Analysis of a cDNA sequence encoding the immunoglobulin heavy chain of the Antarctic teleost Trematomus bernacchii

Coscia, Maria Rosaria; Morea, Veronica; Tramontano, Anna; Oreste, Umberto

doi:10.1006/fsim.1999.0244

Cited by 42 publications

(33 citation statements)

References 38 publications

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“…Thus, the discovery that the notothenioid IgM possesses a C H 2-C H 3 hinge, as shown here and reported previously for another species (Coscia et al, 2000), is intriguing. The increased flexibility of IgM conferred by long hinge-like peptides might be required for proper functioning at cold temperature, as in the case of other molecules (Ciardiello et al, 2000;Fields and Somero, '98).…”

Section: Immunoglobulin Evolution In Notothenioid Fishessupporting

confidence: 81%

“…''Hinge'' peptides Coscia et al (2000) reported that the IgM heavy chain of T. bernacchii contained unusually long C H 2-C H 3 ''hinge'' peptides, which may increase the flexibility of the immunoglobulin molecule. Figure 3 shows that the IgM heavy chains of C. aceratus and N. coriiceps contained similar hinge peptides, although they were four amino acids shorter than the hinge of the T. bernacchii heavy chain.…”

Section: Igh Genes In Antarctic Fishesmentioning

confidence: 99%

“…The only immunological protein characterized at the molecular level has been the m-type immunoglobulin heavy chain (IgM) of Trematomus bernacchii, which possesses a unique ''hinge''-like peptide between the C H 2 and C H 3 domains plausibly to promote flexibility of Ig molecules (Coscia et al, 2000). In order to further investigate whether specific changes have occurred in immunoglobulins under cold temperature and extreme physiological conditions, we have studied the IgM heavy chain genes of two Antarctic notothenioids, an icefish (C. aceratus) and a rockcod (N. coriiceps), with the goal of determining if these changes are adaptive.…”

Section: Introductionmentioning

confidence: 99%

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Positive Darwinian selection operating on the immunoglobulin heavy chain of Antarctic fishes

et al. 2003

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The cooling of the Southern Ocean to the freezing point of seawater (À1.91C) over the past 25 million years played a dominant selective role in the evolution of the Antarctic fish fauna. During this period, the perciform suborder Notothenioidei, which is largely endemic to the Antarctic, diversified and developed numerous cold-adapted characters. In this report, we provide compelling evidence that the immunoglobulin heavy chain (IgH) of the notothenioid fishes has undergone adaptive selection. Two and four IgH clones were isolated, respectively, from spleen cDNA libraries prepared from the Antarctic icefish Chaenocephalus aceratus and the yellowbelly rockcod Notothenia coriiceps. The transmembrane region of the membrane form of the rockcod IgM heavy chain was located at the end of the second constant (C H ) domain, in contrast to other teleost IgMs in which the transmembrane region is located at the end of the third constant domain. Phylogenetic analyses of C H regions revealed that rates of nonsynonymous nucleotide substitution were higher than rates of synonymous nucleotide substitution. Many of the nonsynonymous substitutions introduced charge changes, consistent with positive Darwinian selection acting to adapt the structure of the notothenioid immunoglobulins. The rates of nonsynonymous nucleotide substitutions were higher than the rates of synonymous nucleotide substitutions in complementarity determining regions of variable regions, suggesting that diversity at antigen binding sites is enhanced by genomic and/or somatic selection. Results of Southern blot hybridization experiments were consistent with a translocon type of IgH gene organization reminiscent of bony fishes and tetrapods.

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Section: Immunoglobulin Evolution In Notothenioid Fishessupporting

confidence: 81%

Section: Igh Genes In Antarctic Fishesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Positive Darwinian selection operating on the immunoglobulin heavy chain of Antarctic fishes

et al. 2003

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“…When comparing CH domains of the Antarctic teleost T. bernacchii with several other teleost fish, Coscia et al [14] found that CH2 and CH3 domains are much more diverse than CH1 and CH4, as revealed in the present study. The relative low degree of amino acid identity in CH domains of di#erent fish species, as shown in the present study, may be attributed to the diversity of CH2 and CH3 domains.…”

supporting

confidence: 73%

“…cDNA SEQUENCE OF MANDARIN FISH Ig HEAVY CHAIN adaptation of its Ig molecules to the polar sea environment [14]. The observed similarity between S. chuatsi and P. olivaceus may be accounted for by the close phylogenetic relationship of the two orders to which the two fish belong [15].…”

mentioning

confidence: 99%

cDNA sequence encoding immunoglobulin M heavy chain of the mandarin fish Siniperca chuatsi

Zhang

Nie

Wang

et al. 2003

Fish & Shellfish Immunology

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Immunoglobulin genes and antibody responses in the spotted wolffish (Anarhichas minor Olafsen)

Espelid

Wah

Solem

et al. 2001

Fish & Shellfish Immunology

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Analysis of a cDNA sequence encoding the immunoglobulin heavy chain of the Antarctic teleost Trematomus bernacchii

Cited by 42 publications

References 38 publications

Positive Darwinian selection operating on the immunoglobulin heavy chain of Antarctic fishes

Positive Darwinian selection operating on the immunoglobulin heavy chain of Antarctic fishes

cDNA sequence encoding immunoglobulin M heavy chain of the mandarin fish Siniperca chuatsi

Immunoglobulin genes and antibody responses in the spotted wolffish (Anarhichas minor Olafsen)

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