Structural insights and biomedical potential of IgNAR scaffolds from sharks

Stefan Zielonka; Martin Empting; Julius Grzeschik; Doreen Könning; Caroline Barelle; Harald Kolmar

doi:10.4161/19420862.2015.989032

Structural insights and biomedical potential of IgNAR scaffolds from sharks

Stefan Zielonka, Martin Empting, Julius Grzeschik, Doreen Könning, Caroline Barelle, Harald Kolmar

Medical Sciences

Research output: Contribution to journal › Article › peer-review

103 Citations (Scopus)

7 Downloads (Pure)

Abstract

Abstract In addition to antibodies with the classical composition of heavy and light chains, the adaptive immune repertoire of sharks also includes a heavy-chain only isotype, where antigen binding is mediated exclusively by a small and highly stable domain, referred to as vNAR. In recent years, due to their high affinity and specificity combined with their small size, high physicochemical stability and low-cost of production, vNAR fragments have evolved as promising target-binding scaffolds that can be tailor-made for applications in medicine and biotechnology. This review highlights the structural features of vNAR molecules, addresses aspects of their generation using immunization or in vitro high throughput screening methods and provides examples of therapeutic, diagnostic and other biotechnological applications.

Original language	English
Pages (from-to)	15-25
Number of pages	11
Journal	mAbs
Volume	7
Issue number	1
Early online date	18 Dec 2014
DOIs	https://doi.org/10.4161/19420862.2015.989032
Publication status	Published - 2015

Keywords

antibody technology
biologic therapeutic
heavy chain antibody
IgNAR
shark
single chain binding domain
CDR
complementary-determining region
HV
hypervariable region
immunoglobin new antigen receptor
IgNAR V domain
variable domain of IgNAR
mAbs
monoclonal antibodies
scFv
single chain variable fragment
VL
variable domain of the light chain
VH
variable domain of the heavy chain
VHH
variable domain of camelid heavy chain antibodies
vNAR

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10.4161/19420862.2015.989032Licence: CC BY-NC

Structural insights and biomedical potential of IgNAR scaffolds from sharks
This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.
Final published version, 861 KBLicence: CC BY-NC

Cite this

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title = "Structural insights and biomedical potential of IgNAR scaffolds from sharks",

abstract = "Abstract In addition to antibodies with the classical composition of heavy and light chains, the adaptive immune repertoire of sharks also includes a heavy-chain only isotype, where antigen binding is mediated exclusively by a small and highly stable domain, referred to as vNAR. In recent years, due to their high affinity and specificity combined with their small size, high physicochemical stability and low-cost of production, vNAR fragments have evolved as promising target-binding scaffolds that can be tailor-made for applications in medicine and biotechnology. This review highlights the structural features of vNAR molecules, addresses aspects of their generation using immunization or in vitro high throughput screening methods and provides examples of therapeutic, diagnostic and other biotechnological applications.",

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author = "Stefan Zielonka and Martin Empting and Julius Grzeschik and Doreen K{\"o}nning and Caroline Barelle and Harald Kolmar",

year = "2015",

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AU - Zielonka, Stefan

AU - Empting, Martin

AU - Grzeschik, Julius

AU - Könning, Doreen

AU - Barelle, Caroline

AU - Kolmar, Harald

PY - 2015

Y1 - 2015

N2 - Abstract In addition to antibodies with the classical composition of heavy and light chains, the adaptive immune repertoire of sharks also includes a heavy-chain only isotype, where antigen binding is mediated exclusively by a small and highly stable domain, referred to as vNAR. In recent years, due to their high affinity and specificity combined with their small size, high physicochemical stability and low-cost of production, vNAR fragments have evolved as promising target-binding scaffolds that can be tailor-made for applications in medicine and biotechnology. This review highlights the structural features of vNAR molecules, addresses aspects of their generation using immunization or in vitro high throughput screening methods and provides examples of therapeutic, diagnostic and other biotechnological applications.

AB - Abstract In addition to antibodies with the classical composition of heavy and light chains, the adaptive immune repertoire of sharks also includes a heavy-chain only isotype, where antigen binding is mediated exclusively by a small and highly stable domain, referred to as vNAR. In recent years, due to their high affinity and specificity combined with their small size, high physicochemical stability and low-cost of production, vNAR fragments have evolved as promising target-binding scaffolds that can be tailor-made for applications in medicine and biotechnology. This review highlights the structural features of vNAR molecules, addresses aspects of their generation using immunization or in vitro high throughput screening methods and provides examples of therapeutic, diagnostic and other biotechnological applications.

KW - antibody technology

KW - biologic therapeutic

KW - heavy chain antibody

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KW - single chain binding domain

KW - CDR

KW - complementary-determining region

KW - HV

KW - hypervariable region

KW - immunoglobin new antigen receptor

KW - IgNAR V domain

KW - variable domain of IgNAR

KW - mAbs

KW - monoclonal antibodies

KW - scFv

KW - single chain variable fragment

KW - VL

KW - variable domain of the light chain

KW - VH

KW - variable domain of the heavy chain

KW - VHH

KW - variable domain of camelid heavy chain antibodies

KW - vNAR

U2 - 10.4161/19420862.2015.989032

DO - 10.4161/19420862.2015.989032

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VL - 7

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JO - mAbs

JF - mAbs

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ER -

Structural insights and biomedical potential of IgNAR scaffolds from sharks

Abstract

Keywords

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