The immunoglobulins of cartilaginous fishes

Matz, Hanover; Munir, Danish; Logue, James; Dooley, Helen

doi:10.1016/j.dci.2020.103873

Cited by 20 publications

(19 citation statements)

References 87 publications

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“…As already mentioned above, the structure of the H chain gene locus in cartilaginous fish consists of multiple mini-clusters, each composed of one V , two or three D , and one J , followed by one set of C region exons; some clusters are unique because carrying partially ( VD or VJ ) or completely ( VDJ ) recombined germline gene segments. A varying number of clusters (up to 100) has been found in different species [ 2 ].…”

Section: Evolution Of the Antibody Architecturementioning

confidence: 99%

“…In the jawed vertebrates, two different arrangements of the Ig gene locus are known. In cartilaginous fish, multiple “clusters” of V , D , J , and C segments are present [ 2 ], whereas teleosts, similar to other vertebrates, are characterized by the so-called translocon arrangement consisting of multiple sets of V , D , and J gene segments, followed by a single copy of the exons coding for the constant domains. The IgV domain possesses a distinctive feature, that is a region, encoded by a J gene segment, which forms a diglycine bulge and is important for the V domain dimerization.…”

Section: Introductionmentioning

confidence: 99%

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On Origin and Evolution of the Antibody Molecule

Oreste

Ametrano

Coscia

2021

Biology

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The vertebrate immune system provides a powerful defense because of the ability to potentially recognize an unlimited number of pathogens. The antibody molecule, also termed immunoglobulin (Ig) is one of the major mediators of the immune response. It is built up from two types of Ig domains: the variable domain, which provides the capability to recognize and bind a potentially infinite range of foreign substances, and the constant domains, which exert the effector functions. In the last 20 years, advances in our understanding of the molecular mechanisms and structural features of antibody in mammals and in a variety of other organisms have uncovered the underlying principles and complexity of this fundamental molecule. One notable evolutionary topic is the origin and evolution of antibody. Many aspects have been clearly stated, but some others remain limited or obscure. By considering a wide range of prokaryotic and eukaryotic organisms through a literature survey about the topic, we have provided an integrated view of the emergence of antibodies in evolution and underlined the very ancient origins.

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Section: Evolution Of the Antibody Architecturementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

On Origin and Evolution of the Antibody Molecule

Oreste

Ametrano

Coscia

2021

Biology

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“…Each minilocus usually consists of a single V, D (IgH only) J, and constant gene segments (Hinds & Litman, 1986). The number of minilocus present varies depending on the type of immunoglobulin and the species (Matz et al, 2020). In contrast, in the rest of the jawed vertebrates, the immunoglobulin genes sequences have a different organisation, so-called translocon (Flajnik & Kasahara, 2010), in which multiple variables (V), diversity (D), and joining (J) segments are upstream of constant (C) domains (Tonegawa, 1983).…”

Section: Introductionmentioning

confidence: 99%

Immunoglobulins genes in Neoceratodus forsteri and Protopterus annectens explain the origin of the immunoglobulins of the animals that passed ashore

Gambón-Deza

Mirete-Bachiller

2022

Preprint

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Sarcopterygii fish have great evolutionary interest since tetrapods and animals that came ashore arose from them. Within immunology, they can teach us about the emergence of Immunoglobulins D, A/X, and Y already present in amphibians. We have studied the genes of the immunoglobulins in the fish Sarcopterygii Neoceratodus forsteri and Protopterus annectens. In the first fish, we find that several loci for the constant chains of immunoglobulins are distributed in 4 chromosomes. We have found four genes for IgM, a gene for IgW and a gene for IgN. In the second, we find one locus with genes for IgN and IgM and another with one gene for IgW. With these sequences, together with those obtained in other publications, we have been able to study the possible evolution and emergence of immunoglobulin classes. We conclude that there are two evolutionary lines, one focused on IgM and very conservative, and the other focused on IgW, which allows high variability. The W line gave rise to the IgD of 11 domains of reptiles. IgA and IgY are unique since they arose from recombination between the two evolutionary lines. The W line gave origin to the CH1 and CH2 domains, and the M line gave the CH3 and CH4 domains.

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“…SdAbs are derived from the antigen-binding variable domain (VHH) of camel heavy chain–only antibody or the variable domain (vNAR) of cartilaginous fish immunoglobulin new antigen receptor (IgNAR) ( Koenning et al, 2017 ). As the most ancient vertebrates, cartilaginous fish have three immunoglobulin (Ig) isotypes, namely, IgM, IgW, and IgNAR ( Diaz et al, 2002 ; Dooley and Flajnik, 2005 ; Matz et al, 2021 ). IgM and IgNAR are the major antibodies involved in adaptive humoral immune response.…”

Section: Introductionmentioning

confidence: 99%

Bamboo Shark as a Small Animal Model for Single Domain Antibody Production

Wei

Wang

Xiang

et al. 2021

Front. Bioeng. Biotechnol.

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The development of shark single domain antibodies (sdAbs) is hindered by the high cost and tediousness of large-sized shark farming. Here, we demonstrated white-spotted bamboo sharks (Chiloscyllium plagiosum) being cultivated commercially as a promising small animal model to produce sdAbs. We found that immunoglobulin new antigen receptor (IgNAR) presented in bamboo shark genome, transcriptome, and plasma. Four complete IgNAR clusters including variable domains (vNARs) were discovered in the germline, and the Variable–Joining pair from IgNAR1 cluster was dominant from immune repertoires in blood. Bamboo sharks developed effective immune responses upon green fluorescent protein (GFP), near-infrared fluorescent protein iRFP713, and Freund’s adjuvant immunization revealed by elevated lymphocyte counts and antigen specific IgNAR. Before and after immunization, the complementarity determining region 3 (CDR3) of IgNAR were the major determinant of IgNAR diversity revealed by 400-bp deep sequencing. To prove that bamboo sharks could produce high-affinity IgNAR, we isolated anti-GFP and anti-iRFP713 vNARs with up to 0.3 and 3.8 nM affinities, respectively, from immunized sharks. Moreover, we constructed biparatopic vNARs with the highest known affinities (20.7 pM) to GFP and validated the functions of anti-GFP vNARs as intrabodies in mammalian cells. Taken together, our study will accelerate the discovery and development of bamboo shark sdAbs for biomedical industry at low cost and easy operation.

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The immunoglobulins of cartilaginous fishes

Cited by 20 publications

References 87 publications

On Origin and Evolution of the Antibody Molecule

On Origin and Evolution of the Antibody Molecule

Immunoglobulins genes in Neoceratodus forsteri and Protopterus annectens explain the origin of the immunoglobulins of the animals that passed ashore

Bamboo Shark as a Small Animal Model for Single Domain Antibody Production

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