Special Issue "Immunoglobulin"

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A special issue of Biomolecules (ISSN 2218-273X).

Deadline for manuscript submissions: closed (31 October 2014)

Special Issue Editor

Guest Editor
Prof. Rhodri Ceredig (Website)

Bioscience Building, Corrib Village, National University of Ireland, Galway, Ireland
Interests: mouse lymphocyte development; Interleukin-7; cell lineage decisions in hematopoiesis; mesenchymal stromal cells

Special Issue Information

Dear Colleagues,

Immunoglobulin, the secreted form of the B lymphocyte receptor molecule, represents one of nature’s most flexible and potent biomolecules. Two functions (i.e., highly specific recognition and effector functions) are combined into one molecule. The specific molecular interaction between the antibody paratope and its corresponding antigen epitope activates the effector function of the molecule, thereby linking the exquisite specificity of the adaptive immune system with the prototypic cellular and molecular components of the natural immune response. With current molecular biological techniques, these two immunoglobulin functions can be independently manipulated. Intensive analysis of B lymphocyte responses has uncovered details concerning immunoglobulin class switching and somatic hypermutation during T dependent antibody responses. For readers of Biomolecules, this Special Issue provides an up-to-date account of some of the more intriguing aspects of immunoglobulins.

Prof. Rhodri Ceredig
Guest Editor

Submission

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

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Published Papers (6 papers)

