Characterization of the neutralizing activity of three anti-human TNF monoclonal antibodies and prediction of their TNF epitopes by molecular modeling and mutant protein approach.

@article{Zhu2006CharacterizationOT,
  title={Characterization of the neutralizing activity of three anti-human TNF monoclonal antibodies and prediction of their TNF epitopes by molecular modeling and mutant protein approach.},
  author={Can-sheng Zhu and Xue-song Liu and Jiannan Feng and Wei Zhang and Beifen Shen and Weiming Ouyang and Yun-xin Cao and Boquan Jin},
  journal={Immunology letters},
  year={2006},
  volume={102 2},
  pages={
          177-83
        }
}

Design and Construction of a Novel Humanized Single-Chain Variable-Fragment Antibody Against the Tumor Necrosis Factor Alpha

The results of an MTT assay showed that the purified GST-hD2 has TNF-α neutralizing activity and hence hD 2 has the potential to be developed into a therapeutic agent, however, more investigation is needed to elucidate the potential of in-vivo T NF-αneutralizing activity of hD2 in comparison to other anti-TNF- α antibodies.

Simulation-Based Engineering of Humanized Scfv Antibody against hTNF-α

The analyses of the results proposed Y27F mutation in heavy chain CDR1 of hD2 scFv antibody may be considered as a promising substitution for designing new anti-TNF-α antibody with improved activity.

Effects of Environmental Factors on Soluble Expression of a Humanized Anti-TNF-α scFv Antibody in Escherichia coli.

Low cultivation temperature in the presence of low amount of inducer under a long incubation time or addition of magnesium chloride are the most effective environmental factors studied for obtaining the maximum solubilization of GST-hD2 recombinant protein.

Tumor necrosis factor-alpha and its inhibition strategies: review article

Tumor necrosis factor-alpha (TNF-α) is a pro-inflammatory cytokine produced by a variety of cells, including hematopoietic and non-hematopoietic cells, malignant cells, macrophages, B lymphocytes, T

IL-13 Neutralization by Two Distinct Receptor Blocking Mechanisms Reduces IgE Responses and Lung Inflammation in Cynomolgus Monkeys

A potent effect of IL-13 neutralization on IgE-mediated atopic responses in a primate model of atopic disease is demonstrated, and it is shown that IL- 13 can be efficiently neutralized by targeting either the IL-4R α – binding epitope or theIL-13R α 1-binding epitope.

Epitope mapping by proteolysis of antigen-antibody complexes.

The steps involved in epitope excision, epitope extraction, and indirect immunosorption are outlined thoroughly and conditions required for MS analysis using either matrix assisted laser desorption ionization or electrospray ionization sources are summarized.

Development of a Spacer-optimized Quenchbody against Tumor Necrosis Factor Alpha

The Q-body with the optimized spacer length showed a maximum 4.5-fold increase in fluorescence intensity with a broad antigen concentration range, and nanomolar order of detection limit, indicating the usefulness of this Q- body for one-step detection of TNFα.

Identification and Affinity Determination of Protein-Antibody and Protein-Aptamer Epitopes by Biosensor-Mass Spectrometry Combination

The combination of mass spectrometry and surface plasmon resonance (SPR) biosensor analysis for identification and affinity determination of protein interactions with antibodies and DNA-aptamers is summarized.

1 Design and Construction of a Novel Humanized Single-Chain Variable-Fragment Antibody against the Tumor Necrosis Factor alpha

The results of an MTT assay showed that the purified GST-hD2 has TNF-α neutralizing activity and hence hD 2 has the potential to be developed into a therapeutic agent, however, more investigation is needed to elucidate the potential of in vivo T NF-αneutralizing activity of hD2 in comparison to other anti-TNF- α antibodies.

Interleukin-13 Neutralization by Two Distinct Receptor Blocking Mechanisms Reduces Immunoglobulin E Responses and Lung Inflammation in Cynomolgus Monkeys

A potent effect of IL-13 neutralization on IgE-mediated atopic responses in a primate system is demonstrated and it is shown that IL- 13 can be efficiently neutralized by targeting either the IL-4Rα-binding epitope or theIL-13Rα1- binding epitope.

References

SHOWING 1-10 OF 22 REFERENCES

Mapping the Epitope of an Inhibitory Monoclonal Antibody to the C-terminal DNA-binding Domain of HIV-1 Integrase*

It is shown that mAb33 is a strong inhibitor of IN catalytic activity, whereas mAb32 is only weakly inhibitory, and this mAb may be a potential target for anti-AIDS drug design.

Structure-activity studies of human tumour necrosis factors.

The mechanism by which tumour necrosis factors (TNF and lymphotoxin, also called TNF alpha and TNF beta respectively) exert their cytotoxic activity on many malignant cells, remains largely unknown.

Applying a New PCR Method to Quickly Prepare Human TNF-α Deletion Mutants

The results indicate that the new PCR method is fast, simple, cheap and deserves popularization, and the cytotoxic activity of the mutants against L929 cells falls down obviously, demonstrating that the two loops are necessary for hTNF-α to exert its biological activities.

The Receptor for Advanced Glycation End Products Is Induced by the Glycation Products Themselves and Tumor Necrosis Factor-α through Nuclear Factor-κB, and by 17β-Estradiol through Sp-1 in Human Vascular Endothelial Cells*

It is suggested that AGE, TNF-α, and E2 can activate the RAGE gene through NF-κB and Sp-1, causing enhanced AGE-RAGE interactions, which would lead to an exacerbation of diabetic microvasculopathy.

Comparison of in vitro cell cytotoxic assays for tumor necrosis factor.

Development of an epitope-specific analytical tool for the major peanut allergen Ara h 2 using a high-density multiple-antigenic peptide strategy.

An analytical tool enabling the determination of immunoglobulin E (IgE)-epitopes in processed food allergens was developed and a multiple-antigenic peptide of the IgE-reactive linear epitope 3 was synthesized and raised a monospecific antiserum against this epitope to obtain a positive control for future epitope resolved diagnostics.