Abstract
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.
MeSH Terms
Amino Acid Sequence
Animals
Base Sequence
Gene Products, env/genetics
Gene Products, pol/genetics
Genes, Viral
Humans
Molecular Sequence Data
Retroviridae/genetics
Sequence Homology, Nucleic Acid
Species Specificity
Spumavirus/genetics
Viral Structural Proteins/genetics
Chemicals
Gene Products, env
Gene Products, pol
Viral Structural Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Mergia A
Department of Pathology, School of Medicine, University of California, Davis 95616.
Shaw K E
Lackner J E
Luciw P A
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