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Pharmaceuticals
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Monoclonal Antibody
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Monoclonal Antibody

A special issue of Pharmaceuticals (ISSN 1424-8247).

Deadline for manuscript submissions: closed (31 May 2011) | Viewed by 55657

Special Issue Editor

Prof. Dr. Jagadeesh Bayry

E-Mail Website
Guest Editor
Centre de Recherche des Cordeliers, Sorbonne Université, F-75006 Paris, France
Interests: immunology; immune homeostasis; immunotherapy; host-pathogen interaction
Special Issues, Collections and Topics in MDPI journals

Keywords

  • design and engineering antibody
  • therapy
  • autoimmune diseases
  • cancer
  • B cells
  • T cells
  • cytokines
  • co-stimulatory molecules
  • preclinical evaluation
  • experimental models
  • immunogenecity
  • transplantation
  • dermatology
  • infectious diseases

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Published Papers (5 papers)

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Research

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269 KiB  
Article
Monoclonal Antibodies against Small Molecule Natural Products and Their Applications, Eastern Blotting and Knockout Extract
by Yukihiro Shoyama
Pharmaceuticals 2011, 4(7), 950-963; https://doi.org/10.3390/ph4070950 - 28 Jun 2011
Cited by 4 | Viewed by 8244
Abstract
To determine the hapten number in hapten-carrier protein conjugate matrix-assisted laser desorption/ionization (MALDI) tof mass spectrometry was applied. Highly specific anti-ginsenoside Rb1 and Rg1 monoclonal antibodies (MAbs) were prepared. Ginsenosides were developed on thin layer chromatography (TLC) plates which were covered [...] Read more.
To determine the hapten number in hapten-carrier protein conjugate matrix-assisted laser desorption/ionization (MALDI) tof mass spectrometry was applied. Highly specific anti-ginsenoside Rb1 and Rg1 monoclonal antibodies (MAbs) were prepared. Ginsenosides were developed on thin layer chromatography (TLC) plates which were covered by a polyvinylidene difluoride (PVDF) membrane resulting in blotting. The membrane was treated with NaIO4 solution to release the aldehyde group on the sugar moiety of the ginsenosides. By treatment of the membrane with a protein solution the ginsenoside-protein conjugation as a Schiff-base occurred, which can function to fix it to the PVDF membrane. A part of the ginsenoside aglycone was reacted with anti-ginsenoside Rb1 MAb, secondary MAb conjugated with enzyme and finally a substrate was added, resulting in a specific and highly sensitive staining that we named Eastern blotting. Furthermore, it makes one-step isolation of ginsenoside Rb1 possible using an immuno-affinity column conjugated with anti-ginsenoside Rb1 MAb. Furthermore, immunoaffinity concentration was carried out allowing high sensitivity analysis of lower concentrations of ginsenoside Rb1 so that several unknown bands could be structurally determined. Full article
(This article belongs to the Special Issue Monoclonal Antibody)
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Review

