Hepatitis C virus F protein sequence reveals a lack of functional constraints and a variable pattern of amino acid substitution
Date
2010-10-05Author
Cristina, Juan
López, Fernando
Moratorio, Gonzalo
López, Lilia
Vásquez, Silvia
García-Aguirre, Laura
Metadata
Show full item recordAbstract
Hepatitis C virus (HCV) is an important human pathogen that affects 170 million people
worldwide. The HCV genome is an RNA molecule that is approximately 9?6 kb in length and
encodes a polyprotein that is cleaved proteolytically to generate at least 10 mature viral proteins.
Recently, a new HCV protein named F has been described, which is synthesized as a result of
a ribosomal frameshift. Little is known about the biological properties of this protein, but the
possibility that the F protein may participate in HCV morphology or replication has been raised.
In this work, the presence of functional constraints in the F protein was investigated. It was found
that the rate of amino acid substitutions along the F protein was significantly higher than the rate
of synonymous substitutions, and comparisons involving genes that represented independent
phylogenetic lineages yielded very different divergence/conservation patterns. The distribution of
stop codons in the F protein across all HCV genotypes was also investigated; genotypes 2 and
3 were found to have more stop codons than genotype 1. The results of this work suggest
strongly that the pattern of divergence in the F protein is not affected by functional constraints.
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