Structure and orientation of expressed bovine coronavirus hemagglutinin-esterase protein

Kienzle, Thomas E.; Abraham, Sushma; Hogue, Brenda G.; Brian, David A.

doi:10.1128/jvi.64.4.1834-1838.1990

Cited by 70 publications

(57 citation statements)

References 39 publications

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“…The HE gene encodes a type I membrane protein of 424-439 residues that contains a cleavable signal peptide at its amino terminus (Hogue et al, 1989;Kienzle et al, 1990) and a transmembrane domain close to its carboxy terminus, leaving a short cytoplasmic tail of about 10 residues (Fig. 4).…”

Section: G He Proteinmentioning

confidence: 99%

“…However, influenza C virus, toroviruses, and coronaviruses may well have acquired their HE sequences independently, not from each other but from yet another source (Cornelissen et al, 1997). The HE protein becomes cotranslationally N-glycosylated when expressed in cells, giving rise to a polypeptide of approximately 60-65 kDa that rapidly forms disulfide-linked dimers (Hogue et al, 1989;Kienzle et al, 1990;King et al, 1985;Parker et al, 1989;Yokomori et al, 1989;Yoo et al, 1992). The HE dimers (or a higher order structure thereof) become incorporated into virions, while a proportion is transported to the cell surface (Kienzle et al, 1990;Pfleiderer et al, 1991).…”

Section: G He Proteinmentioning

confidence: 99%

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Molecular Interactions in the Assembly of Coronaviruses

Haan

Rottier

2005

Advances in Virus Research

366

338

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Section: G He Proteinmentioning

confidence: 99%

Section: G He Proteinmentioning

confidence: 99%

Molecular Interactions in the Assembly of Coronaviruses

Haan

Rottier

2005

Advances in Virus Research

366

338

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“…Using TMpred the transmembrane helix was predicted for amino acids 394-415. The putative active site for esterase activity, FGDS (Kienzle et al, 1990), was present at amino acids 37-40.…”

Section: Analysis Of the He Genementioning

confidence: 99%

Isolation and sequence analysis of canine respiratory coronavirus

2007

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Canine respiratory coronavirus (CRCoV) has frequently been detected in respiratory samples from dogs by RT-PCR. In this report the first successful isolation of CRCoV from a dog with respiratory disease is described. The isolate CRCoV-4182 was cultured in HRT-18 cells but failed to replicate in a number of other cell lines. The nucleotide sequence of the 3'-terminal portion of the CRCoV genome was determined including all open reading frames from the NS2 gene to the N gene. Comparison with other coronavirus sequences showed a high similarity to bovine coronavirus (BCoV). The region between the spike and the E gene was found to be the most variable and was used for phylogenetic analysis of several CRCoV strains. CRCoV-4182 showed a mutation within the non-structural protein region downstream of the S gene leading to the translation of an 8.8 kDa putative protein comprising a fusion of the equivalent of the BCoV 4.9 kDa protein to a truncated version of the BCoV 4.8 kDa protein. The culture of CRCoV will enable analysis of the expression and function of this and other CRCoV proteins as well as allowing the study of the role of CRCoV in the aetiology of canine infectious respiratory disease.

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“…3a can also interact specifically with M and E, which are two key players in the viral assembly of coronaviruses, as well as with the S protein (Tan et al, 2004c;Zeng et al, 2004b); hence it may also be important for viral assembly and/or release of virus from infected cells. It is tempting to postulate that 3a is a novel structural protein as only the coronavirus structural proteins, S, hemagglutinin-esterase (HE) and E, have been shown to be transported to the plasma membrane/cell surface (Kienzle et al, 1990;Parker et al, 1990;Smith et al, 1990;Vennema et al, 1990). Indeed, Zeng et al (2004b) could detect disulfide-linked complexes of S and 3a in the medium of SARS-CoV infected cells, indicating that 3a was secreted together with S, possibly through the formation of virus particles.…”

Section: Group-specific Genesmentioning

confidence: 99%

Characterization of viral proteins encoded by the SARS-coronavirus genome

2005

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A new disease, termed severe acute respiratory syndrome (SARS), emerged at the end of 2002 and caused profound disturbances in over 30 countries worldwide in 2003. A novel coronavirus was identified as the aetiological agent of SARS and the 30kb viral genome was deciphered with unprecedented speed in a coordinated manner by the global community. Since then, much progress has been made in the virological and molecular characterization of the proteins encoded by SARS-coronavirus (SARS-CoV) genome, which contains 14 potential open reading frames (ORFs). These investigations can be broadly classified into three groups: (a) studies on the replicase 1a/1b gene products which are important for viral replication, (b) studies on the structural proteins, spike, nucleocapsid, membrane and envelope, which have homologues in all coronaviruses, and are important for viral assembly and (c) expression and functional studies of the "accessory" proteins that are specifically encoded by SARS-CoV. A comparison of the properties of these three groups of SARS-CoV proteins with the knowledge that coronavirologists have generated over more than 30 years of research can help us in the prevention and treatment of SARS in the event of the re-emergence of this new infectious disease.

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Structure and orientation of expressed bovine coronavirus hemagglutinin-esterase protein

Cited by 70 publications

References 39 publications

Molecular Interactions in the Assembly of Coronaviruses

Molecular Interactions in the Assembly of Coronaviruses

Isolation and sequence analysis of canine respiratory coronavirus

Characterization of viral proteins encoded by the SARS-coronavirus genome

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