Abstract
BackgroundIn the host immune system, perforin is a cytotoxic effector molecule that eliminate virus-infected and malignant cells. Moreover, some recent studies also imply the involvement of perforin in antibacterial immunity. Common carp (Cyprinus carpio L.), one of the most economically important fish species in China, has a high susceptibility to viruses and bacteria. Thus far, in common carp, no data are available regarding the identification and immunologic function of the perforin.ResultsIn the present study, the cDNA and genomic DNA sequences of three perforin isoform genes were cloned and characterized in common carp, named CcPRF1, CcPRF2 and CcPRF3. Amino acid sequences of the three CcPRFs were quite different, with identities ranged from 37.3 to 39.5%. Phylogenetic analysis showed that three CcPRFs, each in a separate sub-branch, possessed closer evolutionary relationship with other teleost perforins, especially with cyprinid fishes, than higher vertebrates. Expression analysis revealed that each CcPRF gene was differentially expressed in all of the nine tested tissues. During larvae ontogeny, each CcPRF displayed a distinct expression pattern, while with a common expression peak at 22 days post hatching (dph). Moreover, in vivo or in vitro, after stimulation with polyI:C, LPS and Aeromonas hydrophila, each CcPRF was induced significantly, with differential expression dynamics.ConclusionsOur findings suggest that perforin might play significant roles in larval immune system and in the immune defense of common carp against viral and bacterial pathogens. Meantime, the differential expression dynamics seem to imply possible different cellular locations or functional differences across various CcPRF isoforms.
Highlights
In the host immune system, perforin is a cytotoxic effector molecule that eliminate virus-infected and malignant cells
The pores formed by perforin allow granzymes (Gzms), serine proteases stored in cytoplasmic granules of natural killer (NK)/cytotoxic T lymphocytes (CTLs) cells with perforin, into the cytosol of target cells [13], which will induce the activation of proapoptotic pathways and DNA degradation
Protein domain prediction showed that each CcPRF contained a signal peptide domain, a MACPF domain and a CalB domain (Fig. 1d)
Summary
In the host immune system, perforin is a cytotoxic effector molecule that eliminate virus-infected and malignant cells. Natural killer (NK) cells and CD8+ cytotoxic T lymphocytes (CD8+ CTLs) play important roles in the immune-cytotoxic system against virus-infected and tumor cells. In this process, it has been confirmed that perforin plays a crucial role [1]. Pore formation of perforin depends on these two characteristic domains, in which MACPF is related to pore-forming [9, 10] and the CalB motif is related to calcium-dependent membrane binding to target cells [11]. The pores formed by perforin allow granzymes (Gzms), serine proteases stored in cytoplasmic granules of NK/CTL cells with perforin, into the cytosol of target cells [13], which will induce the activation of proapoptotic pathways and DNA degradation
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