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Antibodies, Volume 2, Issue 3 (September 2013), Pages 392-534

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Research

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Open AccessArticle Development of an Antibody for Detection of Rhamnolipids Characterized as a Major Bacterial Virulence Factor
Antibodies 2013, 2(3), 501-516; doi:10.3390/antib2030501
Received: 20 June 2013 / Revised: 4 August 2013 / Accepted: 16 August 2013 / Published: 28 August 2013
Cited by 1 | PDF Full-text (448 KB) | HTML Full-text | XML Full-text
Abstract
Rhamnolipids (RLs), the glycolipidic biosurfactants found initially as exoproducts of the opportunistic pathogen Pseudomonas aeruginosa, are characterized as virulence factors contributing to its pathogenesis infections. However, RLs are also produced by various bacterial species. They consist of a gluconic part, usually containing
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Rhamnolipids (RLs), the glycolipidic biosurfactants found initially as exoproducts of the opportunistic pathogen Pseudomonas aeruginosa, are characterized as virulence factors contributing to its pathogenesis infections. However, RLs are also produced by various bacterial species. They consist of a gluconic part, usually containing one or two rhamnoses, and a lipid part, containing one or two hydroxy-fatty acids. In this study, we present both the isolation of RLs from bacterial cultures of the non-pathogenic bacterium Thermus thermophilus as well as the development of the rabbit antibody directed against them. The antibody was titrated and evaluated, in respect of its recognition selectivity. Between both RLs constituents, it specifically recognized only the hydroxydecanoic acid between the fatty acids tested, contrary to rhamnose. The potential of the antibody to recognize both purified RLs and RLs present in crude extracellular media produced by T. thermophilus and Escherichia coli cultures, is evidenced by Dot Blot immuno-reaction. The development of this antibody is addressed in detail, as the sensitive analytical technique, and its potential use would facilitate the implementation of rhamnolipids’ detection, or may be a useful and promising tool for determining these microbial secondary metabolites and virulence factors secreted in extracellular culture media or in biological fluids during infections. Full article

