Predicted membrane topology of the coronavirus protein E1

Rottier, Peter J. M.; Welling, Gjalt W.; Welling‐Wester, Sytske; Niesters, H. G. M.; Lenstra, Johannes A.; Zeijst, Bernard A.M. van der

doi:10.1021/bi00354a022

Cited by 86 publications

(68 citation statements)

References 41 publications

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“…The expected membrane topology of the M protein would therefore be likely to resemble the model proposed by Rottier and collaborators (Armstrong et al, 1984;Rottier et al, 1986). Most of the basic amino acids are situated in the C-terminal half of the protein and might, therefore, interact with the negatively charged RNA and the acidic residues of the N protein as suggested by Sturman et al (1980).…”

Section: Discussionmentioning

confidence: 64%

Sequence analysis of the turkey enteric coronavirus nucleocapsid and membrane protein genes: a close genomic relationship with bovine coronavirus

Verbeek¹,

Tijssen²

1991

Journal of General Virology

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The 3' end of the turkey coronavirus (TCV) genome and the gene encoding the nucleocapsid protein (N) were cloned and sequenced. The gene encoding the membrane protein (M) was obtained by cloning a polymerase chain reaction (PCR)-amplified fragment obtained using bovine coronavirus (BCV)-specific primers. Furthermore, five TCV DNA fragments, obtained by PCR on RNA from clinical specimens and corresponding to either the N terminus of the M protein or the complete M protein were also cloned and sequenced. The sequence revealed a 3' non-coding region of 291 bases, an open reading frame (ORF) encoding the N protein with a predicted size of 448 amino acids, or an Mr of 49K, and an ORF encoding the M protein with a predicted size of 230 amino acids and an Mr of 26K. A third ORF, encoding a hypothetical protein of 207 amino acids with an Mr of 23K was found within the N gene sequence. The amino acid sequences of both the N and M proteins were more than 99% similar to those published for BCV. Extensive similarity was also observed between the amino acid sequences of the TCV N protein and those of murine hepatitis virus (MHV) (70%) and human respiratory coronavirus strain OC43 (HCV-OC43) (98%) and between the amino acid sequences of the predicted M proteins of TCV and MHV (86 %). Such striking identity suggests that BCV, TCV and HCV-OC43 must have diverged from each other only recently. A potential N-glycosylation site was found at the N terminus of the TCV M protein and is situated at the same location in BCV, MHV and transmissible gastroenteritis virus.

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Section: Discussionmentioning

confidence: 64%

Sequence analysis of the turkey enteric coronavirus nucleocapsid and membrane protein genes: a close genomic relationship with bovine coronavirus

Verbeek¹,

Tijssen²

1991

Journal of General Virology

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“…Nucleotide sequencing of the M gene of MHV-A59 and MHV-JHM Pfleiderer et al, 1986), IBV-Beaudette and IBV-6/82 Binns et al, 1986a), BCV (Lapps et al, 1987) and TGEV has revealed many interesting features of the M glycoprotein. Computer predictions of its secondary structure have led to a model in which approximately 10~ of the N-terminal part of the molecule is exposed on the outer surface of the virus membrane (see references above and Rottier et al, 1986). This view is supported by experimental evidence Cavanagh et al, 1986a).…”

Section: Glycoproteinmentioning

confidence: 94%

Coronaviruses: Structure and Genome Expression

Spaan

Cavanagh²,

Horzinek

1988

Journal of General Virology

504

485

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“…An internal BamH1 site at nucleotide 338 (equivalent to nucleotide 453 in reference 9) was utilized to generate a fragment containing the 3' half of the coding sequence. This fragment includes the entire sequence encoding the putative cytoplasmic domain of p23 (9,50). This fragment was ligated to a BamHl fragment containing the sequence encoding the extracellular and transmembrane domains of G protein, as well as the four amino-terminal amino acids derived from the G cytoplasmic domain, and reinserted into pJC 119.…”

Section: Construction Of Pg23mentioning

confidence: 99%

Cytoplasmic domains of cellular and viral integral membrane proteins substitute for the cytoplasmic domain of the vesicular stomatitis virus glycoprotein in transport to the plasma membrane.

Puddington¹,

Machamer²,

Rose³

1986

The Journal of Cell Biology

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Abstract. Oligonucleotide-directed mutagenesis was used to construct chimeric cDNAs that encode the extracellular and transmembrane domains of the vesicular stomatitis virus glycoprotein (G) linked to the cytoplasmic domain of either the immunoglobulin u membrane heavy chain, the hemagglutinin glycoprotein of influenza virus, or the small glycoprotein (023) of infectious bronchitis virus. Biochemical analyses and immunofluorescence microscopy demonstrated that these hybrid genes were correctly expressed in eukaryotic cells and that the hybrid proteins were transported to the plasma membrane. The rate of transport to the Golgi complex of G protein with an immunoglobulin # membrane cytoplasmic domain was approximately sixfold slower than G protein with its normal cytoplasmic domain. However, this rate was virtually identical to the rate of transport of ~m heavy chain molecules measured in the B cell line WEHI 231. The rate of transport of G protein with a hemagglutinin cytoplasmic domain was threefold slower than wild type G protein and G protein with a p23 cytoplasmic domain, which were transported at similar rates. The combined results underscore the importance of the amino acid sequence in the cytoplasmic domain for efficient transport of G protein to the cell surface. Also, normal cytoplasmic domains from other transmembrane glycoproteins can substitute for the G protein cytoplasmic domain in transport of G protein to the plasma membrane. The method of constructing precise hybrid proteins described here will be useful in defining functions of specific domains of viral and cellular integral membrane proteins.

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Predicted membrane topology of the coronavirus protein E1

Cited by 86 publications

References 41 publications

Sequence analysis of the turkey enteric coronavirus nucleocapsid and membrane protein genes: a close genomic relationship with bovine coronavirus

Sequence analysis of the turkey enteric coronavirus nucleocapsid and membrane protein genes: a close genomic relationship with bovine coronavirus

Coronaviruses: Structure and Genome Expression

Cytoplasmic domains of cellular and viral integral membrane proteins substitute for the cytoplasmic domain of the vesicular stomatitis virus glycoprotein in transport to the plasma membrane.

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