“…The shark Tm and Sec forms of IgM have the same number of IgSF domains [25]. Typically, the heavy chain of both cell-bound and secreted form of this protein is composed of an Ig-superfamily domain corresponding to the V region and four domains of the C region [41]. Most studies showed an antigen-specific increase in both forms of IgM, as well as an increase in the relative ratio of monomeric to pentameric IgM during the immunization course [36].…”
Section: Cartilaginous Fish Ighmentioning
confidence: 99%
“…IgM is usually expressed in eye, gills, intestine, liver, pancreas, peripheral blood leukocytes, spleen and testis but not in brain, heart, kidney, muscle, skin and stomach [41]. IgM has been considered to have important roles in more ancestral clades of vertebrates in addition to antigen binding.…”
Section: Cartilaginous Fish Ighmentioning
confidence: 99%
“…IgD is orthologous to IgW, found only in cartilaginous fish and lungfish, demonstrating that IgD/W, like IgM, was likely present in the ancestor of all living jawed vertebrates [29]. IgW has been detected to be highly expressed in the shark pancreas, much less in muscle, and faintly in gills, kidney, spleen and testis [41]. Cartilaginous fish IgW exists as either a seven-domain or three-domain form [45,49,52], but in lungfish it can have two to at least 11 C domains [53].…”
Section: Cartilaginous Fish Ighmentioning
confidence: 99%
“…Most notably, it is found as a dimer in serum without light chains [58]. IgNAR has been found in intestine, liver, pancreas, peripheral blood leukocytes, spleen and testis [41]. Similarly as in IgM and IgW, IgNAR genes are organized in the multiple cluster format (Figure 1).…”
Section: Cartilaginous Fish Ighmentioning
confidence: 99%
“…Two transmembrane forms of IgNAR have been identified, with either three or five C domains [41,70]. There is much less IgNAR than IgM in serum (0.1–1 mg/mL) [26].…”
The B cell receptor and secreted antibody are at the nexus of humoral adaptive immunity. In this review, we summarize what is known of the immunoglobulin genes of jawed cartilaginous and bony fishes. We focus on what has been learned from genomic or cDNA sequence data, but where appropriate draw upon protein, immunization, affinity and structural studies. Work from major aquatic model organisms and less studied comparative species are both included to define what is the rule for an immunoglobulin isotype or taxonomic group and what exemplifies an exception.
“…The shark Tm and Sec forms of IgM have the same number of IgSF domains [25]. Typically, the heavy chain of both cell-bound and secreted form of this protein is composed of an Ig-superfamily domain corresponding to the V region and four domains of the C region [41]. Most studies showed an antigen-specific increase in both forms of IgM, as well as an increase in the relative ratio of monomeric to pentameric IgM during the immunization course [36].…”
Section: Cartilaginous Fish Ighmentioning
confidence: 99%
“…IgM is usually expressed in eye, gills, intestine, liver, pancreas, peripheral blood leukocytes, spleen and testis but not in brain, heart, kidney, muscle, skin and stomach [41]. IgM has been considered to have important roles in more ancestral clades of vertebrates in addition to antigen binding.…”
Section: Cartilaginous Fish Ighmentioning
confidence: 99%
“…IgD is orthologous to IgW, found only in cartilaginous fish and lungfish, demonstrating that IgD/W, like IgM, was likely present in the ancestor of all living jawed vertebrates [29]. IgW has been detected to be highly expressed in the shark pancreas, much less in muscle, and faintly in gills, kidney, spleen and testis [41]. Cartilaginous fish IgW exists as either a seven-domain or three-domain form [45,49,52], but in lungfish it can have two to at least 11 C domains [53].…”
Section: Cartilaginous Fish Ighmentioning
confidence: 99%
“…Most notably, it is found as a dimer in serum without light chains [58]. IgNAR has been found in intestine, liver, pancreas, peripheral blood leukocytes, spleen and testis [41]. Similarly as in IgM and IgW, IgNAR genes are organized in the multiple cluster format (Figure 1).…”
Section: Cartilaginous Fish Ighmentioning
confidence: 99%
“…Two transmembrane forms of IgNAR have been identified, with either three or five C domains [41,70]. There is much less IgNAR than IgM in serum (0.1–1 mg/mL) [26].…”
The B cell receptor and secreted antibody are at the nexus of humoral adaptive immunity. In this review, we summarize what is known of the immunoglobulin genes of jawed cartilaginous and bony fishes. We focus on what has been learned from genomic or cDNA sequence data, but where appropriate draw upon protein, immunization, affinity and structural studies. Work from major aquatic model organisms and less studied comparative species are both included to define what is the rule for an immunoglobulin isotype or taxonomic group and what exemplifies an exception.
As in mammals, cartilaginous and teleost fishes possess adaptive immune systems based on antigen recognition by immunoglobulins (Ig), T cell receptors (TCR), and major histocompatibility complex molecules (MHC) I and MHC II molecules. Also it is well established that fish B cells and mammalian B cells share many similarities, including Ig gene rearrangements, and production of membrane Ig and secreted Ig forms. This chapter provides an overview of the IgH and IgL chains in cartilaginous and bony fish, including their gene organizations, expression, diversity of their isotypes, and development of the primary repertoire. Furthermore, when possible, we have included summaries of key studies on immune mechanisms such as allelic exclusion, somatic hypermutation, affinity maturation, class switching, and mucosal immune responses.
To develop a multi-antigen-specific immunoglobulin new antigen receptor (IgNAR) variable (V) region phage display library, CDR3 in the V region of IgNAR from banded houndshark (Triakis scyllium) was artificially randomized, and clones specific for hen egg white lysozyme (HEL) were obtained by the biopanning method. The nucleotide sequence of CDR3 in the V region was randomly rearranged by PCR. Randomized CDR3-containing segments of the V region were ligated into T7 phage vector to construct a phage display library and resulted in a phage titer of 3.7 × 10(7) PFU/ml. Forty clones that contained randomized CDR3 inserts were sequenced and shown to have different nucleotide sequences. The HEL-specific clones were screened by biopanning using HEL-coated ELISA plates. After six rounds of screening, nine clones were identified as HEL-specific, eight of which showed a strong affinity to HEL in ELISA compared to a negative control (i.e., empty phage clone). The deduced amino acid sequences of CDR3 from the HEL-specific phage clones fell into four types (I-IV): type I contains a single cysteine residue and type II-IV contain two cysteine residues. These results indicated that the artificially randomized IgNAR library is useful for the rapid isolation of antigen-specific IgNAR V region without immunization of target antigen and showed that it is possible to isolate an antigen-specific IgNAR V region from this library.
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