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1.
Opt Lett ; 49(2): 367-370, 2024 Jan 15.
Article in English | MEDLINE | ID: mdl-38194570

ABSTRACT

We investigate optical transmission in cavity magnon polaritons and discover a complex multi-window magnetically induced transparency and a bistability with magnetic and optical characteristics. With the regulation of Kerr nonlinear effects and driven fields, a complex multi-window resonant transmission with fast and slow light effects appears, which includes transparency and absorption windows. The magnetically induced transparency and absorption can be explained by the destructive and constructive interference between different excitation pathways. Moreover, we demonstrate the bistability of magnons and photons with a hysteresis loop, where magnetic and optical bistabilities can induce and control each other. Our results pave a new way, to the best of our knowledge, for implementing a room-temperature multiband quantum memory.

2.
Virus Res ; 270: 197670, 2019 09.
Article in English | MEDLINE | ID: mdl-31330206

ABSTRACT

The nuclear localization signals (NLS) were usually composed of basic residues (K and R) and played an important role in delivery of genomes and structural protein into nucleus. In this research, we identified that 3Dpol/3CD entered into nucleus during viral propagation of duck hepatitis A virus type 1 (DHAV-1). To investigate the reason that 3Dpol/3CD entered into nucleus, the amino acid sequence of 3CD was analyzed through NLS Mapper program. The basic region 17PRKTAYMRS25 was subsequently proved to be a functional NLS to guide 3Dpol/3CD into nucleus. 18R, 19K and 24R were found essential for maintaining the nuclear targeting activity, and exchange between 24R and 24K had no impact on cellular localization of 3Dpol. Since the entry of 3Dpol/3CD into nucleus was essential for shutoff of host cell transcription and maintaining the viral propagation of picornavirus numbers, our study provided new insights into the mechanism of DHAV-1 propagation.


Subject(s)
Cell Nucleus/virology , Hepatitis Virus, Duck/genetics , Nuclear Localization Signals , RNA-Dependent RNA Polymerase/genetics , Viral Proteins/genetics , Animals , Hepatitis Virus, Duck/enzymology
3.
Front Microbiol ; 9: 2250, 2018.
Article in English | MEDLINE | ID: mdl-30319572

ABSTRACT

The duck hepatitis A virus type 1 (DHAV-1) is a member of Picornaviridae family, the genome of the virus contains a 5' untranslated region (5' UTR), a large open reading frame that encodes a polyprotein precursor and a 3' UTR followed by a poly(A) tail. The translation initiation of virus proteins depends on the internal ribosome-entry site (IRES) element within the 5' UTR. So far, little information is known about the role of the 3' UTR and poly(A) tail during the virus proliferation. In this study, the function of the 3' UTR and poly(A) tail of DHAV-1 in viral replication and IRES-mediated translation was investigated. The results showed that both 3' UTR and poly(A) tail are important for maintaining viral genome RNA stability and viral genome replication. During DHAV-1 proliferation, at least 20 adenines were required for the optimal genome replication and the virus replication could be severely impaired when the poly (A) tail was curtailed to 10 adenines. In addition to facilitating viral genome replication, the presence of 3' UTR and poly(A) tail significantly enhance IRES-mediated translation efficiency. Furthermore, 3' UTR or poly(A) tail could function as an individual element to enhance the DHAV-1 IRES-mediated translation, during which process, the 3' UTR exerts a greater initiation efficiency than the poly(A)25 tail.

4.
Virology ; 436(1): 112-7, 2013 Feb 05.
Article in English | MEDLINE | ID: mdl-23174505

ABSTRACT

The capsid protein (CP) of duck circovirus (DuCV) is the major immunogenic protein and has a high proportion of arginine residues concentrated at the N terminus of the protein, which inhibits efficient mRNA translation in prokaryotic expression systems. In this study, we investigated the subcellular distribution of DuCV CP expressed via recombinant baculoviruses in Sf9 cells and the DNA binding activities of the truncated recombinant DuCV CPs. The results showed that two independent bipartite nuclear localization signals (NLSs) situated at N-terminal 1-17 and 18-36 amino acid residue of the CP. Moreover, two expression level regulatory signals (ELRSs) and two DNA binding signals (DBSs) were also mapped to the N terminus of the protein and overlapped with the two NLSs. The ability of CP to bind DNA, coupled with the karyophilic nature of this protein, strongly suggests that it may be responsible for nuclear targeting of the viral genome.


