Special Issue "Immunoglobulin"
A special issue of Biomolecules (ISSN 2218-273X).
Deadline for manuscript submissions: closed (31 October 2014)
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
Manuscript Submission Information
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. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short 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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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: firstname.lastname@example.org (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: email@example.com (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.