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- W2545197810 abstract "Peroxinectin (PX) with cell adhesion and per- oxidase activities is important in invertebrate immune responses. We identified a novel PX homolog from Scylla paramamosain (designated as Sp-PX) through transcrip- tome sequencing. The full-length of cDNA sequence was 3,165 bp. And there was a peroxidase domain in the deduced protein sequence. A cell-adhesive sequence (KGD motif) was also found in the N-terminus. The predicted molecular mass of the mature protein is 83.9 kDa, with an estimated pI of 6.21. At the amino acid level, Sp-PX shared much higher similarities with other crustaceans PX pro- teins. And Sp-PX also exhibited some similarities with other peroxidase family members. According to real-time polymerase chain reaction, Sp-PX was mainly distributed in the hemocytes. The gene expression levels in the hemocytes of the normal and white spot syndrome virus (WSSV)- challenged crabs were compared via high-throughput RNA sequencing technology, and the results showed that Sp-PX was upregulated at 48 h post-WSSV challenge. Subse- quently, how Sp-PX responds to WSSV stimulus was explored through time-course experiments. The Sp-PX transcripts dramatically increased and reached the highest level at 12 h post-injection, whereas Sp-PX transcripts were recovered at 96 h post-challenge. Meanwhile, it was found that the WSSV copies proliferated significantly after a period of latent viral infection for 48 h. In addition,Sp-PX transcripts were also upregulated after Vibrio harveyi or Staphylococcus aureus challenge. Overall, Sp-PX not only participates in antibacterial immunity but also plays a cru- cial role in the antiviral immune responses of mud crab at the early stage of WSSV infection." @default.
- W2545197810 created "2016-11-04" @default.
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- W2545197810 date "2013-01-01" @default.
- W2545197810 modified "2023-09-27" @default.
- W2545197810 title "A novel peroxinectin involved in antiviral and antibacterial immunity of mud crab, Scylla paramamosain" @default.
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