Humoral immune response of the small-spotted catshark, Scyliorhinus canicula

Crouch, Kathryn; Smith, Lauren E.; Williams, Rebecca; Cao, Wei; Lee, Mike; Jensen, Allan; Dooley, Helen

doi:10.1016/j.fsi.2013.01.025

Cited by 38 publications

(22 citation statements)

References 21 publications

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“…It has been reported that the immune system of the shark offers a good antibody response against different proteins such as: HEL [14], Ebolavirus nucleoprotein [35], TNFα [36,37], ICOSL [38], VEGF [12], malaria PfHRP2 [39], amongst others. However, the IgNAR response of sharks is slower than the similar process observed in mammalian, and obtaining the desired antibodies could last up to 4–6 months [40, 41]. The generation and use of synthetic libraries has decreased the time at which an antibody can be isolated, since it avoids animal immunization [20, 21, 42].…”

Section: Discussionmentioning

confidence: 99%

Synthetic libraries of shark vNAR domains with different cysteine numbers within the CDR3

et al. 2019

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The variable domain of New Antigen Receptors (vNAR) from sharks, present special characteristics in comparison to the conventional antibody molecules such as: small size (12–15 kDa), thermal and chemical stability and great tissue penetration, that makes them a good alternative source as therapeutic or diagnostic agents. Therefore, it is essential to improve techniques used for the development and selection of vNAR antibodies that recognize distinct antigens. The development of synthetic antibody libraries offers a fast option for the generation of antibodies with the desired characteristics. In this work three synthetic antibody libraries were constructed; without cysteines (Cys), with one Cys and with two Cys residues within its CDR3, with the objective of determining whether the presence or absence of Cys in the CDR3 favors the isolation of vNAR clones from a synthetic library. The libraries were validated selecting against six mammalian proteins. At least one vNAR was found for each of the antigens, and a clone coming from the library without Cys in the CDR3 was selected with all the antigens. In vitro angiogenesis assay with the isolated anti-VEGF antibodies, suggest that these vNARs are capable of inhibiting in vitro angiogenesis. In silico analysis of anti-VEGF antibodies showed that vNARs from synthetic libraries could rival antibodies with affinity maturation by in silico modeling.

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Section: Discussionmentioning

confidence: 99%

Synthetic libraries of shark vNAR domains with different cysteine numbers within the CDR3

et al. 2019

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“…Nevertheless, the reactivity of their antigen-binding site is not limited to hidden targets (Figure 2 ), and HcAbs reacting with a broad range of structurally diverse epitopes have been described, including flat surfaces in macromolecules and small molecules ( 23 – 27 ). Since camelids are easier to handle, produce stronger antibody responses than sharks ( 28 , 29 ), and the recombinant expression of the heavy chain variable domain of camelid HcAb is typically higher ( 30 ), these antibody fragments are more frequently used and will be the focus of this review.…”

Section: Camelids and Sharks Have A Special Type Of Antibodies Devoidmentioning

confidence: 99%

Single-Domain Antibodies As Versatile Affinity Reagents for Analytical and Diagnostic Applications

González‐Sapienza¹,

Rossotti²,

Rosa³

2017

Front. Immunol.

144

130

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With just three CDRs in their variable domains, the antigen-binding site of camelid heavy-chain-only antibodies (HcAbs) has a more limited structural diversity than that of conventional antibodies. Even so, this does not seem to limit their specificity and high affinity as HcAbs against a broad range of structurally diverse antigens have been reported. The recombinant form of their variable domain [nanobody (Nb)] has outstanding properties that make Nbs, not just an alternative option to conventional antibodies, but in many cases, these properties allow them to reach analytical or diagnostic performances that cannot be accomplished with conventional antibodies. These attributes include comprehensive representation of the immune specificity in display libraries, easy adaptation to high-throughput screening, exceptional stability, minimal size, and versatility as affinity building block. Here, we critically reviewed each of these properties and highlight their relevance with regard to recent developments in different fields of immunosensing applications.

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“…50,73 For instance Dooley et al and also our group (unpublished results) were unable to detect an antigen-specific IgNAR response after the immunization of the small spotted catshark, Scyliorhinus canicula. 74 Antigen-specific vNAR fragments have also been isolated from non-immunized libraries against a plethora of different targets, including viral targets, cytokines, proteins involved in cancer and arthritis and toxins. 53,62,64,65,70,75,76 1 illustrates vNARs selected against therapeutically relevant targets from immunized and non-immunized origins (Table 1).…”

Section: Selection Of Antigen-specific Vnar Domains From Shark Immune Repertoiresmentioning

confidence: 99%

Structural insights and biomedical potential of IgNAR scaffolds from sharks

Zielonka

Empting

Grzeschik³

et al. 2015

mAbs

113

124

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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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Humoral immune response of the small-spotted catshark, Scyliorhinus canicula

Cited by 38 publications

References 21 publications

Synthetic libraries of shark vNAR domains with different cysteine numbers within the CDR3

Synthetic libraries of shark vNAR domains with different cysteine numbers within the CDR3

Single-Domain Antibodies As Versatile Affinity Reagents for Analytical and Diagnostic Applications

Structural insights and biomedical potential of IgNAR scaffolds from sharks

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