Results 101 to 110 of about 1,420 (126)

Maturation of Shark Single-domain (IgNAR) Antibodies: Evidence for Induced-fit Binding

Journal of Molecular Biology, 2007
Sharks express an unusual heavy-chain isotype called IgNAR, whose variable regions bind antigen as independent soluble domains. To further probe affinity maturation of the IgNAR response, we structurally characterized the germline and somatically matured versions of a type II variable (V) region, both in the presence and absence of its antigen, hen egg-
Robyn L, Stanfield, Helen, Dooley, Petra, Verdino, Martin F, Flajnik, Ian A, Wilson   +4 more
openaire   +2 more sources

Phage Display Derived IgNAR V Region Binding Domains for Therapeutic Development

Current Pharmaceutical Design, 2017
Phage display technology has revolutionized the science of drug discovery by transforming the generation and manipulation of ligands, such as antibody fragments, enzymes, and peptides. The basis of this technology is the expression of recombinant proteins or peptides fused to a phage coat protein, and subsequent isolation of ligands based on a variety ...
Obinna C, Ubah, Caroline J, Barelle, Magdalena J, Buschhaus, Andrew J, Porter   +3 more
openaire   +2 more sources

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

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

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

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

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, Doreen Könning   +2 more
exaly   +4 more sources

Transcriptomic analysis of immunoglobulin novel antigen receptor (IgNAR) heavy chain constant domains of brownbanded bamboo shark (Chiloscyllium punctatum)

Fish and Shellfish Immunology, 2019
Cartilaginous fish are the evolutionarily oldest group of animals which possess antibodies, T cell receptors and major histocompatibility complex (MHC). The immunoglobulin novel antigen receptor (IgNAR) found in cartilaginous fish is a heavy chain homodimer which lacks light chain.
Shōichi Hosoya, Md Shaheed Reza, Shuichi Asakawa   +2 more
exaly   +3 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