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HKU1 internal protein ameliorate infection in mice

ABSTRACT: HKU1 internal protein ameliorate infection in mice

PROVIDER: PRJNA1232806 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR32600283_1.fastq.gz	Fastqsanger.gz
	SRR32600283_2.fastq.gz	Fastqsanger.gz
	SRR32600284_1.fastq.gz	Fastqsanger.gz
	SRR32600284_2.fastq.gz	Fastqsanger.gz
	SRR32600285_1.fastq.gz	Fastqsanger.gz

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HKU1 internal protein ameliorate infection in mice

Project description:Coronaviruses express a repertoire of accessory proteins for evading host immune responses. Among these accessory proteins, a small internal (I) protein is expressed by members of the genus Betacoronavirus. Previous studies reported that the I proteins of SARS-CoV, MERS-CoV and SARS-CoV-2 inhibit type I interferon (IFN-I) expression through distinct mechanisms and play different roles in pathogenesis. In addition, human coronaviruses HKU1 and OC43 are betacroaonvairuses that predominantly cause common cold and encode the I protein as one of their accessory proteins; the I proteins of hCoV-HKU1 and hCoV-OC43 have not been previously characterized. However, the lack of robust reverse genetic systems, tissue culture and animal models limit the study of hCoV-HKU1 and hCoV-OC43 pathogenesis. Here, we examined the role of hCoV-HKU1 and hCoV-OC43 I proteins in pathogenesis using a prototypic coronavirus. We introduced the I proteins of hCoV-HKU1 and hCoV-OC43 independently to a neurotropic strain of mouse hepatitis virus (MHV-J2.2). MHV-J2.2 infection is well-characterized with clearly defined immune responses which allows the study of I proteins in the context of authentic coronavirus infection. We showed that the I protein of hCoV-HKU1 but not that of hCoV-OC43 ameliorated MHV-J2.2 infection while the I protein of MERS-CoV causes exacerbated disease. Further analysis revealed that infection with MHV-J2.2 expressing the I protein of MERS-CoV leads to increased neutrophil infiltration to the site of infection and virus titers in mice; diminished virus titers was observed in the presence of hCoV-HKU1 I protein. Overall, our findings suggest that the I protein of different betacoronaviruses play unique roles in pathogenesis.

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Project description:HKU1 is a human betacoronavirus and infects host cells via highly glycosylated spike protein (S). At present, N-glycosylation of HKU1 S has been reported, however, little is known about its O-glycosylation, which hinders an in-depth understanding of its biological functions. Herein, a comprehensive study of O-glycosylation of HKU1 S was carried out based on dual-functional histidine-bonded silica materials (HBS). The enrichment method for O-glycopeptides with HBS was developed and validated using standard proteins. The application of the developed method to HKU1 S1 subunit resulted in 61 novel O-glycosylation sites, among which 56% were predicted to be exposed on protein outer surface. Moreover, the O-linked glycans and their abundance on each HKU1 S1 site were also analyzed. The obtained O-glycosylation dataset would provide valuable insights for the understanding of the structure of HKU1 S.

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Project description:Coronaviruses (CoVs) encompass many human pathogens such as HKU-1, OC43, NL63, SARS, MERS and, most recently, nCoV-2019. The spike (S) protein of CoVs has received much attention for its role in host tropism and immunity, but it is becoming increasingly clear that the haemagglutinin esterase (HE) also plays an important role in host adaptation by determining host receptor (sialic acid) specificity. We determined the structure of HKU1 HE by cryo electron microscopy and mapped site-specific N-linked glycosylation by LC-MS/MS of glycopeptides using electron transfer high-energy collision dissociation.

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