A Complete Mutational Fitness Map of the Hepatitis C Virus Nonstructural 3 Protease: Relation to Recognition by Cytotoxic T Lymphocytes | Zendy

Jonas Söderholm | Zendy; Matti Sällberg | Zendy

Open Access

A Complete Mutational Fitness Map of the Hepatitis C Virus Nonstructural 3 Protease: Relation to Recognition by Cytotoxic T Lymphocytes

Author(s) -

Jonas Söderholm,

Matti Sällberg

Publication year - 2006

Publication title -

the journal of infectious diseases

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.69

H-Index - 252

eISSN - 1537-6613

pISSN - 0022-1899

DOI - 10.1086/509513

Subject(s) - ns3 , protease , ns2 3 protease , biology , virology , epitope , virus , alanine , peptide sequence , hepatitis c virus , gene , biochemistry , amino acid , genetics , enzyme , antibody

The hepatitis C virus nonstructural (NS) 3/4A protease sequence is highly conserved for reasons not fully understood. We determined the protease activity in 181 NS3/4A gene products in which each protease residue was replaced by alanine or glycine. Unexpectedly, most (87%) protease residues could be replaced and protease activity would be retained. Using these data, we were able to identify a human leukocyte antigen A2-restricted epitope in which substitutions at 5 of 9 residues destroyed the protease. The NS3 protease shows an unexpectedly high plasticity, and it is therefore important to identify target sequences in which the appearance of mutations is restricted by viral fitness.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research