Variable and hypervariable domains are found in the regions of HCV corresponding to the flavivirus envelope and NS1 proteins and the pestivirus envelope glycoproteins
| Autor: | Ferruccio Bonino, Kevin Crawford, Kathy H. Richman, James W. Tung, Amy J. Weiner, Q L Choo, Jody Rosenblatt, Matthew J. Brauer, Giorgio Maria Saracco, Michael Houghton, Jang H. Han |
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| Rok vydání: | 1991 |
| Předmět: |
Signal peptide
Genes Viral Protein Conformation viruses Molecular Sequence Data Hepacivirus Viral Nonstructural Proteins Polymerase Chain Reaction Capsid Protein structure Viral Envelope Proteins Viral envelope Sequence Homology Nucleic Acid Virology Humans Amino Acid Sequence Gene Peptide sequence chemistry.chemical_classification Genetics Base Sequence biology Flavivirus Viral Core Proteins Pestivirus Nucleic acid sequence virus diseases biology.organism_classification Amino acid chemistry Oligonucleotide Probes Transcription Factors |
| Zdroj: | Virology. 180:842-848 |
| ISSN: | 0042-6822 |
| Popis: | Based on the flavi- and pestivirus model of genome organization for the hepatitis C virus (HCV) (1-5), the nucleotide and deduced amino acid sequences of the putative envelope (E1) and the junction between the E1 and NS1/envelope 2 (E2) region from six different human isolates of HCV were compared with the nucleotide and predicted amino acid sequences of the prototype hepatitis C virus (HCV-1) (5). The overall percentage of nucleotide and amino acid changes among all six isolates, including HCV-1, from nucleotide 713 to 1630 (amino acid 129 to 437) was between 3 and 7%, which is comparable to that seen in some flaviviruses (6-8). An analysis of the number of nucleotide and deduced amino acid sequence changes among all six isolates and HCV-1 revealed a moderately variable domain of approximately 40 amino acids in the E1 region and a hypervariable domain (Region V) of approximately 28 amino acids, which is directly downstream from a putative signal peptide sequence, in the junction between E1 and NS1/E2. A similar hypervariable domain is not found in the C-terminus of the envelope polypeptide or in the N-terminus of the NS1 polypeptide domain of the flaviviruses. These findings suggest that the mature NS1/E2 polypeptide starts about amino acid 380 and that the NS1/E2 domain may correspond to a second envelope glycoprotein as in the case of the pestivirus. The observed heterogeneity in the putative structural proteins of HCV may have important ramifications for future vaccine development. |
| Databáze: | OpenAIRE |
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