The first complete genome sequences of clinical isolates of human coronavirus 229E

Farsani, Seyed Mohammad Jazaeri; Dijkman, Ronald; Jebbink, Maarten F.; Goossens, Herman; Ieven, Margareta; Deijs, Martin; Molenkamp, Richard; Hoek, Lia van der

doi:10.1007/s11262-012-0807-9

Cited by 36 publications

(36 citation statements)

References 25 publications

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“…Also FIPVs seem to have lost the ability to replicate in the enteric tract (Pedersen, 2014). Clinical isolates of human coronavirus 229E as well as of the related alpaca coronavirus, both of which cause respiratory infections, encode relatively short spike proteins that lack the NTR (Crossley et al, 2012;Farsani et al, 2012). In contrast, closely related bat coronaviruses with intestinal tropism contain S proteins with a NTR or sometimes even two copies of the NTR (Corman et al, 2015) (Fig.…”

Section: S 1 Ntr Changesmentioning

confidence: 99%

Coronavirus Spike Protein and Tropism Changes

Hulswit

Haan

Bosch

2016

Advances in Virus Research

430

404

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Coronaviruses (CoVs) have a remarkable potential to change tropism. This is particularly illustrated over the last 15 years by the emergence of two zoonotic CoVs, the severe acute respiratory syndrome (SARS)- and Middle East respiratory syndrome (MERS)-CoV. Due to their inherent genetic variability, it is inevitable that new cross-species transmission events of these enveloped, positive-stranded RNA viruses will occur. Research into these medical and veterinary important pathogens-sparked by the SARS and MERS outbreaks-revealed important principles of inter- and intraspecies tropism changes. The primary determinant of CoV tropism is the viral spike (S) entry protein. Trimers of the S glycoproteins on the virion surface accommodate binding to a cell surface receptor and fusion of the viral and cellular membrane. Recently, high-resolution structures of two CoV S proteins have been elucidated by single-particle cryo-electron microscopy. Using this new structural insight, we review the changes in the S protein that relate to changes in virus tropism. Different concepts underlie these tropism changes at the cellular, tissue, and host species level, including the promiscuity or adaptability of S proteins to orthologous receptors, alterations in the proteolytic cleavage activation as well as changes in the S protein metastability. A thorough understanding of the key role of the S protein in CoV entry is critical to further our understanding of virus cross-species transmission and pathogenesis and for development of intervention strategies.

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Section: S 1 Ntr Changesmentioning

confidence: 99%

Coronavirus Spike Protein and Tropism Changes

Hulswit

Haan

Bosch

2016

Advances in Virus Research

430

404

View full text Add to dashboard Cite

show abstract

“…It has been previously shown that the HCoV-229E genome codes for two accessory proteins, p4a and p4b. However, recent sequencing of clinical isolates revealed the presence of a fulllength p4, whereas laboratory strains show the presence of a truncated p4 (Farsani et al, 2012). It has been suggested that extensive culturing of HCoV 229E might have resulted in this truncation (Dijkman et al, 2006).…”

Section: Accessory Proteins In Alphacoronavirusmentioning

confidence: 99%

Accessory proteins of SARS-CoV and other coronaviruses

et al. 2014

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The huge RNA genome of SARS coronavirus comprises a number of open reading frames that code for a total of eight accessory proteins. Although none of these are essential for virus replication, some appear to have a role in virus pathogenesis. Notably, some SARS-CoV accessory proteins have been shown to modulate the interferon signaling pathways and the production of pro-inflammatory cytokines. The structural information on these proteins is also limited, with only two (p7a and p9b) having their structures determined by X-ray crystallography. This review makes an attempt to summarize the published knowledge on SARS-CoV accessory proteins, with an emphasis on their involvement in virus-host interaction. The accessory proteins of other coronaviruses are also briefly discussed. This paper forms part of a series of invited articles in Antiviral Research on "From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses" (see Introduction by Hilgenfeld and Peiris (2013)).

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“…strains UU16 and UU21, Fig. 1b) have a large deletion in the N-domain; iii) clinical isolates of HCoV-229E encode a relatively short spike protein of 1173 residues in length due to the apparent lack of the N-domain (Farsani et al, 2012). Recently, bat coronaviruses related to HCoV-229E have been isolated from hipposiderid bats, some of them encoding unusual large spike glycoproteins of 1571-1582 residues in length (Corman et al, 2015).…”

Section: N-domains In Spike Proteins Of Alphacoronavirusesmentioning

confidence: 99%

Cellular entry of the porcine epidemic diarrhea virus

et al. 2016

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Porcine epidemic diarrhea virus (PEDV), a coronavirus discovered more than 40 years ago, regained notoriety recently by its devastating outbreaks in East Asia and the Americas, causing substantial economic losses to the swine husbandry. The virus replicates extensively and almost exclusively in the epithelial cells of the small intestine resulting in villus atrophy, malabsorption and severe diarrhea. Cellular entry of this enveloped virus is mediated by the large spike (S) glycoprotein, trimers of which mediate virus attachment to the target cell and subsequent membrane fusion. The S protein has a multidomain architecture and has been reported to bind to carbohydrate (sialic acid) and proteinaceous (aminopeptidase N) cell surface molecules. PEDV propagation in vitro requires the presence of trypsin(-like) proteases in the culture medium, which capacitates the fusion function of the S protein. Here we review the current data on PEDV entry into its host cell, including therein our new observations regarding the functional role of the sialic acid binding activity of the S protein in virus infection. Moreover, we summarize the recent progress on the proteolytic activation of PEDV S proteins, and discuss factors that may determine tissue tropism of PEDV in vivo.

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The first complete genome sequences of clinical isolates of human coronavirus 229E

Cited by 36 publications

References 25 publications

Coronavirus Spike Protein and Tropism Changes

Coronavirus Spike Protein and Tropism Changes

Accessory proteins of SARS-CoV and other coronaviruses

Cellular entry of the porcine epidemic diarrhea virus

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