Relationship of the env genes and the endonuclease domain of the pol genes of simian foamy virus type 1 and human foamy virus
| Autor: | Paul A. Luciw, Karen E. S. Shaw, J. E. Lackner, Ayalew Mergia |
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| Jazyk: | angličtina |
| Rok vydání: | 1990 |
| Předmět: |
Genes
Viral Sequence analysis viruses Immunology Molecular Sequence Data Gene Products pol Sequence alignment Simian foamy virus Biology Microbiology Species Specificity Virology Sequence Homology Nucleic Acid Animals Humans Amino Acid Sequence Spumavirus Gene Peptide sequence Genetics Viral Structural Proteins Base Sequence virus diseases Gene Products env Human foamy virus biochemical phenomena metabolism and nutrition biology.organism_classification Open reading frame Retroviridae Insect Science Research Article |
| Popis: | We have molecularly cloned and sequenced a portion of the simian foamy virus type 1 (SFV-1); open reading frames representing the endonuclease domain of the polymerase (pol) and the envelope (env) genes were identified by comparison with the human foamy virus (HFV). Unlike the HFV genomic organization, the SFV-1 pol gene overlaps the env gene; thus, the open reading frames reported for HFV between pol and env is not present in SFV-1. Comparisons of predicted amino acid sequences of HFV and SFV-1 reveal that the endonuclease domains of the pol genes are about 84% related. The region predicted to encode the SFV-1 extracellular env domain is 569 codons; SFV-1 and HFV have 64% amino acid similarity in this env domain. The predicted hydrophobic transmembrane env proteins of both HFV and SFV-1 show about 73% similarity. A total of 16 potential glycosylation sites are found in SFV-1 env, and 15 are found in HFV; 11 are shared. SFV-1 has 25 cysteine residues, and HFV has 23 residues; all 23 cysteine residues of HFV are conserved in SFV-1. This sequence analysis reveals that the human and simian foamy viruses are highly related. |
| Databáze: | OpenAIRE |
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