Selected article for: "accession number and dna sequence"
Author: Brian G. Pierce; Zhen-Yong Keck; Ruixue Wang; Patrick Lau; Kyle Garagusi; Khadija Elkholy; Eric A. Toth; Richard A. Urbanowicz; Johnathan D. Guest; Pragati Agnihotri; Melissa C. Kerzic; Alexander Marin; Alexander K. Andrianov; Jonathan K. Ball; Roy A. Mariuzza; Thomas R. Fuerst; Steven K.H. Foung
Title: Structure-based design of hepatitis C virus E2 glycoprotein improves serum binding and cross-neutralization
  • Document date: 2020_4_17
    • ID: b6to1v4u_51
    Snippet: Cloning and characterization of E2 mutant antigenicity using ELISA was performed as described previously (28). Mutants were constructed in plasmids carrying the 1a H77C E1E2 coding sequence (GenBank accession number AF009606), as described previously (59) . All the mutations were confirmed by DNA sequence analysis (Elim Biopharmaceuticals, Inc., Hayward, CA) for the desired mutations and for absence of unexpected residue changes in the full-lengt.....
    Document: Cloning and characterization of E2 mutant antigenicity using ELISA was performed as described previously (28). Mutants were constructed in plasmids carrying the 1a H77C E1E2 coding sequence (GenBank accession number AF009606), as described previously (59) . All the mutations were confirmed by DNA sequence analysis (Elim Biopharmaceuticals, Inc., Hayward, CA) for the desired mutations and for absence of unexpected residue changes in the full-length E1E2-encoding sequence. The resulting plasmids were transfected into HEK 293T cells for transient protein expression using the calcium-phosphate method. Individual E2 protein expression was normalized by binding of CBH-17, an HCV E2 HMAb to a linear epitope (60) . Data are shown as mean values of two experiments performed in triplicate.

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