Selection and Characterization of Anti-idiotypic Shark Antibody Domains

Könning, Doreen; Zielonka, Stefan; Kaempffe, Anna; Jäger, Sebastian; Kolmar, Harald; Schröter, Christian

doi:10.1007/978-1-4939-9853-1_11

Cited by 2 publications

(4 citation statements)

References 33 publications

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“…The desired immunogenicity in humans is exhibited by lowering the differences between the natural IgG and bispecific antibody format [ 17 , 43 , 44 , 45 ]. The engineered full-length mAbs give rise to reduction into single-chain Fv fragments (scFvs) that retain the binding specificity of the parent antibody [ 46 , 47 , 48 ], thus leading to low immunogenicity [ 49 ] as well as a potentially unique molecule to be used especially in cancer treatment [ 46 ].…”

Section: Viability Of Vnar In Relation With Immunogenicitymentioning

confidence: 99%

“…There are many residues in IgG which are not available in VNAR, and thus making it the smallest antibody fragment [ 48 , 61 ]. The long CDR3 gives the VNAR uniqueness to be able to target a small epitope that can be easily reached by conventional IgG.…”

Section: Strength Of Vnar Domain Over Traditional Mabsmentioning

confidence: 99%

“…The binding-specific activity of VNAR can be attained even after exposure to temperature up to 95 °C [ 61 ]. Besides, VNAR exhibited high physicochemical stability [ 48 ]. This feature is desirable for applications of VNAR than traditional antibodies in a therapeutic and biotechnological setup.…”

Section: Strength Of Vnar Domain Over Traditional Mabsmentioning

confidence: 99%

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Shark New Antigen Receptor (IgNAR): Structure, Characteristics and Potential Biomedical Applications

Juma

Gong

et al. 2021

Cells

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Shark is a cartilaginous fish that produces new antigen receptor (IgNAR) antibodies. This antibody is identified with a similar human heavy chain but dissimilar sequences. The variable domain (VNAR) of IgNAR is stable and small in size, these features are desirable for drug discovery. Previous study results revealed the effectiveness of VNAR as a single molecule or a combination molecule to treat diseases both in vivo and in vitro with promising clinical applications. We showed the first evidence of IgNAR alternative splicing from spotted bamboo shark (Chiloscyllium plagiosum), broadening our understanding of the IgNARs characteristics. In this review, we summarize the discoveries on IgNAR with a focus on its advantages for therapeutic development based on its peculiar biochemistry and molecular structure. Proper applications of IgNAR will provide a novel avenue to understand its special presence in cartilaginous fishes as well as designing a number of drugs for undefeated diseases.

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Section: Viability Of Vnar In Relation With Immunogenicitymentioning

confidence: 99%

Section: Strength Of Vnar Domain Over Traditional Mabsmentioning

confidence: 99%

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Shark New Antigen Receptor (IgNAR): Structure, Characteristics and Potential Biomedical Applications

Juma

Gong

et al. 2021

Cells

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“…The structurally related Ab fragments of shark origin (vNARs) as well as the small alternative scaffold of affimers seem also suitable for isolating anti-idiotypic binders specific for IgG paratopes starting from synthetic/semi-synthetic libraries. They have been exploited to obtain reagents selective for therapeutic Abs [ 25 , 26 , 27 ] that could be employed, for instance, for pharmacokinetic studies and to detect the concentration of circulating Abs in treated patients. In these cases, it was not evaluated whether anti-idiotypic binders were mimics of the antigens, despite anti-idiotypic Abs can be exploited as immunogenic factors to induce an epitope-specific response.…”

Section: Discussionmentioning

confidence: 99%

Nanobodies Selectively Binding to the Idiotype of a Dengue Virus Neutralizing Antibody Do Not Necessarily Mimic the Viral Epitope

et al. 2023

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Vaccination against dengue virus is challenged by the fact that a generic immune response can induce antibody-dependent-enhancement (ADE) in secondary infections. Only some antibodies targeting a quaternary epitope formed by the dimerization of the virus protein E possess sufficient neutralizing capacity. Therefore, the immunization with anti-idiotypic antibodies of neutralizing antibodies might represent a safe vaccination strategy. Starting from a large pre-immune library, we succeeded in isolating a wide set of anti-idiotypic nanobodies characterized by selective and strong binding to the paratope of the neutralizing antibody 1C10. However, the mice immunized with such constructs did not produce effective antibodies, despite at least some of them eliciting an immune response selective for the nanobody variable regions. The results suggest that complex conformational epitopes might be difficult to be recreated by anti-idiotypic structures. The selection process of the anti-idiotypic candidates might be optimized by applying epitope mapping and modeling approaches aimed at identifying the key residues that is necessary to bind to trigger selective immune response.

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Selection and Characterization of Anti-idiotypic Shark Antibody Domains

Cited by 2 publications

References 33 publications

Shark New Antigen Receptor (IgNAR): Structure, Characteristics and Potential Biomedical Applications

Shark New Antigen Receptor (IgNAR): Structure, Characteristics and Potential Biomedical Applications

Nanobodies Selectively Binding to the Idiotype of a Dengue Virus Neutralizing Antibody Do Not Necessarily Mimic the Viral Epitope

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