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133 KiB  
Review
The Role of Monoclonal Antibodies in the Management of Leukemia
by Ali Al-Ameri, Mohamad Cherry, Aref Al-Kali and Alessandra Ferrajoli
Pharmaceuticals 2010, 3(10), 3258-3274; https://doi.org/10.3390/ph3103258 - 18 Oct 2010
Viewed by 8558
Abstract
This article will review the monoclonal antibodies more commonly used in leukemias. In the last three decades, scientists have made considerable progress understanding the structure and the functions of various surface antigens, such as CD20, CD33. The introduction of rituximab, an anti CD20 [...] Read more.
This article will review the monoclonal antibodies more commonly used in leukemias. In the last three decades, scientists have made considerable progress understanding the structure and the functions of various surface antigens, such as CD20, CD33. The introduction of rituximab, an anti CD20 monoclonal antibody, had a great impact in the treatment of lymphoproliferative disorders. Gemtuzumab, an anti CD 33 conjugated monoclonal antibody has activity in acute mylegenous leukemia (AML). As this field is undergoing a rapid growth, the years will see an increasing use of monoclonal antibodies in hematological malignancies. Full article
(This article belongs to the Special Issue Monoclonal Antibody)
296 KiB  
Review
Monoclonal Antibodies for Systemic Lupus Erythematosus (SLE)
by Claudio Ponticelli and Gabriella Moroni
Pharmaceuticals 2010, 3(1), 300-322; https://doi.org/10.3390/ph3010300 - 20 Jan 2010
Cited by 12 | Viewed by 14252
Abstract
A number of monoclonal antibodies (mAb) are now under investigation in clinical trials to assess their potential role in Systemic Lupus Erythematosus (SLE). The most frequently used mAb is rituximab, which is directed against CD20, a membrane protein expressed on B lymphocytes. Uncontrolled [...] Read more.
A number of monoclonal antibodies (mAb) are now under investigation in clinical trials to assess their potential role in Systemic Lupus Erythematosus (SLE). The most frequently used mAb is rituximab, which is directed against CD20, a membrane protein expressed on B lymphocytes. Uncontrolled trials reported an improvement of SLE activity in non-renal patients and other studies even reported an improvement of severe lupus nephritis unresponsive to conventional treatments. However two randomized trials failed to show the superiority of rituximab over conventional treatment in non renal SLE and in lupus nephritis. Preliminary trials reported promising results with epratuzumab, a humanized mAb directed against CD22, and with belimumab, a human mAb that specifically recognizes and inhibits the biological activity of BLyS a cytokine of the tumornecrosis-factor (TNF) ligand superfamily. Other clinical trials with mAb directed against TNF-alpha, interleukin-10 (Il-10), Il-6, CD154, CD40 ligand, IL-18 or complement component C5 are under way. At present, however, in spite of good results reported by some studies, no firm conclusion on the risk-benefit profile of these mAbs in patients with SLE can be drawn from the available studies. Full article
(This article belongs to the Special Issue Monoclonal Antibody)
1675 KiB  
Review
Impact of Glycosylation on Effector Functions of Therapeutic IgG
by Riad Abès and Jean-Luc Teillaud
Pharmaceuticals 2010, 3(1), 146-157; https://doi.org/10.3390/ph3010146 - 12 Jan 2010
Cited by 101 | Viewed by 16721
Abstract
Human IgG has only one conserved glycosylation site located in the Cγ2 domain of the Fc region that accounts for the presence of two sugar moieties per IgG. These IgG sugar cores play a critical role in a number of IgG effector functions. [...] Read more.
Human IgG has only one conserved glycosylation site located in the Cγ2 domain of the Fc region that accounts for the presence of two sugar moieties per IgG. These IgG sugar cores play a critical role in a number of IgG effector functions. In the present review, we describe the main characteristics of IgG Fc glycosylation and some abnormalities of serum IgG glycosylation. We also discuss how glycosylation impacts on monoclonal antibodies (mAbs) and IVIg effector functions and how these molecules can be engineered. Several therapeutic antibodies have now been engineered to be no- or low-fucose antibodies and are currently tested in clinical trials. They exhibit an increased binding to activating FcγRIIIA and trigger a strong antibody-dependent cell cytotoxicity (ADCC) as compared to their highly-fucosylated counterparts. They represent a new generation of therapeutic antibodies that are likely to show a better clinical efficacy in patients, notably in cancer patients where cytotoxic antibodies are needed. Full article
(This article belongs to the Special Issue Monoclonal Antibody)
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Other

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146 KiB  
Commentary
In Response to: ‘Impact of Glycosylation on Effector Functions of Therapeutic IgG’ (Pharmaceuticals 2010, 3, 146–157)
by Andreas Nechansky, Iris Koller and Ralf Kircheis
Pharmaceuticals 2010, 3(6), 1887-1891; https://doi.org/10.3390/ph3061887 - 10 Jun 2010
Cited by 1 | Viewed by 6938
Abstract
To complete the review article by Abes and colleagues (Pharmaceuticals 2010, 3, 146–157) which provides a good overview on recently developed approaches for generation of glyco-modified antibodies and the impact of glyco-modification of antibodies on their effector functions, important information [...] Read more.
To complete the review article by Abes and colleagues (Pharmaceuticals 2010, 3, 146–157) which provides a good overview on recently developed approaches for generation of glyco-modified antibodies and the impact of glyco-modification of antibodies on their effector functions, important information should be added, namely that — besides the Glycart and the Biowa approach to generate de-fucosylated antibodies — innovative, moss derived methods have been shown to generate glyco-modified antibodies with improved effector function profile. Full article
(This article belongs to the Special Issue Monoclonal Antibody)
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