Results 91 to 100 of about 335 (107)

Cytoplasmic and periplasmic expression of recombinant shark VNAR antibody in Escherichia coli

Preparative Biochemistry and Biotechnology, 2019
Shark variable new antigen receptors (VNARs) are known to possess excellent heat-stability, and the long complementarity determining region 3 (CDR3) has permitted it to penetrate into the cleft region of antigens. The number of cysteine (Cys) residues contained within VNAR is greater than in conventional antibodies, entailing disulfide bond formation ...
Herng C. Leow, Katja Fischer, Yee C. Leow, Katleen Braet, Qin Cheng, James McCarthy   +5 more
openaire   +5 more sources

Generation of VNAR Libraries from Immunized Sharks and Selection of Target-Specific Clones

2021
Cartilaginous fishes (sharks, skates, rays, and chimeras) are the most phylogenetically distant lineage relative to mammals in which somatically rearranging immunoglobulins (Igs or antibodies) have also been found. Alongside their conventional (heavy-light chain) isotypes, IgM and IgW, sharks produce the novel isotype, IgNAR, a heavy-chain homodimer ...
openaire   +2 more sources

In Vitro Maturation of a Humanized Shark VNAR Domain to Improve Its Biophysical Properties

2019
VNAR domains are the binding regions of new antigen receptor proteins (IgNAR) which are unique to sharks, skates, and rays (Elasmobranchii). Individual VNAR domains can bind antigens independently and are the smallest reported adaptive immune recognition entities in the vertebrate kingdom.
John, Steven, Obinna C, Ubah, Magdalena, Buschhaus, Marina, Kovaleva, Laura, Ferguson, Andrew J, Porter, Caroline J, Barelle   +6 more
openaire   +2 more sources

Antigen specific VNAR screening in whitespotted bamboo shark (Chiloscyllium plagiosum) with next generation sequencing

Fish and Shellfish Immunology
IgNAR exhibits significant promise in the fields of cancer and anti-virus biotherapies. Notably, the variable regions of IgNAR (VNAR) possess comparable antigen binding affinity with much smaller molecular weight (∼12 kDa) compared to IgNAR. Antigen specific VNAR screening is a changeling work, which limits its application in medicine and therapy ...
Bo Zhong, Guodong Chen
exaly   +3 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
Doreen Könning, Julius Grzeschik, Christian Schröter   +2 more
exaly   +3 more sources

Abstract 576: Shark VNAR single domain-based CAR T cells targeting PD-L1 for cancer therapy

Cancer Research, 2022
Abstract Background: Chimeric antigen receptor (CAR)-T therapy shows great potency against hematological malignancies, whereas it is difficult to transfer CAR T into solid tumors due to lack of appropriate antigenic targets and immunosuppressive tumor microenvironment.
Dan Li, Hejiao English, Jessica Hong, Tianyuzhou Liang, Glenn Merlino, Chi-Ping Day, Mitchell Ho   +6 more
openaire   +1 more source

A shark VNAR-IL-15 fusion protein that suppresses TROP2+ tumor growth

International Journal of Biological Macromolecules
Interleukin-15 (IL-15) holds great promise for cancer immunotherapy because it selectively activates cytotoxic immune cells without expanding regulatory T cells. It also has the potential to convert "cold" tumors into more immunologically active ones. However, its clinical utility is limited by systemic toxicity.
Zhongqiu, Wu, Hao, Li, Yanqing, Wang, Ling, Lu, Yuchao, Gu, Ming-Wei, Wang   +5 more
openaire   +2 more sources

A shark VNAR with cross-species reactivity for serum albumin: Implications for long-term therapeutic applications

International Journal of Biological Macromolecules
Since recombinant biotherapeutics were accepted in the therapeutic drug market, one of the significant challenges has been the insufficient circulatory half-life of many protein and peptide-based drugs. To overcome this pharmacokinetic limitation, serum albumin has been widely utilized as a molecular carrier due to its intrinsic FcRn-mediated recycling
Yuchao Gu
exaly   +3 more sources

Monoclonal Antibodies for the Identification and Purification of vNAR Domains and IgNAR Immunoglobulins from the Horn Shark Heterodontus 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

Characterization and humanization of VNARs targeting human serum albumin from the whitespotted bamboo shark (Chiloscyllium plagiosum)

International Journal of Biological Macromolecules
The Shark-derived immunoglobulin new antigen receptors (IgNARs) have gained increasing attention for their high solubility, exceptional thermal stability, and intricate sequence variation. In this study, we immunized whitespotted bamboo shark (Chiloscyllium plagiosum) to create phage display library of variable domains of IgNAR (VNARs) for screening ...
Weijie, Li, Mingliang, Chen, Tao, Wang, Xin, Feng, Xierui, Jiang, Xiaoning, Dong, Huan, Zhang, Xixiang, Tang, Rui, Tian, Yongyou, Zhang, Zengpeng, Li   +10 more
openaire   +2 more sources