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Review

Open AccessReview The Production Processes and Biological Effects of Intravenous Immunoglobulin
Biomolecules 2016, 6(1), 15; doi:10.3390/biom6010015
Received: 23 August 2015 / Revised: 1 March 2016 / Accepted: 1 March 2016 / Published: 9 March 2016
PDF Full-text (272 KB) | HTML Full-text | XML Full-text
Abstract
Immunoglobulin is a highly diverse autologous molecule able to influence immunity in different physiological and diseased situations. Its effect may be visible both in terms of development and function of B and T lymphocytes. Polyclonal immunoglobulin may be used as therapy in [...] Read more.
Immunoglobulin is a highly diverse autologous molecule able to influence immunity in different physiological and diseased situations. Its effect may be visible both in terms of development and function of B and T lymphocytes. Polyclonal immunoglobulin may be used as therapy in many diseases in different circumstances such as primary and secondary hypogammaglobulinemia, recurrent infections, polyneuropathies, cancer, after allogeneic transplantation in the presence of infections and/or GVHD. However, recent studies have broadened the possible uses of polyclonal immunoglobulin showing that it can stimulate certain sub-populations of T cells with effects on T cell proliferation, survival and function in situations of lymphopenia. These results present a novel and considerable impact of intravenous immunoglobulin (IVIg) treatment in situations of severe lymphopenia, a situation that can occur in cancer patients after chemo and radiotherapy treatments. In this review paper the established and experimental role of polyclonal immunoglobulin will be presented and discussed as well as the manufacturing processes involved in their production. Full article
(This article belongs to the Special Issue Immunoglobulin)
Open AccessReview Immunoglobulin Isotypes in Atlantic Salmon, Salmo Salar
Biomolecules 2015, 5(1), 166-177; doi:10.3390/biom5010166
Received: 10 November 2014 / Revised: 10 February 2015 / Accepted: 22 February 2015 / Published: 27 February 2015
Cited by 4 | PDF Full-text (6332 KB) | HTML Full-text | XML Full-text
Abstract
There are three major immunoglobulin (Ig) isotypes in salmonid fish: IgM, IgD and IgT, defined by the heavy chains μ, δ and τ, respectively. As a result of whole genome duplication in the ancestor of the salmonid fish family, Atlantic salmon ( [...] Read more.
There are three major immunoglobulin (Ig) isotypes in salmonid fish: IgM, IgD and IgT, defined by the heavy chains μ, δ and τ, respectively. As a result of whole genome duplication in the ancestor of the salmonid fish family, Atlantic salmon (Salmo salar) possess two highly similar Ig heavy chain gene complexes (A and B), comprising two μ genes, two δ genes, three intact τ genes and five τ pseudogenes. The μA and μB genes correspond to two distinct sub-populations of serum IgM. The IgM-B sub-variant has a characteristic extra cysteine near the C-terminal part of the heavy chain and exhibits a higher degree of polymer disulfide cross-linking compared to IgM-A. The IgM-B:IgM-A ratio in serum is typically 60:40, but skewed ratios are also observed. The IgT isotype appears to be specialized to mucosal immune responses in salmonid fish. The concentration of IgT in serum is 100 to 1000 times lower than IgM. Secreted forms of IgD have been detected in rainbow trout, but not yet in Atlantic salmon. Full article
(This article belongs to the Special Issue Immunoglobulin)
Open AccessReview Artificial Affinity Proteins as Ligands of Immunoglobulins
Biomolecules 2015, 5(1), 60-75; doi:10.3390/biom5010060
Received: 13 November 2014 / Revised: 17 December 2014 / Accepted: 23 January 2015 / Published: 30 January 2015
Cited by 2 | PDF Full-text (4247 KB) | HTML Full-text | XML Full-text
Abstract
A number of natural proteins are known to have affinity and specificity for immunoglobulins. Some of them are widely used as reagents for detection or capture applications, such as Protein G and Protein A. However, these natural proteins have a defined spectrum [...] Read more.
A number of natural proteins are known to have affinity and specificity for immunoglobulins. Some of them are widely used as reagents for detection or capture applications, such as Protein G and Protein A. However, these natural proteins have a defined spectrum of recognition that may not fit specific needs. With the development of combinatorial protein engineering and selection techniques, it has become possible to design artificial affinity proteins with the desired properties. These proteins, termed alternative scaffold proteins, are most often chosen for their stability, ease of engineering and cost-efficient recombinant production in bacteria. In this review, we focus on alternative scaffold proteins for which immunoglobulin binders have been identified and characterized. Full article
(This article belongs to the Special Issue Immunoglobulin)
Open AccessReview Factors Regulating Immunoglobulin Production by Normal and Disease-Associated Plasma Cells
Biomolecules 2015, 5(1), 20-40; doi:10.3390/biom5010020
Received: 5 November 2014 / Accepted: 13 January 2015 / Published: 21 January 2015
Cited by 3 | PDF Full-text (122 KB) | HTML Full-text | XML Full-text
Abstract
Immunoglobulins are molecules produced by activated B cells and plasma cells in response to exposure to antigens. Upon antigen exposure, these molecules are secreted allowing the immune system to recognize and effectively respond to a myriad of pathogens. Immunoglobulin or antibody secreting [...] Read more.
Immunoglobulins are molecules produced by activated B cells and plasma cells in response to exposure to antigens. Upon antigen exposure, these molecules are secreted allowing the immune system to recognize and effectively respond to a myriad of pathogens. Immunoglobulin or antibody secreting cells are the mature form of B lymphocytes, which during their development undergo gene rearrangements and selection in the bone marrow ultimately leading to the generation of B cells, each expressing a single antigen-specific receptor/immunoglobulin molecule. Each individual immunoglobulin molecule has an affinity for a unique motif, or epitope, found on a given antigen. When presented with an antigen, activated B cells differentiate into either plasma cells (which secrete large amounts of antibody that is specific for the inducing antigen), or memory B cells (which are long-lived and elicit a stronger and faster response if the host is re-exposed to the same antigen). The secreted form of immunoglobulin, when bound to an antigen, serves as an effector molecule that directs other cells of the immune system to facilitate the neutralization of soluble antigen or the eradication of the antigen-expressing pathogen. This review will focus on the regulation of secreted immunoglobulin by long-lived normal or disease-associated plasma cells. Specifically, the focus will be on signaling and transcriptional events that regulate the development and homeostasis of long-lived immunoglobulin secreting plasma cells. Full article
