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Sequence and N-terminal processing of the transmembrane protein E1 of the coronavirus transmissible gastroenteritis
Abstract:
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.
Insights
Researchers identified the transmissible gastroenteritis virus E1 matrix protein gene. The mature protein lacks a predicted signal peptide, aligning with experimental data for this important viral protein.
Area of Science:
- Virology
- Molecular Biology
- Protein Chemistry
Background:
- Transmissible gastroenteritis virus (TGEV) is a significant pathogen in swine.
- Understanding viral protein structure is crucial for developing antiviral strategies.
- The E1 matrix protein's role in TGEV infection requires detailed characterization.
Purpose of the Study:
- To identify and characterize the gene encoding the E1 matrix protein of TGEV.
- To analyze the primary translation product and mature E1 protein structure.
- To compare TGEV E1 protein features with related coronaviruses.
Main Methods:
- Sequencing of a TGEV genome cDNA library clone.
- Amino acid sequence analysis of the predicted translation product.
- N-terminal amino acid sequencing of the virion-associated E1 protein.
Main Results:
- Identification of the TGEV E1 matrix protein gene.
- The primary translation product consists of 262 residues.
- A predicted 17-residue signal peptide is absent in the mature, virion-associated E1 protein.
- Predicted unglycosylated molecular weight matches experimental values.
Conclusions:
- The E1 matrix protein of TGEV shares structural similarities with homologous proteins from other coronaviruses.
- Post-translational processing removes the putative signal peptide from the mature TGEV E1 protein.
- This characterization provides foundational knowledge for TGEV molecular biology.