Nucleotide Sequence of the Gene Encoding the Spike Glycoprotein of Human Coronavirus HCV 229E

Raabe, Thomas; Schelle-Prinz, B.; Siddell, Stuart G.

doi:10.1099/0022-1317-71-5-1065

Cited by 46 publications

(49 citation statements)

References 49 publications

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“…The HCoV-229E S glycoprotein is the membrane glycoprotein responsible for the attachment of virions to the cell surface and the fusion of the envelope with cellular membranes (11,20). Studies of related coronaviruses, such as transmissible gastroenteritis virus, MHV, and infectious bronchitis virus of chickens, also demonstrate a similar function for the S protein (5,6,28,29).…”

Section: Discussionmentioning

confidence: 99%

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Human Coronavirus 229E Infects Polarized Airway Epithelia from the Apical Surface

Wang

Deering

Macke

et al. 2000

J Virol

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Gene transfer to differentiated airway epithelia with existing viral vectors is very inefficient when they are applied to the apical surface. This largely reflects the polarized distribution of receptors on the basolateral surface. To identify new receptor-ligand interactions that might be used to redirect vectors to the apical surface, we investigated the process of infection of airway epithelial cells by human coronavirus 229E (HCoV-229E), a common cause of respiratory tract infections. Using immunohistochemistry, we found the receptor for HCoV-229E (CD13 or aminopeptidase N) localized mainly to the apical surface of airway epithelia. When HCoV-229E was applied to the apical or basolateral surface of well-differentiated primary cultures of human airway epithelia, infection primarily occurred from the apical side. Similar results were noted when the virus was applied to cultured human tracheal explants. Newly synthesized virions were released mainly to the apical side. Thus, HCoV-229E preferentially infects human airway epithelia from the apical surface. The spike glycoprotein that mediates HCoV-229E binding and fusion to CD13 is a candidate for pseudotyping retroviral envelopes or modifying other viral vectors.While gene transfer is considered the most direct means to treat or prevent the lung disease associated with cystic fibrosis, several barriers prevent the practical application of this approach (36). A problem that currently limits efficient gene transfer to airway epithelia is that the receptor in most cases is localized to the basolateral surface. This has been demonstrated for several retroviral envelopes (32, 33), adenovirus (19,31,34), and adeno-associated virus (7). Thus, the mere fact that a viral vector is derived from a respiratory pathogen does not imply that it will efficiently transduce airway epithelia via the apical surface.As a first step in identifying novel ligand-receptor interactions that might be exploited to direct vectors to the apical surface of airway epithelia, we studied the infection process of human coronavirus 229E (HCoV-229E) in well-differentiated airway epithelia. Human coronaviruses are enveloped, plusstranded RNA viruses represented by the two serologically unrelated strains, HCoV-229E and HCoV-OC43, that cause mainly upper respiratory tract infections (3, 16). Epidemiological data demonstrate that the HCoV infections are responsible for approximately one-third of common colds (17, 35). HCoV-229E contains a genomic RNA of 27,277 nucleotides, a nucleocapsid (N) protein and a lipid envelope with three major membrane proteins. The three membrane proteins are the membrane (M) glycoprotein, the envelope (E) protein, and the surface spike (S) glycoprotein (11).We selected HCoV-229E for our studies for several reasons. First, it is a common cause of respiratory infections in humans (16). Second, the viral proteins involved in cell binding and the host cell glycoprotein that serves as the receptor have been identified (20,38). Third, infection by HCoV-229E involves both binding ...

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Section: Discussionmentioning

confidence: 99%

“…First, it is a common cause of respiratory infections in humans (16). Second, the viral proteins involved in cell binding and the host cell glycoprotein that serves as the receptor have been identified (20,38). Third, infection by HCoV-229E involves both binding and membrane fusion events that are mediated by the S glycoprotein.…”

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confidence: 99%

Human Coronavirus 229E Infects Polarized Airway Epithelia from the Apical Surface

Wang

Deering

Macke

et al. 2000

J Virol

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“…If one excludes the FIPV/CCV pair (Horsburgh et aI., 1992), this domain shows a high level of divergence, as was previously noted for the TGEV/FIPV pair (Jacobs et al, 1987). Furthermore, it has no counterpart in the S sequence of HCV 229E (Raabe et al, 1990) or of porcine respiratory coronavirus, the respiratory variant of TGEV (Rasschaert et al, 1990) not included in the alignment. In contrast, PEDV encodes a large S molecule, thus strengthening our earlier speculation that this domain may play some role in the expression of the enteric tropism .…”

Section: Inra Unit~ De Virologie Et Immunologiementioning

confidence: 95%

“…Close to the C terminus, there is a stretch of hydrophobic residues (positions 1322 to 1337 in PEDV S), which is predicted to form an a-helix and to function as a membrane anchor. Incidentally, the flanking sequence KWPWWVWL is identical in PEDV and HCV 229E and differs by one aa from the sequence KWPWYVWL which was shown to be conserved in all S protein genes sequenced to date (Raabe et al, 1990). The downstream, 46 aa presumably intra-virion domain contains six Cys residues strictly conserved within all the members of the subset.…”

Section: Inra Unit~ De Virologie Et Immunologiementioning

confidence: 99%

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Sequence of the Spike Srotein of the Porcine Epidemic Diarrhoea Virus

Duarte

Laude

1994

Journal of General Virology

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The complete sequence of the spike (S) gene of the Brl/87 isolate of porcine epidemic diarrhoea virus (PEDV) was determined from cDNA clones. The predicted polypeptide was 1383 amino acids long, contained 29 potential N-linked glycosylation sites and showed structural features similar to those of the coronavirus spike protein. The PEDV S protein, like that of the members of the transmissible gastroenteritis virus (TGEV)-related subset, lacks a proteolytic site to yield cleaved amino and carboxy subunits S1 and $2. Viral polypeptide species of the expected Mr, i.e. 170K/190K, were observed in PEDV-infected cells. Sequence comparison confirmed that, within the subset, PEDV was most closely related to the human respiratory coronavirus HCV 229E. However, PEDV S protein has an additional 250 residue N-terminal domain which is absent from HCV 229E and porcine respiratory coronavirus, the respiratory variant of TGEV. Alignment of the S1 regions revealed a second domain of about 90 residues with increased sequence divergence which might possibly express virus-specific determinants.

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Characterization of a nucleic acid probe for the diagnosis of human coronavirus 229E infections

Myint¹,

Harmsen

Raabe

et al. 1990

Journal of Medical Virology

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A cDNA copy of the HCV229E nucleocapsid protein gene was isolated and characterized. Sequence analysis predicts a nucleocapsid polypeptide of 389 amino acids with a molecular weight (mol. wt.) of 43,450. Single strand RNA probes derived from the cDNA copy hybridize specifically to HCV229E RNA and approximately 50 pg of intracellular viral RNA can be readily detected. The application of nucleic acid hybridization as a routine procedure for the diagnosis of HCV229E infection is discussed.

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Nucleotide Sequence of the Gene Encoding the Spike Glycoprotein of Human Coronavirus HCV 229E

Cited by 46 publications

References 49 publications

Human Coronavirus 229E Infects Polarized Airway Epithelia from the Apical Surface

Human Coronavirus 229E Infects Polarized Airway Epithelia from the Apical Surface

Sequence of the Spike Srotein of the Porcine Epidemic Diarrhoea Virus

Characterization of a nucleic acid probe for the diagnosis of human coronavirus 229E infections

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