(This article belongs to the Special Issue Immunoglobulin)
Open AccessReview Immunoglobulins: 25 Years of Immunoinformatics and IMGT-ONTOLOGY
Biomolecules 2014, 4(4), 1102-1139; doi:10.3390/biom4041102
Received: 5 November 2014 / Revised: 2 December 2014 / Accepted: 3 December 2014 / Published: 16 December 2014
Cited by 3 | PDF Full-text (80077 KB) | HTML Full-text | XML Full-text
Abstract
IMGT®, the international ImMunoGeneTics information system® (CNRS and Montpellier University) is the global reference in immunogenetics and immunoinformatics. By its creation in 1989, IMGT® marked the advent of immunoinformatics, which emerged at the interface between immunogenetics and bioinformatics. [...] Read more.
IMGT®, the international ImMunoGeneTics information system® (CNRS and Montpellier University) is the global reference in immunogenetics and immunoinformatics. By its creation in 1989, IMGT® marked the advent of immunoinformatics, which emerged at the interface between immunogenetics and bioinformatics. IMGT® is specialized in the immunoglobulins (IG) or antibodies, T cell receptors (TR), major histocompatibility (MH), and IgSF and MhSF superfamilies. IMGT® has been built on the IMGT-ONTOLOGY axioms and concepts, which bridged the gap between genes, sequences and three-dimensional (3D) structures. The concepts include the IMGT® standardized keywords (identification), IMGT® standardized labels (description), IMGT® standardized nomenclature (classification), IMGT unique numbering and IMGT Colliers de Perles (numerotation). IMGT® comprises seven databases, 15,000 pages of web resources and 17 tools. IMGT® tools and databases provide a high-quality analysis of the IG from fish to humans, for basic, veterinary and medical research, and for antibody engineering and humanization. They include, as examples: IMGT/V-QUEST and IMGT/JunctionAnalysis for nucleotide sequence analysis and their high-throughput version IMGT/HighV-QUEST for next generation sequencing, IMGT/DomainGapAlign for amino acid sequence analysis of IG domains, IMGT/3Dstructure-DB for 3D structures, contact analysis and paratope/epitope interactions of IG/antigen complexes, and the IMGT/mAb-DB interface for therapeutic antibodies and fusion proteins for immunological applications (FPIA). Full article
(This article belongs to the Special Issue Immunoglobulin)
Open AccessReview The Immunoglobulins of Cold-Blooded Vertebrates
Biomolecules 2014, 4(4), 1045-1069; doi:10.3390/biom4041045
Received: 28 September 2014 / Revised: 10 November 2014 / Accepted: 13 November 2014 / Published: 24 November 2014
Cited by 4 | PDF Full-text (24386 KB) | HTML Full-text | XML Full-text
Abstract
Although lymphocyte-like cells secreting somatically-recombining receptors have been identified in the jawless fishes (hagfish and lamprey), the cartilaginous fishes (sharks, skates, rays and chimaera) are the most phylogenetically distant group relative to mammals in which bona fide immunoglobulins (Igs) have been found. [...] Read more.
Although lymphocyte-like cells secreting somatically-recombining receptors have been identified in the jawless fishes (hagfish and lamprey), the cartilaginous fishes (sharks, skates, rays and chimaera) are the most phylogenetically distant group relative to mammals in which bona fide immunoglobulins (Igs) have been found. Studies of the antibodies and humoral immune responses of cartilaginous fishes and other cold-blooded vertebrates (bony fishes, amphibians and reptiles) are not only revealing information about the emergence and roles of the different Ig heavy and light chain isotypes, but also the evolution of specialised adaptive features such as isotype switching, somatic hypermutation and affinity maturation. It is becoming increasingly apparent that while the adaptive immune response in these vertebrate lineages arose a long time ago, it is most definitely not primitive and has evolved to become complex and sophisticated. This review will summarise what is currently known about the immunoglobulins of cold-blooded vertebrates and highlight the differences, and commonalities, between these and more “conventional” mammalian species. Full article
(This article belongs to the Special Issue Immunoglobulin)
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Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Type of Paper: Review
Title: Artificial affinity proteins as ligands of immunoglobulins
Authors: Barbaba Mouratou and Frédéric Pecorari
Affiliation: Institut de Recherche en Santé de l'Université de Nantes. INSERM U892 - CNRS 6299 - CRCNA, 8 quai Moncousu, BP 70721, 44007 Nantes Cedex 1, France; E-Mails: frederic.pecorari@univ-nantes.fr (F.P.); Barbara.Mouratou@univ-nantes.fr (B.M.)
Abstract: A number of natural proteins are known to have affinity and specificity for immunoglobulins. Some of them are widely used as reagents for detection or capture applications, such as Protein G and Protein A, which are able to bind IgG mainly via their Fc region, or Protein L, which recognizes antibodies through light-chain interactions. However, these natural proteins have a defined spectrum of recognition that may not fit specific needs. With the development of combinatorial protein engineering and selection techniques, it has become possible to design artificial affinity proteins with the desired properties. These proteins, termed scaffold proteins, are most often chosen for their stability, ease of engineering and cost-efficient recombinant production in bacteria. In this review, we will focus on scaffold proteins for which immunoglobulin binders have been characterized.

Type of Paper: Review
Title: The immunoglobulins of cold-blooded vertebrates
Authors: Rita Pettinello and Helen Dooley
Affiliation: School of Biological Sciences, University of Aberdeen, Aberdeen. AB24 2TZ. UK;
E-Mails: h.dooley@abdn.ac.uk (H.D.)
Abstract: Although lymphocyte-like cells secreting somatically-recombining receptors have been identified in the jawless fishes (hagfish and lamprey), the cartilaginous fishes (sharks, skates, rays and chimaera) are the most phylogenetically distant group relative to mammals in which bona fide immunoglobulins (Igs) have been found. Studies of the antibodies and humoral immune responses of cartilaginous fishes and other cold-blooded vertebrates (bony fishes, amphibians and reptiles) are not only revealing information about the emergence and roles of the different Ig heavy and light chain isotypes but also the evolution of specialised adaptive features such as isotype switching, somatic hypermutation and affinity maturation. It is becoming increasingly apparent that while the adaptive immune response in these vertebrate lineages may be ancient, it is most definitely not ‘primitive’. This review will summarise what is currently known about the immunoglobulins of cold-blooded vertebrates and highlight the differences, and commonalities, between these and more ‘conventional’ mammalian species.

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