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Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site

The nucleotide sequence of the peplomer (E2) gene of MHV-A59 was determined from a set of overlapping cDNA clones. The E2 gene encodes a protein of 1324 amino acids including a hydrophobic signal peptide. A second large hydrophobic domain is found near the COOH terminus and probably represents the m...

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Autores principales: Luytjes, Willem, Sturman, Lawrence S., Bredenbee, Peter J., Charite, Jeroen, van der Zeijst, Bernard A.M., Horzinek, Marian C., Spaan, Willy J.M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Published by Elsevier Inc. 1987
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7130946/
https://www.ncbi.nlm.nih.gov/pubmed/2825419
http://dx.doi.org/10.1016/0042-6822(87)90142-5
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author Luytjes, Willem
Sturman, Lawrence S.
Bredenbee, Peter J.
Charite, Jeroen
van der Zeijst, Bernard A.M.
Horzinek, Marian C.
Spaan, Willy J.M.
author_facet Luytjes, Willem
Sturman, Lawrence S.
Bredenbee, Peter J.
Charite, Jeroen
van der Zeijst, Bernard A.M.
Horzinek, Marian C.
Spaan, Willy J.M.
author_sort Luytjes, Willem
collection PubMed
description The nucleotide sequence of the peplomer (E2) gene of MHV-A59 was determined from a set of overlapping cDNA clones. The E2 gene encodes a protein of 1324 amino acids including a hydrophobic signal peptide. A second large hydrophobic domain is found near the COOH terminus and probably represents the membrane anchor. Twenty glycosylation sites are predicted. Cleavage of the E2 protein results in two different 90K species, 90A and 90B (L. S. Sturman, C. S. Ricard, and K. V. Holmes (1985)J. Virol. 56, 904–911), and activates cell fusion. Protein sequencing of the trypsin-generated N-terminus revealed the position of the cleavage site. 90A and 90B could be identified as the C-terminal and the N-terminal parts, respectively. Amino acid sequence comparison of the A59 and 1HM E2 proteins showed extensive homology and revealed a stretch of 89 amino acids in the 90B region of the A59 E2 protein that is absent in JHM.
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spelling pubmed-71309462020-04-08 Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site Luytjes, Willem Sturman, Lawrence S. Bredenbee, Peter J. Charite, Jeroen van der Zeijst, Bernard A.M. Horzinek, Marian C. Spaan, Willy J.M. Virology Article The nucleotide sequence of the peplomer (E2) gene of MHV-A59 was determined from a set of overlapping cDNA clones. The E2 gene encodes a protein of 1324 amino acids including a hydrophobic signal peptide. A second large hydrophobic domain is found near the COOH terminus and probably represents the membrane anchor. Twenty glycosylation sites are predicted. Cleavage of the E2 protein results in two different 90K species, 90A and 90B (L. S. Sturman, C. S. Ricard, and K. V. Holmes (1985)J. Virol. 56, 904–911), and activates cell fusion. Protein sequencing of the trypsin-generated N-terminus revealed the position of the cleavage site. 90A and 90B could be identified as the C-terminal and the N-terminal parts, respectively. Amino acid sequence comparison of the A59 and 1HM E2 proteins showed extensive homology and revealed a stretch of 89 amino acids in the 90B region of the A59 E2 protein that is absent in JHM. Published by Elsevier Inc. 1987-12 2004-02-09 /pmc/articles/PMC7130946/ /pubmed/2825419 http://dx.doi.org/10.1016/0042-6822(87)90142-5 Text en Copyright © 1987 Published by Elsevier Inc. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Luytjes, Willem
Sturman, Lawrence S.
Bredenbee, Peter J.
Charite, Jeroen
van der Zeijst, Bernard A.M.
Horzinek, Marian C.
Spaan, Willy J.M.
Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site
title Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site
title_full Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site
title_fullStr Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site
title_full_unstemmed Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site
title_short Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site
title_sort primary structure of the glycoprotein e2 of coronavirus mhv-a59 and identification of the trypsin cleavage site
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7130946/
https://www.ncbi.nlm.nih.gov/pubmed/2825419
http://dx.doi.org/10.1016/0042-6822(87)90142-5
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