Results 151 to 160 of about 4,347 (168)

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

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

The Shark Strikes Twice: Hypervariable Loop 2 of Shark IgNAR Antibody Variable Domains and Its Potential to Function as an Autonomous Paratope [PDF]

Marine Biotechnology, 2015
In this present study, we engineered hypervariable loop 2 (HV2) of the IgNAR variable domain in a way that it solely facilitates antigen binding, potentially functioning as an autonomous paratope. For this, the surface-exposed loop corresponding to HV2 was diversified and antigen-specific variable domain of IgNAR antibody (vNAR) molecules were isolated
Stefan Zielonka, Martin Empting, Harald Kolmar   +2 more
exaly   +4 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.
Jun-ichi Hikima, Tae Sung Jung, Hidehiro Kondo   +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

In vitro improvement of a shark IgNAR antibody by Qβ replicase mutation and ribosome display mimics in vivo affinity maturation

Immunology Letters, 2006
We have employed a novel mutagenesis system, which utilizes an error-prone RNA dependent RNA polymerase from Qbeta bacteriophage, to create a diverse library of single domain antibody fragments based on the shark IgNAR antibody isotype. Coupling of these randomly mutated mRNA templates directly to the translating ribosome allowed in vitro selection of ...
Victor A Streltsov
exaly   +3 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
exaly   +3 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

Monoclonal Antibodies for the Identification and Purification of vNAR Domains and IgNAR Immunoglobulins from the Horn SharkHeterodontus francisci

Hybridoma, 2011
In addition to conventional antibodies, cartilaginous fish have evolved a distinctive type of immunoglobulin, designated as IgNAR, which lacks the light polypeptide chains and is composed entirely by heavy chains. IgNAR molecules can be manipulated by molecular engineering to produce the variable domain of a single heavy chain polypeptide (vNARs ...
Karla, Juarez, Gudrun, Dubberke, Pavel, Lugo, Friedrich, Koch-Nolte, Friedrich, Buck, Friedrich, Haag, Alexei, Licea   +6 more
openaire   +2 more sources

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

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
Doreen, Könning, Steffen, Hinz, Julius, Grzeschik, Christian, Schröter, Simon, Krah, Stefan, Zielonka, Harald, Kolmar   +6 more
openaire   +2 more sources