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Special Issue "Monoclonal Antibody"

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

Deadline for manuscript submissions: closed (31 May 2011)

Special Issue Editor

Guest Editor
Dr. Jagadeesh Bayry

Institut National de la Santé et de la Recherche Médicale (INSERM), INSERM Unité 872, Equipe 16  " Immunopathology and therapeutic immunointervention", Centre de Recherche des Cordeliers, 15 Rue de l'Ecole de Médecine, 75006 PARIS, France
Website | E-Mail
Phone: 0033144278203
Fax: +33 1 44 27 81 94
Interests: immunology; autoimmunity; host-pathogen interaction; therapy

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

Published Papers (5 papers)

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Research

Jump to: Review, Other

Open AccessArticle Monoclonal Antibodies against Small Molecule Natural Products and Their Applications, Eastern Blotting and Knockout Extract
Pharmaceuticals 2011, 4(7), 950-963; doi:10.3390/ph4070950
Received: 27 April 2011 / Revised: 3 June 2011 / Accepted: 8 June 2011 / Published: 28 June 2011
Cited by 2 | PDF Full-text (269 KB) | HTML Full-text | XML Full-text
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)

Review

Jump to: Research, Other

Open AccessReview The Role of Monoclonal Antibodies in the Management of Leukemia
Pharmaceuticals 2010, 3(10), 3258-3274; doi:10.3390/ph3103258
Received: 20 September 2010 / Accepted: 18 October 2010 / Published: 18 October 2010
PDF Full-text (133 KB) | HTML Full-text | XML Full-text
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
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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)
Open AccessReview Monoclonal Antibodies for Systemic Lupus Erythematosus (SLE)
Pharmaceuticals 2010, 3(1), 300-322; doi:10.3390/ph3010300
Received: 3 December 2009 / Revised: 12 January 2010 / Accepted: 15 January 2010 / Published: 20 January 2010
Cited by 7 | PDF Full-text (296 KB) | HTML Full-text | XML Full-text
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)
Open AccessReview Impact of Glycosylation on Effector Functions of Therapeutic IgG
Pharmaceuticals 2010, 3(1), 146-157; doi:10.3390/ph3010146
Received: 15 December 2009 / Revised: 30 December 2009 / Accepted: 8 January 2010 / Published: 12 January 2010
Cited by 37 | PDF Full-text (1675 KB) | HTML Full-text | XML Full-text
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)

Other

Jump to: Research, Review

Open AccessCommentary In Response to: ‘Impact of Glycosylation on Effector Functions of Therapeutic IgG’ (Pharmaceuticals 2010, 3, 146–157)
Pharmaceuticals 2010, 3(6), 1887-1891; doi:10.3390/ph3061887
Received: 29 April 2010 / Revised: 31 May 2010 / Accepted: 9 June 2010 / Published: 10 June 2010
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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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