Author: Izquierdo, Laure; Oliveira, Catarina; Fournier, Carole; Descamps, Véronique; Morel, Virginie; Dubuisson, Jean; Brochot, Etienne; Francois, Catherine; Castelain, Sandrine; Duverlie, Gilles; Helle, Francois
Title: Hepatitis C Virus Resistance to Carbohydrate-Binding Agents Document date: 2016_2_12
ID: 1a4l1beo_33
Snippet: Since some of the mutations identified upon lectin exposure affected the N-glycosylation of E2 envelope protein which is known to protect the CD81 binding site from neutralizing antibodies, we also investigated the mutant sensitivity to the 3/11 neutralizing MAb and to a soluble form of the CD81 large extracellular loop (CD81-LEL). As shown in Fig 6A, we observed that V284A-V392D-S449P, M338V-L612M-L755M and M338V-A400D-L755M mutants were more se.....
Document: Since some of the mutations identified upon lectin exposure affected the N-glycosylation of E2 envelope protein which is known to protect the CD81 binding site from neutralizing antibodies, we also investigated the mutant sensitivity to the 3/11 neutralizing MAb and to a soluble form of the CD81 large extracellular loop (CD81-LEL). As shown in Fig 6A, we observed that V284A-V392D-S449P, M338V-L612M-L755M and M338V-A400D-L755M mutants were more sensitive to 3/11 neutralization than WT (more than 95% inhibition at 30 μg/mL compared to about 70% for WT) whereas M338V-N417S-L755M mutant was resistant (only 30% inhibition at 30 μg/mL). In addition, we noticed that M338V-L612M-L755M and M338V-N417S-L755M mutants were slightly more sensitive to CD81-LEL inhibition than WT (more than 85% inhibition at 10 μg/mL compared to about 50% for WT; Fig 6B) .
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