- Adenosylhomocysteinase like 1 interacts with nonstructural 5A and regulates hepatitis C virus propagation
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Yun-Sook Lim , Han N. Mai , Lap P. Nguyen , Sang Min Kang , Dongseob Tark , Soon B. Hwang
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J. Microbiol. 2021;59(1):101-109. Published online December 23, 2020
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DOI: https://doi.org/10.1007/s12275-021-0470-8
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 Abstract
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Hepatitis C virus (HCV) life cycle is highly dependent on cellular
proteins for viral propagation. In order to identify the
cellular factors involved in HCV propagation, we previously
performed a protein microarray assay using the HCV nonstructural
5A (NS5A) protein as a probe. Of ~9,000 human
cellular proteins immobilized in a microarray, adenosylhomocysteinase
like 1 (AHCYL1) was among 90 proteins identified
as NS5A interactors. Of these candidates, AHCYL1 was
selected for further study. In the present study, we verified
the physical interaction between NS5A and AHCYL1 by both
in vitro pulldown and coimmunoprecipitation assays. Furthermore,
HCV NS5A interacted with endogenous AHCYL1 in
Jc1-infected cells. Both NS5A and AHCYL1 were colocalized
in the cytoplasmic region in HCV-replicating cells. siRNAmediated
knockdown of AHCYL1 abrogated HCV propagation.
Exogenous expression of the siRNA-resistant AHCYL1
mutant, but not of the wild-type AHCYL1, restored HCV protein
expression levels, indicating that AHCYL1 was required
specifically for HCV propagation. Importantly, AHCYL1 was
involved in the HCV internal ribosome entry site-mediated
translation step of the HCV life cycle. Finally, we demonstrated
that the proteasomal degradation pathway of AHCYL1 was
modulated by persistent HCV infection. Collectively, these
data suggest that HCV may modulate the AHCYL1 protein
to promote viral propagation.
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Citations
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