Sequence analysis of the membrane protein gene of human coronavirus 229E

Patricia Jouvenne; Christopher D. Richardson; Steven S. Schreiber; Michael M.C. Lai; Pierre J. Talbot

doi:10.1016/0042-6822(90)90115-8

Sequence analysis of the membrane protein gene of human coronavirus 229E

Patricia Jouvenne, Christopher D. Richardson, Steven S. Schreiber, Michael M.C. Lai, Pierre J. Talbot

Research output: Contribution to journal › Article › peer-review

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Abstract

Human coronaviruses (HCV) are ubiquitous pathogens which cause respiratory, gastrointestinal, and possibly neurological disorders. To better understand the molecular biology of the prototype HCV-229E strain, the complete nucleotide sequence of the membrane protein (M) gene was determined from cloned cDNA. The open reading frame is preceded by a consensus transcriptional initiation sequence UCUAAACU, identical to the one found upstream of the N gene. The M gene encodes a 225-amino acid polypeptide with a molecular weight (MW) of 25,822, slightly higher than the apparent MW of 19,000-22,000 observed for the unprocessed M protein obtained after in vitro translation and immunoprecipitation. The M amino acid sequence presents a significant degree of homology (38%) with its counterpart of transmissible gastroenteritis coronavirus (TGEV). The M protein of HCV-229E is highly hydrophobic and its hydropathicity profile shows a transmembranous region composed of three major hydrophobic domains characteristic of a typical coronavirus M protein. About 10% (20 amino acids) of the HCV-229E M protein constitutes a hydrophilic and probably external portion. One N-glycosylation and three potential O-glycosylation sites are found in this exposed domain.

Original language	English
Pages (from-to)	608-612
Number of pages	5
Journal	Virology
Volume	174
Issue number	2
DOIs	https://doi.org/10.1016/0042-6822(90)90115-8
Publication status	Published - Feb 1990
Externally published	Yes

Bibliographical note

Funding Information:
We thank Francois Fossiez for helpful discussions and Lucie Sum-merside for typing the manuscript . This work was supported by Grant MT-9203 from the Medical Research Council of Canada to P . 1 . Talbot, and U .S . Public Health Services Research Grant NS18146 to M. M. C. Lai. P. J. Talbot is also the recipient of a University Research Scholarship from the Natural Sciences and Engineering Research Council of Canada . P . Jouvenne acknowledges a studentship support from the Fonds de la recherche en Same du Quebec . S . S . Schreiber was supported by a postdoctoral training fellowship from the U .S . National Institutes of Health Grant NS07149 .

ASJC Scopus Subject Areas

Virology

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10.1016/0042-6822(90)90115-8

Cite this

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title = "Sequence analysis of the membrane protein gene of human coronavirus 229E",

abstract = "Human coronaviruses (HCV) are ubiquitous pathogens which cause respiratory, gastrointestinal, and possibly neurological disorders. To better understand the molecular biology of the prototype HCV-229E strain, the complete nucleotide sequence of the membrane protein (M) gene was determined from cloned cDNA. The open reading frame is preceded by a consensus transcriptional initiation sequence UCUAAACU, identical to the one found upstream of the N gene. The M gene encodes a 225-amino acid polypeptide with a molecular weight (MW) of 25,822, slightly higher than the apparent MW of 19,000-22,000 observed for the unprocessed M protein obtained after in vitro translation and immunoprecipitation. The M amino acid sequence presents a significant degree of homology (38%) with its counterpart of transmissible gastroenteritis coronavirus (TGEV). The M protein of HCV-229E is highly hydrophobic and its hydropathicity profile shows a transmembranous region composed of three major hydrophobic domains characteristic of a typical coronavirus M protein. About 10% (20 amino acids) of the HCV-229E M protein constitutes a hydrophilic and probably external portion. One N-glycosylation and three potential O-glycosylation sites are found in this exposed domain.",

