Unique N-linked glycosylation of murine coronavirus MHV-2 membrane protein at the conserved O-linked glycosylation site

Yamada, Yasuko; Yabe, Mikiko; Ohtsuki, Takahiro; Taguchi, Fumihiro

doi:10.1016/s0168-1702(99)00134-3

Cited by 21 publications

(19 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Since the recombinant viruses generated in this study were able to use this MHV receptor isoform to infect the same cells (data not shown), the result obtained with MHV-RI is not due to the lack of O-linked sugars on its M protein but can probably be attributed to mutations in its S protein. Recently, MHV-2 was demonstrated to carry both N-linked and O-linked sugars at its M protein, indicating that both types of glycosylation can occur side by side on the same M protein (Yamada et al, 2000), as we had observed as well (de Haan et al, 1998a).…”

Section: Discussionsupporting

confidence: 77%

“…However, we now show that, in addition to the S protein, mutations in the M protein that alter the glycosylation state of the protein affect, in a still unknown way, the outcome of infection in the liver. The strong hepatotropism of MHV-2, although mainly determined by the S protein, may therefore be supported by the attachment of sugars to the M protein both via O-and N-linkages (Navas et al, 2001;Yamada et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

The glycosylation status of the murine hepatitis coronavirus M protein affects the interferogenic capacity of the virus in vitro and its ability to replicate in the liver but not the brain

et al. 2003

View full text Add to dashboard Cite

The coronavirus M protein, the most abundant coronaviral envelope component, is invariably glycosylated, which provides the virion with a diffuse, hydrophilic cover on its outer surface. Remarkably, while the group 1 and group 3 coronaviruses all have M proteins with N-linked sugars, the M proteins of the group 2 coronaviruses [e.g., mouse hepatitis virus (MHV)] are O-glycosylated. The conservation of the N- and O-glycosylation motifs suggests that each of these types of carbohydrate modifications is beneficial to their respective virus. Since glycosylation of the M protein is not required for virus assembly, the oligosaccharides are likely to be involved in the virus-host interaction. In order to investigate the role of the M protein glycosylation in the host, two genetically modified MHVs were generated by using targeted RNA recombination. The recombinant viruses carried M proteins that were either N-glycosylated or not glycosylated at all, and these were compared with the parental, O-glycosylated, virus. The M protein glycosylation state did not influence the tissue culture growth characteristics of the recombinant viruses. However, it affected their interferogenic capacity as measured using fixed, virus-infected cells. Viruses containing M proteins with N-linked sugars induced type I interferons to higher levels than viruses carrying M proteins with O-linked sugars. MHV with unglycosylated M proteins appeared to be a poor interferon inducer. In mice, the recombinant viruses differed in their ability to replicate in the liver, but not in the brain, whereas their in vivo interferogenic capacity did not appear to be affected by their glycosylation status. Strikingly, their abilities to replicate in the liver correlated with their in vitro interferogenic capacity. This apparent correlation might be explained by the functioning of lectins, such as the mannose receptor, which are abundantly expressed in the liver but also play a role in the induction of interferon-alpha by dendritic cells.

show abstract

Section: Discussionsupporting

confidence: 77%

Section: Discussionmentioning

confidence: 99%

The glycosylation status of the murine hepatitis coronavirus M protein affects the interferogenic capacity of the virus in vitro and its ability to replicate in the liver but not the brain

et al. 2003

View full text Add to dashboard Cite

show abstract

“…The M protein is the most abundant viral constituent and is almost invariably glycosylated. Intriguingly, whereas the group 1 and group 3 coronaviruses-with transmissible gastroenteritis virus (TGEV) and infectious bronchitis virus (IBV) as important representatives, respectively-all contain M proteins with only N-linked sugars, the M proteins of group 2 coronaviruses such as mouse hepatitis virus (MHV) are O-glycosylated [13], An exception is MHV-2, the M protein of which carries both O-and N-linked sugars [14]. The M protein plays a central role in coronavirus assembly.…”

