[1] |
PALINSKI R, PIÑEYRO P, SHANG P C, et al. A novel porcine circovirus distantly related to known circoviruses is associated with porcine dermatitis and nephropathy syndrome and reproductive failure[J]. Journal of Virology, 2016, 91(1): e01879-e01816.
|
[2] |
KROEGER M, TEMEEYASEN G, PIÑEYRO P E. Five years of porcine circovirus 3: what have we learned about the clinical disease, immune pathogenesis, and diagnosis[J]. Virus Research, 2022, 314: 198764.
|
[3] |
CHEN S, ZHANG L Y, LI X, et al. Recent progress on epidemiology and pathobiology of porcine circovirus 3[J]. Viruses, 2021, 13(10): 1944.
|
[4] |
TURLEWICZ-PODBIELSKA H, AUGUSTYNIAK A, POMORSKA-MÓL M. Novel porcine circoviruses in view of lessons learned from porcine circovirus type 2-epidemiology and threat to pigs and other species[J]. Viruses, 2022, 14(2): 261.
|
[5] |
SAPORITI V, FRANZO G, SIBILA M, et al. Porcine circovirus 3 (PCV-3) as a causal agent of disease in swine and a proposal of PCV-3 associated disease case definition[J]. Transboundary and Emerging Diseases, 2021, 68(6): 2936-2948.
|
[6] |
ZHAO L L, ROSARIO K, BREITBART M, et al. Eukaryotic circular rep-encoding single-stranded DNA (CRESS DNA) viruses: ubiquitous viruses with small genomes and a diverse host range[J]. Advances in Virus Research, 2019, 103: 71-133.
|
[7] |
JIANG H J, WANG D, WANG J, et al. Induction of porcine dermatitis and nephropathy syndrome in piglets by infection with porcine circovirus type 3[J]. Journal of Virology, 2019, 93(4): e02045-e02018.
|
[8] |
RUIZ A, SAPORITI V, HUERTA E, et al. Exploratory study of the frequency of detection and tissue distribution of Porcine circovirus 3 (PCV-3) in pig fetuses at different gestational ages[J]. Pathogens, 2022, 11(2): 118.
|
[9] |
JIANG Z X, WU J J, JIANG M, et al. A novel technique for constructing infectious cloning of type 3 porcine circovirus[J]. Frontiers in Microbiology, 2020, 11: 1067.
|
[10] |
王喆. 猪圆环病毒3型衣壳蛋白的表达及感染性克隆的建立[D]. 南昌: 江西农业大学, 2019.
|
|
WANG Z. Expression of porcine circovirus type 3 capsid protein and establishment of infectious clone[D]. Nanchang: Jiangxi Agricultural University, 2019. (in Chinese with English abstract)
|
[11] |
耿世超. 猪圆环病毒3型在浙江的流行及其核衣壳蛋白诱导细胞自噬的机制[D]. 杭州: 浙江大学, 2020.
|
|
GENG S C. Prevalence of porcine circovirus type 3 in Zhejiang and mechanism of cell autophagy induced by its capsid protein[D]. Hangzhou: Zhejiang University, 2020. (in Chinese with English abstract)
|
[12] |
祝羊. PCV3感染性克隆质粒的构建与病毒拯救研究[D]. 贵阳: 贵州大学, 2022.
|
|
ZHU Y. Construction of infectious clone plasmid of PCV3 and study on virus rescue[D]. Guiyang: Guizhou University, 2022. (in Chinese with English abstract)
|
[13] |
JIANG H J, WEI L, WANG D, et al. ITRAQ-based quantitative proteomics reveals the first proteome profiles of piglets infected with porcine circovirus type 3[J]. Journal of Proteomics, 2020, 212: 103598.
|
[14] |
ZHU B L, ZHOU Y S, XU F, et al. Porcine circovirus type 2 induces autophagy via the AMPK/ERK/TSC2/mTOR signaling pathway in PK-15 cells[J]. Journal of Virology, 2012, 86(22): 12003-12012.
|
[15] |
朱炳林. 猪圆环病毒2型感染诱导PK-15细胞自噬机制研究[D]. 杭州: 浙江大学, 2012.
|
|
ZHU B L. Mechanisms of autophagy in PK-15 cells induced by porcine circovirus type 2 infection[D]. Hangzhou: Zhejiang University, 2012. (in Chinese with English abstract)
|
[16] |
GU Y X, QI B Z, ZHOU Y S, et al. Porcine circovirus type 2 activates CaMMKβ to initiate autophagy in PK-15 cells by increasing cytosolic calcium[J]. Viruses, 2016, 8(5): 135.
|
[17] |
GENG S C, LI X L, FANG W H. Porcine circovirus 3 capsid protein induces autophagy in HEK293T cells by inhibiting phosphorylation of the mammalian target of rapamycin[J]. Journal of Zhejiang University-SCIENCE B, 2020, 21(7): 560-570.
|
[18] |
PAN Y H, LI P F, JIA R Y, et al. Regulation of apoptosis during porcine circovirus type 2 infection[J]. Frontiers in Microbiology, 2018, 9: 2086.
|
[19] |
李周勉. PCV3 Cap蛋白序列分析及其对细胞凋亡影响的研究[D]. 长沙: 湖南农业大学, 2020.
|
|
LI Z M. The study of sequence analysis of PCV3 Cap and its effect on cell apotosis[D]. Changsha: Hunan Agricultural University, 2020. (in Chinese with English abstract)
|
[20] |
CHEN X X, REN F, HESKETH J, et al. Selenium blocks porcine circovirus type 2 replication promotion induced by oxidative stress by improving GPx1 expression[J]. Free Radical Biology and Medicine, 2012, 53(3): 395-405.
