ZO-2 determines cell membrane localization of receptor NTCP and supports hepatitis B virus infection

Although a number of candidates have been reported to bind to the hepatitis B virus (HBV) envelope, accumulating evidence indicates that NTCP is accepted as a functional receptor for HBV infection. Thus, NTCP is an attractive target for antiviral therapies. Here, we showed that ZO-2 interacts with NTCP. The silencing of ZO-2 decreased HBV infection, whereas ZO-1 and ZO-3 knockdown had no effect on HBV infection. Moreover, knockout of ZO-2 induced the downregulation of NTCP from the cell surface. This aberrant NTCP localization causes the reduction of the half-life of NTCP in ZO-2 knockout cells. PreS1 treatment or HBV infection disrupted the NTCP/ZO-2 complex through the dissociation of the actin-binding domain of ZO-2, leading to internalization of a newly formed preS1/NTCP/actin complex into the cell. The actin polymerization inhibitor latrunculin A suppressed HBV infection. These results suggest that ZO-2 regulates cell surface localization of NTCP.

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Publication Details

Journal
mBio
Published
2026-03-23
DOI
https://doi.org/10.1128/mbio.02704-25
Primary Topic
Heme Oxygenase-1 and Carbon Monoxide
Type
article
Field-Weighted Citation Impact
0.00
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article

ZO-2 determines cell membrane localization of receptor NTCP and supports hepatitis B virus infection

M. Yamasaki, Hironori Nishitsuji, Taro Tachibana, Saori Yoshimura et al.
mBio
Heme Oxygenase-1 and Carbon Monoxide
article

ZO-2 determines cell membrane localization of receptor NTCP and supports hepatitis B virus infection

M. Yamasaki, Hironori Nishitsuji, Taro Tachibana, Saori Yoshimura, Masaya Sugiyama, Daijiro Konno, Kunitada Shimotohno, Takayuki Murata, Masashi Mizokami
article en

Abstract

Although a number of candidates have been reported to bind to the hepatitis B virus (HBV) envelope, accumulating evidence indicates that NTCP is accepted as a functional receptor for HBV infection. Thus, NTCP is an attractive target for antiviral therapies. Here, we showed that ZO-2 interacts with NTCP. The silencing of ZO-2 decreased HBV infection, whereas ZO-1 and ZO-3 knockdown had no effect on HBV infection. Moreover, knockout of ZO-2 induced the downregulation of NTCP from the cell surface. This aberrant NTCP localization causes the reduction of the half-life of NTCP in ZO-2 knockout cells. PreS1 treatment or HBV infection disrupted the NTCP/ZO-2 complex through the dissociation of the actin-binding domain of ZO-2, leading to internalization of a newly formed preS1/NTCP/actin complex into the cell. The actin polymerization inhibitor latrunculin A suppressed HBV infection. These results suggest that ZO-2 regulates cell surface localization of NTCP.

mBio
Fujita Health University (JP), Metropolitan University (RS), National Center for Global Health and Medicine (JP), Microbial Chemistry Research Foundation (JP), Cellular Research (United States) (US), Cell Medica (Switzerland) (CH), Celladon Corporation (United States) (US), Kindai University (JP)
Good health and well-being
Openalex Percentile: Top 13%
Heme Oxygenase-1 and Carbon Monoxide
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ZO-2 determines cell membrane localization of receptor NTCP and supports hepatitis B virus infection — M. Yamasaki, Hironori Nishitsuji, et al. · mBio (2026) | TGRS Research Map | TGRS