Results 141 to 150 of about 4,347 (168)

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
exaly   +3 more sources

Structure of an IgNAR-AMA1 Complex: Targeting a Conserved Hydrophobic Cleft Broadens Malarial Strain Recognition [PDF]

Structure, 2007
Apical membrane antigen 1 (AMA1) is essential for invasion of erythrocytes and hepatocytes by Plasmodium parasites and is a leading malarial vaccine candidate. Although conventional antibodies to AMA1 can prevent such invasion, extensive polymorphisms within surface-exposed loops may limit the ability of these AMA1-induced antibodies to protect against
Victor A Streltsov, Olan Dolezal, Aditi Gupta   +2 more
exaly   +3 more sources

Shark IgNAR-derived binding domains as potential diagnostic and therapeutic agents

Developmental & Comparative Immunology, 2019
Many of the most successful drugs generated in recent years are based upon monoclonal antibodies (mAbs). However, for some therapeutic and diagnostic applications mAbs are far from ideal; for example, while their relatively large size and inherent receptor binding aids their longevity in vivo it can also limit their tissue penetration.
Hanover, Matz, Helen, Dooley
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

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

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

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.
Md Shaheed Reza, Shuichi Asakawa
exaly   +3 more sources

Variable domain antibodies specific for viral hemorrhagic septicemia virus (VHSV) selected from a randomized IgNAR phage display library

Fish and Shellfish Immunology, 2013
Phage display libraries are used to screen for nucleotide sequences that encode immunoglobulin variable (V) regions that are specific for a target antigen. We previously constructed an immunoglobulin new antigen receptor (IgNAR) phage display library.
Jun-ichi Hikima, Hidehiro Kondo, Ikuo Hirono   +2 more
exaly   +4 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

Selection and characterization of naturally occurring single-domain (IgNAR) antibody fragments from immunized sharks by phage display

Molecular Immunology, 2003
The novel immunoglobulin isotype novel antigen receptor (IgNAR) is found in cartilaginous fish and is composed of a heavy-chain homodimer that does not associate with light chains. The variable regions of IgNAR function as independent domains similar to those found in the heavy-chain immunoglobulins of Camelids. Here, we describe the successful cloning
Martin F Flajnik, Helen Dooley
exaly   +3 more sources