|
[21] |
CHEN X X, REN F, HESKETH J, et al. Interaction of porcine circovirus type 2 replication with intracellular redox status in vitro[J]. Redox Report, 2013, 18(5): 186-192.
|
[22] |
SUN R J, DENG Z F, HAN X A, et al. Porcine circovirus 2 manipulates the PERK-ERO1α axis of the endoplasmic reticulum to favor its replication by derepressing viral DNA from HMGB1 sequestration within nuclei[J]. Journal of Virology, 2021, 95(19): e0100921.
|
[23] |
NIU G Y, CHEN S, LI X, et al. Advances in crosstalk between porcine circoviruses and host[J]. Viruses, 2022, 14(7): 1419.
|
[24] |
LIU X H, SHEN H Q, ZHANG X M, et al. Porcine circovirus type 3 capsid protein induces NF-κB activation and upregulates pro-inflammatory cytokine expression in HEK-293T cells[J]. Archives of Virology, 2021, 166(8): 2141-2149.
|
[25] |
李萌. PCV3 Cap和Rep诱导相关细胞因子mRNA转录及IL-10表达机制的初步研究[D]. 长沙: 湖南农业大学, 2020.
|
|
LI M. PCV3 Cap and Rep protein induce related cytokine mRNA transcription and IL-10 expression mechanism[D]. Changsha: Hunan Agricultural University, 2020. (in Chinese with English abstract)
|
[26] |
申翰钦. 猪圆环病毒3型Cap调控IFN-β及其下游通路的作用机制研究[D]. 广州: 华南农业大学, 2019.
|
|
SHEN H Q. Mechanisms of inhibition of IFN-β induction and its down stream signaling by porcine circovirus type 3 Cap[D]. Guangzhou: South China Agricultural University, 2019. (in Chinese with English abstract)
|
[27] |
ZHANG P F, SHEN H Q, LIU X H, et al. Porcine circovirus type 3 Cap inhibits type I interferon induction through interaction with G3BP1[J]. Frontiers in Veterinary Science, 2020, 7: 594438.
|
[28] |
SHEN H Q, LIU X H, ZHANG P F, et al. Porcine circovirus 3 Cap inhibits type I interferon signaling through interaction with STAT2[J]. Virus Research, 2020, 275: 197804.
|
[29] |
SONG J W, HOU L, WANG D, et al. Nucleolar phosphoprotein NPM1 interacts with porcine circovirus type 3 Cap protein and facilitates viral replication[J]. Frontiers in Microbiology, 2021, 12: 679341.
|
[30] |
ZHANG H H, HU W Q, LI J Y, et al. Novel circovirus species identified in farmed pigs designated as Porcine circovirus 4, Hunan Province, China[J]. Transboundary and Emerging Diseases, 2020, 67(3): 1057-1061.
|
[31] |
CHEN N H, XIAO Y Z, LI X S, et al. Development and application of a quadruplex real-time PCR assay for differential detection of porcine circoviruses (PCV1 to PCV4) in Jiangsu Province of China from 2016 to 2020[J]. Transboundary and Emerging Diseases, 2021, 68(3): 1615-1624.
|
[32] |
HA Z, YU C D, XIE C Z, et al. Retrospective surveillance of porcine circovirus 4 in pigs in Inner Mongolia, China, from 2016 to 2018[J]. Archives of Virology, 2021, 166(7): 1951-1959.
|
[33] |
TIAN R B, ZHAO Y, CUI J T, et al. Molecular detection and phylogenetic analysis of Porcine circovirus 4 in Henan and Shanxi Provinces of China[J]. Transboundary and Emerging Diseases, 2021, 68(2): 276-282.
|
[34] |
NGUYEN V G, DO H Q, HUYNH T M L, et al. Molecular-based detection, genetic characterization and phylogenetic analysis of porcine circovirus 4 from Korean domestic swine farms[J]. Transboundary and Emerging Diseases, 2022, 69(2): 538-548.
|
[35] |
ZHOU J W, WANG Y X, ZHOU L Y, et al. Interaction network of porcine circovirus type 3 and 4 capsids with host proteins[J]. Viruses, 2022, 14(5): 939.
|
[36] |
DHINDWAL S, AVILA B, FENG S S, et al. Porcine circovirus 2 uses a multitude of weak binding sites to interact with heparan sulfate, and the interactions do not follow the symmetry of the capsid[J]. Journal of Virology, 2019, 93(6): e02222-e02218.
|
[37] |
SHI R H, HOU L, WEI L, et al. Porcine circovirus type 3 enters into PK15 cells through clathrin-and dynamin-2-mediated endocytosis in a Rab5/Rab7 and pH-dependent fashion[J]. Frontiers in Microbiology, 2021, 12: 636307.
|
[38] |
MOU C X, WANG M M, PAN S N, et al. Identification of nuclear localization signals in the ORF2 protein of porcine circovirus type 3[J]. Viruses, 2019, 11(12): 1086.
|
[39] |
ZHOU J W, DAI Y D, LIN C, et al. Nucleolar protein NPM1 is essential for circovirus replication by binding to viral capsid[J]. Virulence, 2020, 11(1): 1379-1393.
|
[40] |
ZHOU J W, LI J, LI H M, et al. The serine-48 residue of nucleolar phosphoprotein nucleophosmin-1 plays critical role in subcellular localization and interaction with porcine circovirus type 3 capsid protein[J]. Veterinary Research, 2021, 52(1): 1-17.
|