Subject(s)
Capsid Proteins/chemistry , Capsid Proteins/metabolism , Circovirus/metabolism , Nuclear Localization Signals/metabolism , Animals , Baculoviridae/genetics , Capsid Proteins/genetics , Cell Line , Cell Nucleus/metabolism , Circovirus/genetics , DNA-Binding Proteins/chemistry , DNA-Binding Proteins/metabolism , Ducks/virology , Genome, Viral , Nuclear Localization Signals/chemistry , Nuclear Localization Signals/genetics , Recombinant Proteins/metabolism , Sf9 Cells , Signal Transduction , Virus Replication
5.
Bing Du Xue Bao ; 27(5): 456-61, 2011 Sep.
Article in Chinese | MEDLINE | ID: mdl-21998958

ABSTRACT

The objective of this study was to investigate the function of vimentin in PRRSV infection. Vimentin gene from Marc-145 cells was amplified by RT-PCR, cloned into pET-28a vector and expressed in Escherichia coli BL21(DE3). The expressed vimentin was confirmed by Western blot and purified which was used to immunize BALB/c mice for the production of antibodies. Vimentin and antibodies were tested for blocking PRRSV infection of Marc-145 cells. The binding of vimentin to PRRSV N and GP5 proteins were tested by the ELISA. The results showed that vimentin gene was amplified successfully and expressed as identified by SDS-PAGE and Western blot. Mouse anti-vimentin antibodies were produced with the titer of 10(5). PRRSV infection of Marc-145 cells was blocked partially by vimentin while blocked completely by the antibobies. In addition, vimentin was bound N protein, but not GP5. These results provide additional information on PRRSV entry into Marc-145 cells.


Subject(s)
Porcine Reproductive and Respiratory Syndrome/metabolism , Porcine respiratory and reproductive syndrome virus/physiology , Vimentin/metabolism , Animals , Antibodies/immunology , Antibodies/metabolism , Cell Line , Escherichia coli/genetics , Escherichia coli/metabolism , Female , Genetic Vectors/genetics , Mice , Mice, Inbred BALB C , Porcine Reproductive and Respiratory Syndrome/genetics , Porcine Reproductive and Respiratory Syndrome/virology , Protein Binding/physiology , Recombinant Proteins/genetics , Recombinant Proteins/immunology , Recombinant Proteins/isolation & purification , Recombinant Proteins/metabolism , Swine , Vimentin/genetics , Vimentin/immunology , Vimentin/isolation & purification , Viral Proteins/metabolism
6.
Bing Du Xue Bao ; 27(3): 250-6, 2011 May.
Article in Chinese | MEDLINE | ID: mdl-21774251

ABSTRACT

The spike (S) glycoprotein of HCoV-NL63 is a major target in the development of diagnostic assays and vaccines, but its antigenic and immunogenic properties remain unclear. Four fragments coding spike proteins (S1, S2, RL and RS) from HCoV-NL63 were amplified and cloned into the expression vector derived from vaccinia virus (Tiantan strain), and recombinant vaccinia viruses expressing four segments of spike proteins were generated (vJSC1175-S1; vJSC1175-S2; vJSC1175-RL; vJSC1175-RS), respectively. Their expression location in cell and level were characterized using indirect immune fluorescence assay (IFA) and Western-Blot, respectively. The expressions of four segments of spike proteins in recombinant vaccinia viruses were showed at appropriate level and with posttranslational modification (glycosylation), and S1, RL and RS were mainly distributed in the cell membrane, while the S2 was mainly distributed in the cytoplasm. Our results provide a basis for further exploring diagnostic role and vaccine development of different spike segments from HCoV-NL63.


Subject(s)
Coronavirus NL63, Human/chemistry , Membrane Glycoproteins/genetics , Recombinant Proteins/biosynthesis , Vaccinia virus/genetics , Viral Envelope Proteins/genetics , Base Sequence , Blotting, Western , Fluorescent Antibody Technique, Indirect , Humans , Membrane Glycoproteins/biosynthesis , Molecular Sequence Data , Plasmids , Spike Glycoprotein, Coronavirus , Viral Envelope Proteins/biosynthesis
7.
Article in Chinese | MEDLINE | ID: mdl-20848852

ABSTRACT

OBJECTIVE: To rational design HCV DNA vaccine candidates and evaluate their specific We design to construct two DNA vaccine candidates, one consists of immunity to HCV in mice. METHODS: We design to construct two DNA vaccine candidates, one consists of E2 (the envelope glycoprotein 2 of HCV) gene only, the second consists of E2-gAD (Globular Domain of Human Adiponectin) fusion gene via overlapping PCR. Confirm the expression of the DNA vaccines by Western blotting, and then vaccinated by injection of DNA vaccines with gene electrotransfer (GET) in BALB/c mice. The immune response was measured by IFN-gamma ELISPOT. RESULTS: The DNA vaccine candidate consists of E2-gAD could effectively express in vitro , and it could induced a higher anti-HCV T cell response in mice than the one consists of E2 only. CONCLUSION: The HCV DNA vaccine consists of E2-gAD fusion can increase the immunity of the E, to some extend, and the research paved a way to develop and optimize the novel HCV DNA vaccine.


Subject(s)
Hepacivirus/immunology , Hepatitis C/immunology , Vaccines, DNA/immunology , Viral Envelope Proteins/immunology , Viral Hepatitis Vaccines/immunology , Adiponectin/administration & dosage , Adiponectin/genetics , Adiponectin/immunology , Animals , Female , Hepacivirus/genetics , Hepatitis C/prevention & control , Humans , Mice , Mice, Inbred BALB C , Recombinant Fusion Proteins/administration & dosage , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/immunology , Vaccines, DNA/administration & dosage , Vaccines, DNA/genetics , Viral Envelope Proteins/administration & dosage , Viral Envelope Proteins/genetics , Viral Hepatitis Vaccines/administration & dosage , Viral Hepatitis Vaccines/genetics
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