the method of Frankel and Gerhard (30). Scatchard analysis was done to obtain the slope.…”

Section: Determination Of Avidity Constantmentioning

confidence: 99%

NHS76/PEP2, a Fully Human Vasopermeability-Enhancing Agent to Increase The Uptake and Efficacy of Cancer Chemotherapy

Khawli

Epstein

2005

Clinical Cancer Research

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Purpose: Previously, we have shown that the attachment of interleukin 2 (IL-2) to a tumortargeting antibody can produce a 4-fold enhancement in the uptake of antibodies and drugs in tumors. More recently, we discovered that a 37-amino-acid linear sequence of IL-2 designated vasopermeability-enhancing peptide (PEP), contained the vasopermeability activity of IL-2, and could be used after linkage to tumor-targeting antibodies to produce the same enhancement of drugs and antibodies in tumors. We now describe the generation of a fully human antibody fusion protein, designated NHS76/PEP 2 , which can be used in patients to enhance the therapeutic potential of chemotherapy. Methods: NHS76/PEP 2 was expressed in NS0 cells using the glutamine synthetase gene amplification system. To show its clinical potential as a pretreatment to chemotherapy, NHS76/PEP 2 was given i.v. 2 hours before the injection of suboptimal doses of etoposide, doxorubicin, Taxol, Taxotere, 5-fluorouracil, or vinblastine in mice bearing established solid tumors. Results were recorded by measuring tumor volumes thrice per week. Results: Compared with drug treatment alone, NHS76/PEP 2 pretreatment substantially improved the effectiveness of chemotherapeutic agents in solid tumor models.Tumor suppression was most pronounced in those groups of mice bearing tumors known to be sensitive to the specific drug under study. However, in certain instances, tumors previously known to be resistant to specific single chemotherapeutic agents were shown to respond by the addition of NHS76/PEP 2 pretreatment. Conclusions: NHS76/PEP 2 seems an excellent candidate to improve the value of standard chemotherapy drug treatment by virtue of its ability to increase the uptake of drugs in solid tumors selectively.

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“…Prior to the competitive binding studies, therefore, the avidities of the anti-NP and anti-M MAbs were compared by ELISA, assuming that at antigen saturation the maximum amount of antibody bound to the wells is a direct reflection of the avidity of the antibody for its epitope (Frankel & Gerhard, 1979). As seen in Fig.…”

Section: Antigenic Analysis Of Np and M By Competitive Binding Assaysmentioning

confidence: 99%

Antigenic Characterization of the Nucleoprotein and Matrix Protein of Influenza C Virus with Monoclonal Antibodies

Sugawara

Nishimura

Hongō

et al. 1991

Journal of General Virology

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Monoclonal antibodies against the nucleoprotein (NP) and matrix (M) protein of influenza C virus were prepared and characterized. At least two non-overlapping or partially overlapping antigenic sites were delineated on each of the proteins by competitive binding assays. Western blot analysis showed that two antigenic sites on the M protein were highly resistant to conformational changes whereas two sites on NP were sensitive. No antigenic variation was seen in either the NP or the M protein when the reactivity of monoclonal antibodies with 23 different influenza C strain s isolated over a 41 year period was studied by radioimmunoprecipitation and enzyme-linked immunosorbent assay. Immunofluorescence analysis with the monoclonal antibodies revealed that both the NP and M proteins migrated to the cell nucleus during the replication cycle of influenza C virus.

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The rapid determination of binding constants for antiviral antibodies by a radioimmunoassay. An analysis of the interaction between hybridoma proteins and influenza virus

Cited by 185 publications

References 12 publications

Human monoclonal antibodies that recognize conserved epitopes in the core-lipid A region of lipopolysaccharides.

Human monoclonal antibodies that recognize conserved epitopes in the core-lipid A region of lipopolysaccharides.

NHS76/PEP2, a Fully Human Vasopermeability-Enhancing Agent to Increase The Uptake and Efficacy of Cancer Chemotherapy

Antigenic Characterization of the Nucleoprotein and Matrix Protein of Influenza C Virus with Monoclonal Antibodies

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