Author: Laude, H; Rasschaert, D; Huet, J C
Title: Sequence and N-terminal processing of the transmembrane protein E1 of the coronavirus transmissible gastroenteritis virus. Cord-id: 6ea63e64 Document date: 1987_1_1
ID: 6ea63e64
Snippet: Sequencing of part of a clone from a transmissible gastroenteritis virus genome cDNA library led to the identification of the gene encoding the E1 matrix protein. The amino acid sequence of the primary translation product predicts a polypeptide of 262 residues which shares many features with the previously characterized murine hepatitis virus and infectious bronchitis virus E1 proteins. However, N-terminal amino acid sequencing revealed that a putative signal peptide of 17 residues was absent in
Document: Sequencing of part of a clone from a transmissible gastroenteritis virus genome cDNA library led to the identification of the gene encoding the E1 matrix protein. The amino acid sequence of the primary translation product predicts a polypeptide of 262 residues which shares many features with the previously characterized murine hepatitis virus and infectious bronchitis virus E1 proteins. However, N-terminal amino acid sequencing revealed that a putative signal peptide of 17 residues was absent in the virion-associated polypeptide. The predicted mol. wt. of the mature unglycosylated product, 27,800, is in agreement with the experimental Mr value.
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