Results 131 to 140 of about 1,618 (161)

Organ-specific repertoires of IgNAR gene in a cartilaginous fish

Fish & Shellfish Immunology
Cartilaginous fish possess one of the most ancient adaptive immune systems, and they uniquely produce the heavy chain-only antibody, immunoglobulin novel antigen receptor (IgNAR). In this study, we explored the mRNA transcription of genes related to antibody production and IgNAR diversity in various organs in banded houndsharks.
Soichiro Yoshizawa, Kayo Konishi, Keiichiro Koiwai, Ikuo Hirono, Hidehiro Kondo   +4 more
openaire   +2 more sources

Generation of Semi-Synthetic Shark IgNAR Single-Domain Antibody Libraries

2017
Besides classical antibodies with the composition of heavy and light chains, sharks produce a unique heavy chain only isotype, termed Immunoglobulin New Antigen Receptor (IgNAR), in which antigen binding is solely mediated by a single domain, referred to as vNAR.
Julius, Grzeschik, Doreen, Könning, Steffen C, Hinz, Simon, Krah, Christian, Schröter, Martin, Empting, Harald, Kolmar, Stefan, Zielonka   +7 more
openaire   +2 more sources

Construction of Histidine-Enriched Shark IgNAR Variable Domain Antibody Libraries for the Isolation of pH-Sensitive vNAR Fragments

Methods in Molecular Biology, 2018
The adaptive immune system of sharks comprises a heavy chain-only antibody isotype, referred to as immunoglobulin new antigen receptor (IgNAR). Antigen binding in case of IgNAR antibodies is mediated by a single variable domain (vNAR). Due to their inherent beneficial biophysical properties, such as small size and high thermal stability combined with a
Stefan Zielonka, Harald Kolmar, Doreen Könning   +2 more
exaly   +3 more sources

Selection and affinity maturation of IgNAR variable domains targeting Plasmodium falciparum AMA1

Proteins: Structure, Function, and Bioinformatics, 2004
AbstractThe new antigen receptor (IgNAR) is an antibody unique to sharks and consists of a disulphide‐bonded dimer of two protein chains, each containing a single variable and five constant domains. The individual variable (VNAR) domains bind antigen independently, and are candidates for the smallest antibody‐based immune recognition units.
Nuttall, S. D., Hudson, P. J., Irving, Robert., Foley, Michael., Anders, Robin., Casey, Joanne., Coley, Andrew., Hattarki, Meghan., Doughty, Larissa., Carmichael, Jennifer Ann., Krishnan, Usha., Harris, Karen Sandra.   +11 more
openaire   +2 more sources

Isolation and characterization of an IgNAR variable domain specific for the human mitochondrial translocase receptor Tom70

European Journal of Biochemistry, 2003
The new antigen receptor (IgNAR) from sharks is a disulphide bonded dimer of two protein chains, each containing one variable and five constant domains, and functions as an antibody. In order to assess the antigen‐binding capabilities of isolated IgNAR variable domains (VNAR), we have constructed an in vitro library incorporating synthetic CDR3 regions
Pearson, Kylie., Doughty, Larissa., Krishnan, Usha., Nuttall, Stewart D., Hudson, Peter., Irving, Robert., Carmichael, Jennifer Ann., Hattarki, Meghan., Hoogenraad, Nick., Ryan, Michael.   +9 more
openaire   +2 more sources

Overview and Discovery of IgNARs and Generation of VNARs

2012
Immunoglobulin new antigen receptors (IgNARs) from sharks are a distinct class of immune receptors, consisting of homodimers with no associated light chains. Antigen binding is encapsulated within single VNAR immunoglobulin domains of 13-14 kDa in size.
openaire   +2 more sources

Shark IgNAR antibody mimotopes target a murine immunoglobulin through extended CDR3 loop structures

Proteins: Structure, Function, and Bioinformatics, 2007
AbstractMimotopes mimic the three‐dimensional topology of an antigen epitope, and are frequently recognized by antibodies with affinities comparable to those obtained for the original antibody–antigen interaction. Peptides and anti‐idiotypic antibodies are two classes of protein mimotopes that mimic the topology (but not necessarily the sequence) of ...
Simmons, D. P., Streltsov, Victor A., Dolezal, Olan., Hudson, Peter., Coley, Andrew Mark., Foley, Michael., Proll, D., Nuttall, Stewart D.   +7 more
openaire   +2 more sources

Rapid isolation of IgNAR variable single-domain antibody fragments from a shark synthetic library

Molecular Immunology, 2007
The immunoglobulin isotype IgNAR (Novel Antigen Receptor) was discovered in the serum of the nurse shark (Ginglymostoma cirratum) and wobbegong shark (Orectolobus maculates) as a homodimer of two protein chains, each composed of a single variable domain (V) domain and five constant domains.
Cui-Ying, Shao, Chris J, Secombes, Andrew J, Porter   +2 more
openaire   +2 more sources

Construction of an Artificially Randomized IgNAR Phage Display Library: Screening of Variable Regions that Bind to Hen Egg White Lysozyme

Marine Biotechnology, 2012
To develop a multi-antigen-specific immunoglobulin new antigen receptor (IgNAR) variable (V) region phage display library, CDR3 in the V region of IgNAR from banded houndshark (Triakis scyllium) was artificially randomized, and clones specific for hen egg white lysozyme (HEL) were obtained by the biopanning method.
Hidehiro Kondo, Tae Sung Jung, Ikuo Hirono   +2 more
exaly   +3 more sources

Isolation of a pH-Sensitive IgNAR Variable Domain from a Yeast-Displayed, Histidine-Doped Master Library

Marine Biotechnology, 2016
In recent years, engineering of pH-sensitivity into antibodies as well as antibody-derived fragments has become more and more attractive for biomedical and biotechnological applications. Herein, we report the isolation of the first pH-sensitive IgNAR variable domain (vNAR), which was isolated from a yeast-displayed, semi-synthetic master library.
Doreen, Könning, Stefan, Zielonka, Carolin, Sellmann, Christian, Schröter, Julius, Grzeschik, Stefan, Becker, Harald, Kolmar   +6 more
openaire   +2 more sources