author = "Patricia Jouvenne and Richardson, {Christopher D.} and Schreiber, {Steven S.} and Lai, {Michael M.C.} and Talbot, {Pierre J.}",

note = "Funding Information: We thank Francois Fossiez for helpful discussions and Lucie Sum-merside for typing the manuscript . This work was supported by Grant MT-9203 from the Medical Research Council of Canada to P . 1 . Talbot, and U .S . Public Health Services Research Grant NS18146 to M. M. C. Lai. P. J. Talbot is also the recipient of a University Research Scholarship from the Natural Sciences and Engineering Research Council of Canada . P . Jouvenne acknowledges a studentship support from the Fonds de la recherche en Same du Quebec . S . S . Schreiber was supported by a postdoctoral training fellowship from the U .S . National Institutes of Health Grant NS07149 .",

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AU - Lai, Michael M.C.

AU - Talbot, Pierre J.

N1 - Funding Information: We thank Francois Fossiez for helpful discussions and Lucie Sum-merside for typing the manuscript . This work was supported by Grant MT-9203 from the Medical Research Council of Canada to P . 1 . Talbot, and U .S . Public Health Services Research Grant NS18146 to M. M. C. Lai. P. J. Talbot is also the recipient of a University Research Scholarship from the Natural Sciences and Engineering Research Council of Canada . P . Jouvenne acknowledges a studentship support from the Fonds de la recherche en Same du Quebec . S . S . Schreiber was supported by a postdoctoral training fellowship from the U .S . National Institutes of Health Grant NS07149 .

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N2 - Human coronaviruses (HCV) are ubiquitous pathogens which cause respiratory, gastrointestinal, and possibly neurological disorders. To better understand the molecular biology of the prototype HCV-229E strain, the complete nucleotide sequence of the membrane protein (M) gene was determined from cloned cDNA. The open reading frame is preceded by a consensus transcriptional initiation sequence UCUAAACU, identical to the one found upstream of the N gene. The M gene encodes a 225-amino acid polypeptide with a molecular weight (MW) of 25,822, slightly higher than the apparent MW of 19,000-22,000 observed for the unprocessed M protein obtained after in vitro translation and immunoprecipitation. The M amino acid sequence presents a significant degree of homology (38%) with its counterpart of transmissible gastroenteritis coronavirus (TGEV). The M protein of HCV-229E is highly hydrophobic and its hydropathicity profile shows a transmembranous region composed of three major hydrophobic domains characteristic of a typical coronavirus M protein. About 10% (20 amino acids) of the HCV-229E M protein constitutes a hydrophilic and probably external portion. One N-glycosylation and three potential O-glycosylation sites are found in this exposed domain.

AB - Human coronaviruses (HCV) are ubiquitous pathogens which cause respiratory, gastrointestinal, and possibly neurological disorders. To better understand the molecular biology of the prototype HCV-229E strain, the complete nucleotide sequence of the membrane protein (M) gene was determined from cloned cDNA. The open reading frame is preceded by a consensus transcriptional initiation sequence UCUAAACU, identical to the one found upstream of the N gene. The M gene encodes a 225-amino acid polypeptide with a molecular weight (MW) of 25,822, slightly higher than the apparent MW of 19,000-22,000 observed for the unprocessed M protein obtained after in vitro translation and immunoprecipitation. The M amino acid sequence presents a significant degree of homology (38%) with its counterpart of transmissible gastroenteritis coronavirus (TGEV). The M protein of HCV-229E is highly hydrophobic and its hydropathicity profile shows a transmembranous region composed of three major hydrophobic domains characteristic of a typical coronavirus M protein. About 10% (20 amino acids) of the HCV-229E M protein constitutes a hydrophilic and probably external portion. One N-glycosylation and three potential O-glycosylation sites are found in this exposed domain.

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Sequence analysis of the membrane protein gene of human coronavirus 229E

Abstract

Bibliographical note

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