Review

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Open AccessReview Antibody Glycosylation and Inflammation
Antibodies 2013, 2(3), 392-414; doi:10.3390/antib2030392
Received: 3 April 2013 / Revised: 11 June 2013 / Accepted: 18 June 2013 / Published: 25 June 2013
Cited by 18 | PDF Full-text (275 KB) | HTML Full-text | XML Full-text
Abstract
IgG antibodies are the basis of some of the most effective therapeutics developed over the last 20 years. These antibodies are highly specific, have long serum-half lives, and can be produced relatively routinely, making them ideal drugs for immunotherapy. The degree of regulation
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IgG antibodies are the basis of some of the most effective therapeutics developed over the last 20 years. These antibodies are highly specific, have long serum-half lives, and can be produced relatively routinely, making them ideal drugs for immunotherapy. The degree of regulation on IgG antibody effector functions by the composition of the single, N-linked glycan attached to the Fc is increasingly appreciated. IgG antibodies with identical protein sequences can gain a 50-fold potency, in terms of initiating antibody-dependent cellular cytotoxicity (ADCC) by removal of the single fucose residue from the Fc glycan. Conversely, the addition of sialic acid to the terminus of the Fc glycan converts IgG antibodies into anti-inflammatory mediators, capable of suppressing autoantibody driven inflammation. This review will discuss the contribution of the Fc glycan to IgG antibody effector functions, the regulation of the antibody glycosylation in vivo, implications for the rational design of IgG antibody-based therapeutics, and touch upon the contribution of glycosylation to other immunoglobulin isotypes. Full article
(This article belongs to the Special Issue Modes of Antibody Action for Cancer Therapy)
Open AccessReview In Vivo Secretion of Bispecific Antibodies Recruiting Lymphocytic Effector Cells
Antibodies 2013, 2(3), 415-425; doi:10.3390/antib2030415
Received: 13 March 2013 / Revised: 6 June 2013 / Accepted: 19 June 2013 / Published: 27 June 2013
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Abstract
Engineered Fc-lacking bispecific antibodies have shown an exceptionally high potency for recruiting lymphocyte effector cells and enhancing antitumor activity, which is under evaluation in several clinical trials. However, current treatment regimens raise some issues that should be considered, such as the high cost
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Engineered Fc-lacking bispecific antibodies have shown an exceptionally high potency for recruiting lymphocyte effector cells and enhancing antitumor activity, which is under evaluation in several clinical trials. However, current treatment regimens raise some issues that should be considered, such as the high cost of clinical-grade bispecific antibodies and the achievement of sustained therapeutic plasma levels. The use of gene transfer methods may circumvent problems related to large-scale production and purification, and result in sustained therapeutic plasma concentrations of the Fc-lacking bispecific antibodies. In fact, terminally differentiated cells and non-terminally differentiated cells can be genetically modified to secrete functionally active bispecific antibodies exerting clear anti-tumor effects. This review highlights the relevance of different promising strategies for in vivo delivery of therapeutic bispecific antibodies. Full article
(This article belongs to the Special Issue Bispecific Antibodies for Dual Targeting Strategies)
Open AccessReview Molecular Engineering of Therapeutic Cytokines
Antibodies 2013, 2(3), 426-451; doi:10.3390/antib2030426
Received: 9 May 2013 / Revised: 13 June 2013 / Accepted: 13 June 2013 / Published: 3 July 2013
Cited by 7 | PDF Full-text (342 KB) | HTML Full-text | XML Full-text
Abstract
Over the past three decades, a large body of work has been directed at the development of therapeutic cytokines. Despite their central role in immune modulation, only a handful of cytokine therapeutics has achieved regulatory approval. One of the major challenges associated with
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Over the past three decades, a large body of work has been directed at the development of therapeutic cytokines. Despite their central role in immune modulation, only a handful of cytokine therapeutics has achieved regulatory approval. One of the major challenges associated with the therapeutic use of cytokines relates to their short serum half-life and low bioavailability. High doses are required to overcome these problems, which often result in dose-limiting toxicities. Consequently, most cytokines require protein engineering approaches to reduce toxicity and increase half-life. For this purpose, PEGylation, fusion proteins, antibody complexes and mutagenesis have been utilized. Here, we summarize past, recent and emerging strategies in this area. Full article
(This article belongs to the Special Issue Cytokine Growth Factor Antibodies in Immunotherapy)
Open AccessReview Developments and Challenges for mAb-Based Therapeutics
Antibodies 2013, 2(3), 452-500; doi:10.3390/antib2030452
Received: 23 May 2013 / Revised: 18 July 2013 / Accepted: 2 August 2013 / Published: 16 August 2013
Cited by 20 | PDF Full-text (867 KB) | HTML Full-text | XML Full-text
Abstract
The continuous increase in the number of approved monoclonal antibody (mAb)-based therapy suggests that mAbs, and their derivatives, will continue to be the focus of the biotherapeutics industry for years to come. Although vast improvements in our capability to manufacture, characterize, and stabilize
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The continuous increase in the number of approved monoclonal antibody (mAb)-based therapy suggests that mAbs, and their derivatives, will continue to be the focus of the biotherapeutics industry for years to come. Although vast improvements in our capability to manufacture, characterize, and stabilize mAbs have been achieved, there are still challenges to be overcome. These include analytical and stabilization approaches associated with the development of high concentration mAb formulations. In addition, several mAb-based modalities are under development, including antibody drug conjugates (ADCs), fusion proteins, and bispecific antibodies (bsAbs), all designed to overcome the limitations encountered with mAb therapy. The current status of their development, with emphasis on manufacturing challenges as well as preliminary clinical results, will be reviewed. Full article
Open AccessReview T-Cell Receptor-Like Antibodies: Targeting the Intracellular Proteome Therapeutic Potential and Clinical Applications
Antibodies 2013, 2(3), 517-534; doi:10.3390/antib2030517
Received: 15 August 2013 / Revised: 22 August 2013 / Accepted: 22 August 2013 / Published: 17 September 2013
Cited by 2 | PDF Full-text (215 KB) | HTML Full-text | XML Full-text
Abstract
Major histocompatibility complex (MHC) class I molecules are key in the immune response against malignant cells by shaping the T-cell repertoire and presenting peptides from endogenous antigens to CD8+ cytotoxic T cells. Because of their unique specificity, MHC-peptide complexes are a desirable target
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Major histocompatibility complex (MHC) class I molecules are key in the immune response against malignant cells by shaping the T-cell repertoire and presenting peptides from endogenous antigens to CD8+ cytotoxic T cells. Because of their unique specificity, MHC-peptide complexes are a desirable target for novel immunotherapeutic approaches. These complexes can be targeted by recombinant T-cell receptors (TCRs). However, most TCRs produced thus far have affinities which are too low for target detection under normal assay conditions, and limited stability (due to their generation in a single-chain version). Developing high-affinity soluble antibody molecules endowed with a TCR-like specificity toward tumor epitopes, termed TCR-like antibodies, addresses the low affinity of TCRs. These TCR-like antibodies are being developed as a new immunotherapeutic class for targeting tumor cells and mediating their specific killing. In addition, these antibodies are valuable research reagents enabling the study of human class I peptide-MHC ligand-presentation and TCR–peptide–MHC interactions. Full article
(This article belongs to the Special Issue Recombinant Immunotoxins)

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