Acta Agriculturae Zhejiangensis ›› 2022, Vol. 34 ›› Issue (10): 2138-2148.DOI: 10.3969/j.issn.1004-1524.2022.10.08
• Animal Science • Previous Articles Next Articles
Preparation and immunoprotection of ORF57 subunit vaccine of Cyprinid herpesvirus 3
LIU Shuya1(
), HE Wenlu2, TAO Yu1, HUANG Shuanghui1, REN Yongqiang1, GENG Yi1, HUANG Xiaoli3, CHEN Defang3, OUYANG Ping1,*()
- 1. College of Veterinary Medicine, Sichuan Agricultural University, Chengdu 611130, China
2. China Portugal International Cooperation Center of Traditional Chinese Medicine, Affiliated Hospital of Traditional Chinese Medicine of Southwest Medical University, Luzhou 646099, Sichuan, China
3. College of Animal Science, Sichuan Agricultural University, Chengdu 611130, China
-
Received:2021-04-20Online:2022-10-25Published:2022-10-26 -
Contact:OUYANG Ping
CLC Number:
Cite this article
LIU Shuya, HE Wenlu, TAO Yu, HUANG Shuanghui, REN Yongqiang, GENG Yi, HUANG Xiaoli, CHEN Defang, OUYANG Ping. Preparation and immunoprotection of ORF57 subunit vaccine of Cyprinid herpesvirus 3[J]. Acta Agriculturae Zhejiangensis, 2022, 34(10): 2138-2148.
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| 引物名称 The name of the primer | 引物序列 Primer sequence (5'-3') | 酶切位点 Restriction enzyme cutting site |
|---|---|---|
| F1 | GGATCCATGGCAGCCAGGGA | BamH Ⅰ |
| R1 | AAGCTTGGATTTGGTTTTGGGTAGGTTC | Hind Ⅲ |
Table 1 Specific primers for CyHV-3 ORF57
| 引物名称 The name of the primer | 引物序列 Primer sequence (5'-3') | 酶切位点 Restriction enzyme cutting site |
|---|---|---|
| F1 | GGATCCATGGCAGCCAGGGA | BamH Ⅰ |
| R1 | AAGCTTGGATTTGGTTTTGGGTAGGTTC | Hind Ⅲ |
Fig.1 ORF57 amino acid sequence composition analysis, affinity/hydrophobicity analysis and prediction of transmembrane domain and signal peptide A, Composition analysis of ORF57 amino acid sequence; B, Affinity/hydrophobicity analysis of ORF57 amino acid sequence; C, Prediction of transmembrane region of ORF57 amino acid sequence by TMHMM; D, Prediction of signal peptide.
Fig.2 Prediction of phosphorylation site of CyHV-3ORF57 amino acid sequence
Fig.3 Secondary structure (A) and tertiary structure (B) of CyHV-3 ORF57 protein h, α-helix; e, β-sheet; t, β-turn; c, Random coil.
Fig.4 The PCR amplication result of the CyHV-3 ORF57 sequence and identification of cloing plasmid In Fig. A: M, DNA Marker 10000; 1, ORF57 amplification product; 2, Negative control. In Fig. B, M, DNA Marker 10000; 1, pMD19-T-CyHV-3-ORF57 double digestion identification; 2, pMD19-T-CyHV-3-ORF57 single digestion identification.
Fig.5 Digestion identification of CyHV-3-ORF57 recombinant expression plasmid1, 2, pET-32a (+); 3, 4, pMD19-T-CyHV-3-ORF57 double digestion.
Fig.6 Expression of recombinant protein ORF57 M, Protein Marker; 1, 2, Induced supernatant of BL21-pET32a by IPTG; 3, 4, Induced precipitation of BL21-pET32a by IPTG.
Fig.7 Purification and Western-blot analysis of ORF57 In Fig. A: M, Protein Marker; 1, Purified protein. In Fig. B: M, Protein Marker; 1, Target protein.
Fig.8 Cumulative survival rate after infection
Fig.9 The carp serum antibody levels detected by ELISA The bars without the same lowercase letters indicated the significant difference(P<0.05).
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