@article{mbs:/content/journal/jgv/10.1099/0022-1317-68-7-1883, author = "Rasschaert, Denis and Laude, Hubert", title = "The Predicted Primary Structure of the Peplomer Protein E2 of the Porcine Coronavirus Transmissible Gastroenteritis Virus", journal= "Journal of General Virology", year = "1987", volume = "68", number = "7", pages = "1883-1890", doi = "https://doi.org/10.1099/0022-1317-68-7-1883", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-68-7-1883", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", keywords = "peplomer protein E2", keywords = "gene sequence", keywords = "TGEV", abstract = "Summary The complete nucleotide sequence of cloned cDNAs containing the E2 glycoproteinencoding region of the genome of transmissible gastroenteritis virus (TGEV) has been determined. A single large translatable frame of 4·3 kb starting at 8·2 kb from the 3′ end of the genome was identified. Its deduced amino acid sequence contains the characteristic features of a coronavirus peplomer protein: (i) the precursor polypeptide of TGEV E2 is 1447 residues long (i.e. 285 longer than the avian infectious bronchitis coronavirus spike protein); (ii) partial N-terminal sequencing demonstrated that a putative secretory signal sequence of 16 amino acids is absent in the virion-associated protein; (iii) the predicted mol. wt. of the apoprotein is 158K; most of the 32 potential N-glycosylation sites available in the sequence are presumed to be functional to account for the difference between this and the experimentally determined value (200K to 220K); (iv) a typical hydrophobic sequence near the C terminus is likely to be responsible for anchoring the peplomer to the virion envelope.", }