Jan 1, 2019 · Our findings indicate that AR4A targets a low-variation epitope with a high barrier to resistance, which in conjunction with high AR4A cross-genotype conservation makes the epitope a prime candidate for inclusion in HCV vaccine candidates.

Here, we present the cryo–electron microscopy structure of the membrane-extracted full-length E1E2 heterodimer in complex with three broadly neutralizing antibodies—AR4A, AT1209, and IGH505—at ~3.5-angstrom resolution.

Apr 4, 2012 · In particular, the mAb AR4A, recognizing a discontinuous epitope outside the CD81bs on the E1E2 complex, has an exceptionally broad neutralizing activity toward diverse HCV genotypes and protects against heterologous HCV challenge in a small animal model.

Jul 5, 2023 · Here, we present a cryo-EM structure of an engineered, secreted E1E2 ectodomain of genotype 1b in complex with neutralizing antibodies AR4A, HEPC74, and IGH520.

Jul 1, 2019 · AR3-specific antibodies neutralized HCV pseudoparticles and cell culture viruses. A large number of clearers develop antibodies targeting antigenic region 4 (AR4). AR4-specific antibody AT1618 also neutralized neutralization-resistant variants.

Feb 17, 2023 · We evaluated passaged viruses for fitness in viral kinetic assays and for exposure of conserved neutralizing epitopes using mAb targeting AR2, AR3, AR4, and AR5 in neutralization assays.

Jul 28, 2021 · E1E2 variants with resistance to both HC33.4 (an AS412 bNAb) and AR4A (an E1E2 bNAb) were identified using a large panel of HCVpp generated using natural E1E2 isolates.

Jan 1, 2019 · Global control of hepatitis C virus (HCV) depends on development of a prophylactic vaccine. We studied escape for cross-genotype-reactive neutralizing antibody AR4A, providing valuable information for HCV vaccine design. We cultured HCV core-NS2 recombinants H77 (genotype 1a)/JFH1 or the highly anti …

The exporter needs to apply on a form known as AR4 or AR4A to the Central Excise Range Superintendent for obtaining excise clearance. Form A is filed when goods are to be cleared after examination by the excise

Here, we present the cryo–electron microscopy structure of the membrane-extracted full-length E1E2 heterodimer in complex with three broadly neutralizing antibodies — AR4A, AT1209, and IGH505 at ~3.5-angstrom resolution.