Section: Discussionmentioning

confidence: 99%

Molecular characterization and phylogenetic analysis of membrane protein genes of porcine epidemic diarrhea virus isolates in China

et al. 2008

View full text Add to dashboard Cite

Six porcine epidemic diarrhea viruses (PEDVs) were isolated from the fecal samples of piglets infected with PEDV in 2006 in China. The membrane (M) protein genes of six PEDV isolates were amplified by reverse transcriptase-polymerase chain reaction (RT-PCR), then cloned, sequenced, and compared with each other as well as those ten PEDV reference strains. The M protein genes of six Chinese PEDV isolates consisted of 692 nucleotides containing a single open reading frame (ORF) of 681 nucleotides, which encoded a 226aa-long peptide. The conserved intergenic motif (ATAAAC), as previously recognized in Br1/87, was found in the 5 nucleotides upstream of the initiator ATG of M protein genes of six Chinese PEDV isolates. The hexamer motif was also found in CV777, JMe2, LZC, and QH. The M protein of six isolates had three main transmembrane domains (aa20-38, aa43-65, aa75-97). The M protein of one isolate, CH/IMT/06, had one potential glycosylation site, but those of the other five isolates had two. The glycosylation sequence Asn-Phe-Thr was highly conserved in the M proteins of six PEDV isolates. The six PEDV isolates showed nucleotide sequence homology between 98.8 and 100% and deduced amino acid sequence homology between 98.2 and 100% with each other. The nucleotide and amino acid identity of M protein genes between the six PEDV isolates and ten reference PEDV strains varied from 97.2 to 99.4% and 96.9 to 100%, respectively. On the basis of the phylogenetic relationship of M protein genes, six Chinese PEDV isolates composed of a separate cluster including one Chinese strain JS-2004-02, however, not including the Chinese strain LJB/03. These results demonstrated that there was a new genotype of PEDV prevailing in China.

show abstract

“…The ectodomain, which is the least conserved part of the M molecule, is glycosylated. For most group 2 coronaviruses, glycosylation is O-linked, although two exceptions to this pattern are MHV strain 2 (Yamada et al, 2000) and SARS-CoV (Nal et al, 2005), both of which have M proteins with N-linked carbohydrate. Group 1 and group 3 coronavirus M proteins, by contrast, exhibit N-linked glycosylation exclusively (Cavanagh and Davis, 1988;Garwes et al, 1984;Jacobs et al, 1986;.…”

Section: Membrane Protein (M)mentioning

confidence: 99%

The Molecular Biology of Coronaviruses

Masters

2006

Advances in Virus Research

1,555

1,677

View full text Add to dashboard Cite

Coronaviruses are large, enveloped RNA viruses of both medical and veterinary importance. Interest in this viral family has intensified in the past few years as a result of the identification of a newly emerged coronavirus as the causative agent of severe acute respiratory syndrome (SARS). At the molecular level, coronaviruses employ a variety of unusual strategies to accomplish a complex program of gene expression. Coronavirus replication entails ribosome frameshifting during genome translation, the synthesis of both genomic and multiple subgenomic RNA species, and the assembly of progeny virions by a pathway that is unique among enveloped RNA viruses. Progress in the investigation of these processes has been enhanced by the development of reverse genetic systems, an advance that was heretofore obstructed by the enormous size of the coronavirus genome. This review summarizes both classical and contemporary discoveries in the study of the molecular biology of these infectious agents, with particular emphasis on the nature and recognition of viral receptors, viral RNA synthesis, and the molecular interactions governing virion assembly.

show abstract

Unique N-linked glycosylation of murine coronavirus MHV-2 membrane protein at the conserved O-linked glycosylation site

Cited by 21 publications

References 21 publications

The glycosylation status of the murine hepatitis coronavirus M protein affects the interferogenic capacity of the virus in vitro and its ability to replicate in the liver but not the brain

The glycosylation status of the murine hepatitis coronavirus M protein affects the interferogenic capacity of the virus in vitro and its ability to replicate in the liver but not the brain

Molecular characterization and phylogenetic analysis of membrane protein genes of porcine epidemic diarrhea virus isolates in China

The Molecular Biology of Coronaviruses

Contact Info

Product

Resources

About