Dissection and identification of regions required to form pseudoparticles by the interaction between the nucleocapsid (N) and membrane (M) proteins of SARS coronavirus

Hatakeyama, Seisuke; Matsuoka, Yusuke; Ueshiba, Hidehiro; Komatsu, Nobukazu; Itoh, Kyogo; Shichijo, Shigeki; Kanai, Tatsuaki; Fukushi, Masaya; Kirikae, Teruo; Sasazuki, Takehiko; Miyoshi‐Akiyama, Tohru

doi:10.1016/j.virol.2008.07.012

Cited by 23 publications

(31 citation statements)

References 31 publications

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“…The multimerization of N proteins occurs primarily through the C terminus (14). The N-terminal portion of the N protein (amino acids [aa] 168 to 208) is important for the interaction with the viral M protein, indicating that this region may be crucial for viral packaging (15,16). The N protein of SARS-CoV has been demonstrated to upregulate the expression of the proinflammatory factor COX2 and to interact with the proteasome subunit p42, which affects a variety of basic cellular processes and inflammatory responses (17,18).…”

mentioning

confidence: 99%

The Severe Acute Respiratory Syndrome Coronavirus Nucleocapsid Inhibits Type I Interferon Production by Interfering with TRIM25-Mediated RIG-I Ubiquitination

Hu¹,

Li²,

Gao³

et al. 2017

J Virol

269

315

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Severe acute respiratory syndrome (SARS) is a respiratory disease, caused by a coronavirus (SARS-CoV), that is characterized by atypical pneumonia. The nucleocapsid protein (N protein) of SARS-CoV plays an important role in inhibition of type I interferon (IFN) production via an unknown mechanism. In this study, the SARS-CoV N protein was found to bind to the SPRY domain of the tripartite motif protein 25 (TRIM25) E3 ubiquitin ligase, thereby interfering with the association between TRIM25 and retinoic acid-inducible gene I (RIG-I) and inhibiting TRIM25-mediated RIG-I ubiquitination and activation. Type I IFN production induced by poly I·C or Sendai virus (SeV) was suppressed by the SARS-CoV N protein. SARS-CoV replication was increased by overexpression of the full-length N protein but not N amino acids 1 to 361, which could not interact with TRIM25. These findings provide an insightful interpretation of the SARS-CoV-mediated host innate immune suppression caused by the N protein.IMPORTANCE The SARS-CoV N protein is essential for the viral life cycle and plays a key role in the virus-host interaction. We demonstrated that the interaction between the C terminus of the N protein and the SPRY domain of TRIM25 inhibited TRIM25-mediated RIG-I ubiquitination, which resulted in the inhibition of IFN production. We also found that the Middle East respiratory syndrome CoV (MERS-CoV) N protein interacted with TRIM25 and inhibited RIG-I signaling. The outcomes of these findings indicate the function of the coronavirus N protein in modulating the host's initial innate immune response.

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confidence: 99%

The Severe Acute Respiratory Syndrome Coronavirus Nucleocapsid Inhibits Type I Interferon Production by Interfering with TRIM25-Mediated RIG-I Ubiquitination

Hu¹,

Li²,

Gao³

et al. 2017

J Virol

269

315

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“…Sources of NP proteins for the sandwich ELISA included cultured human A/New York/55/2004(H3N2) and A/New Caledonia/20/1999 (H1N1) viruses in tissue culture, and recombinant NPs from HEK293 cells transfected with cytomegalovirus (CMV) promoter‐driven plasmids 14,15 encoding an NP gene with the sequence of H1N1/2009 (A/California/04/2009(H1N1)) and that of HPAI (A/Viet Nam/VL‐020/2005(H5N1).…”

Section: Methodsmentioning

confidence: 99%

Discrimination of influenza A subtype by antibodies recognizing host‐specific amino acids in the viral nucleoprotein

