2016
DOI: 10.1016/j.dci.2016.03.009
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The complement system of elasmobranches revealed by liver transcriptome analysis of a hammerhead shark, Sphyrna zygaena

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Cited by 28 publications
(15 citation statements)
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“…BjC1q can also bind mammalian C1r and C1s proteases, as well as human IgG, and thus can replace human C1q to activate the human classical pathway. The C1q molecule further evolved with three different A, B and C subunits, possibly during the diversification of cartilaginous fishes, with clear sequence signatures characterizing their functional evolutionary diversification (Gao et al, 2014; Tariq et al, 2015; Goshima et al, 2016). Although only one C1q, C1r, C1s protein sequence has been obtained from the liver transcriptome of a hammerhead shark, the presence of three C1q chains in the nurse shark has been reported at the protein level, suggesting that C1q could be expressed in extra-hepatic sites in sharks as in mammals (Goshima et al, 2016).…”
Section: The Complement C1q Molecule: From Early Appearance In Evomentioning
confidence: 99%
See 1 more Smart Citation
“…BjC1q can also bind mammalian C1r and C1s proteases, as well as human IgG, and thus can replace human C1q to activate the human classical pathway. The C1q molecule further evolved with three different A, B and C subunits, possibly during the diversification of cartilaginous fishes, with clear sequence signatures characterizing their functional evolutionary diversification (Gao et al, 2014; Tariq et al, 2015; Goshima et al, 2016). Although only one C1q, C1r, C1s protein sequence has been obtained from the liver transcriptome of a hammerhead shark, the presence of three C1q chains in the nurse shark has been reported at the protein level, suggesting that C1q could be expressed in extra-hepatic sites in sharks as in mammals (Goshima et al, 2016).…”
Section: The Complement C1q Molecule: From Early Appearance In Evomentioning
confidence: 99%
“…The C1q molecule further evolved with three different A, B and C subunits, possibly during the diversification of cartilaginous fishes, with clear sequence signatures characterizing their functional evolutionary diversification (Gao et al, 2014; Tariq et al, 2015; Goshima et al, 2016). Although only one C1q, C1r, C1s protein sequence has been obtained from the liver transcriptome of a hammerhead shark, the presence of three C1q chains in the nurse shark has been reported at the protein level, suggesting that C1q could be expressed in extra-hepatic sites in sharks as in mammals (Goshima et al, 2016). A recent study details the C1q sequences in the Chinese goose and the corresponding evolutionary relationships of the three C1q subunits in duck, chicken, bird and alligator (Tariq et al, 2015).…”
Section: The Complement C1q Molecule: From Early Appearance In Evomentioning
confidence: 99%
“…While extremely useful tools for comparative analyses, draft assemblies may often be limited by their fragmented nature, a problem compounded by the large and complex genomes of elasmobranches [ 25 , 26 ]. Several cartilaginous fish transcriptomes are also available [ 6 , 27 36 ], but none include a complete set of immune tissues. For these reasons, one goal of the current study was to generate elasmobranch transcriptome data that includes a full set of immune tissues, in the hope of revealing immune genes missed by other studies.…”
Section: Introductionmentioning
confidence: 99%
“…However, not all fish species contain all three pathways. MBL and ficolin genes have not been identified in any cartilaginous fish studied to date, while MASP2 transcripts are lacking in the elephant shark, little skate ( Leucoraja erinacea ) and catshark ( Scyliorhinus canicular ) (54, 106, 107). In addition, the hammerhead shark contains a MASP2 transcript that contains no serine protease domain, which is necessary to initiate the lectin pathway.…”
Section: Complement Systemmentioning
confidence: 99%