Miyoshi‐Akiyama

Yamashiro

Quynh

et al. 2012

Influenza Resp Viruses

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Please cite this paper as: Miyoshi‐Akiyama et al. (2012) Discrimination of influenza A subtype by antibodies recognizing host‐specific amino acids in the viral nucleoprotein. Influenza and Other Respiratory Viruses 6(6), 434–441. Background Nucleoprotein (NP) of influenza viruses is utilized to differentiate between the A, B, and C viral serotypes. The availability of influenza genome sequence data has allowed us to identify specific amino acids at particular positions in viral proteins, including NP, known as “signature residues,” which can be used to discriminate human influenza A viruses from H5N1 highly pathogenic avian influenza in human cases (HPAI) and pandemic H1N1(2009) (H1N1/2009) viruses. Methods Screening and epitope mapping of monoclonal antibodies (mAb) against NP of influenza A, which reacted differently with NP from human influenza A virus from HPAI and H1N1/2009 A virus. To identify the epitope(s) responsible for the discrimination of viral NP by mAbs, we prepared mutant NP proteins in the 293 cell expression system because some of the mAbs reacted with non‐linear epitopes. Results and Conclusions In the present study, we identified 3 mAbs. The results of epitope mapping showed that the epitopes were located at the signature residues. These results indicated that signature residues of NP could discriminate influenza A viruses from different origin.

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“…Recombinant NP of influenza A virus [A/Viet Nam/VL-020/2005 (H5N1)] (GenBank accession number AAZ72762), a virus isolated from a patient infected with HPAI, was prepared from Escherichia coli BL21(DE3) CodonPlus-RIPL cells (Stratagene), which carry a TAGZyme pQE2 (Qiagen) derivative carrying the NP protein gene (7). The NP was used to immunize 7-to 9-week-old female WKY rats (Oriental Yeast Co., Ltd.), and rat MAbs were prepared as described previously (10).…”

Section: Monoclonal Antibodies To Influenza a Virus Nucleoprotein (Np)mentioning

confidence: 99%

Development of an Immunochromatographic Assay Specifically Detecting Pandemic H1N1 (2009) Influenza Virus

et al. 2010

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The pandemic caused by a new type of influenza virus, pandemic H1N1 (2009) influenza virus A (AH1pdm), has had a major worldwide impact. Since hemagglutinin (HA) genes are among the most specific genes in the influenza virus genome, AH1pdm can be definitively diagnosed by viral gene analysis targeting the HA genes. This type of analysis, however, cannot be easily performed in clinical settings. While commercially available rapid diagnosis kits (RDKs) based on immunochromatography can be used to detect nucleoproteins (NPs) of influenza A and B viruses in clinical samples, there are no such kits that are specific for AH1pdm. We show here that an RDK using a combination of monoclonal antibodies against NP can be used to specifically detect AH1pdm. The RDK recognized AH1pdm virus isolates but did not recognize seasonal H1N1 and H3N2 and influenza B viruses, indicating that the specificity of the RDK is 100%. A parallel comparison of RDK with a commercial influenza A/B virus kit revealed that both types of kits had equal sensitivities in detecting their respective viruses. Preliminary evaluation of clinical samples from 5 individuals with PCR-confirmed human AH1pdm infection showed that the RDK was positive for all samples, with the same detection intensity as that of a commercial influenza A/B virus kit. This RDK, together with a new vaccine and the stockpiling of anti-influenza drugs, will make aggressive measures to contain AH1pdm infections possible.

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Dissection and identification of regions required to form pseudoparticles by the interaction between the nucleocapsid (N) and membrane (M) proteins of SARS coronavirus

Cited by 23 publications

References 31 publications

The Severe Acute Respiratory Syndrome Coronavirus Nucleocapsid Inhibits Type I Interferon Production by Interfering with TRIM25-Mediated RIG-I Ubiquitination

The Severe Acute Respiratory Syndrome Coronavirus Nucleocapsid Inhibits Type I Interferon Production by Interfering with TRIM25-Mediated RIG-I Ubiquitination

Discrimination of influenza A subtype by antibodies recognizing host‐specific amino acids in the viral nucleoprotein

Development of an Immunochromatographic Assay Specifically Detecting Pandemic H1N1 (2009) Influenza Virus

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