Hepatitis C virus envelope protein dynamics and the link to hypervariable region 1

Department of Immunology and Microbiology

Research output: Contribution to journal › Review › Research › peer-review

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Hepatitis C virus envelope protein dynamics and the link to hypervariable region 1. / Augestad, Elias H.; Bukh, Jens; Prentoe, Jannick.

In: Current Opinion in Virology, Vol. 50, 2021, p. 69-75.

Research output: Contribution to journal › Review › Research › peer-review

Harvard

Augestad, EH, Bukh, J & Prentoe, J 2021, 'Hepatitis C virus envelope protein dynamics and the link to hypervariable region 1', Current Opinion in Virology, vol. 50, pp. 69-75. https://doi.org/10.1016/j.coviro.2021.07.006

APA

Augestad, E. H., Bukh, J., & Prentoe, J. (2021). Hepatitis C virus envelope protein dynamics and the link to hypervariable region 1. Current Opinion in Virology, 50, 69-75. https://doi.org/10.1016/j.coviro.2021.07.006

Vancouver

Augestad EH, Bukh J, Prentoe J. Hepatitis C virus envelope protein dynamics and the link to hypervariable region 1. Current Opinion in Virology. 2021;50:69-75. https://doi.org/10.1016/j.coviro.2021.07.006

Author

Augestad, Elias H. ; Bukh, Jens ; Prentoe, Jannick. / Hepatitis C virus envelope protein dynamics and the link to hypervariable region 1. In: Current Opinion in Virology. 2021 ; Vol. 50. pp. 69-75.

Bibtex

@article{f22a81dd0a3c4de9a3dcd34b7454870b,

title = "Hepatitis C virus envelope protein dynamics and the link to hypervariable region 1",

abstract = "Conformational dynamics of viral envelope proteins seem to be involved in mediating evasion from neutralizing antibodies (NAbs) by mechanisms that limit exposure of conserved protein motifs. For hepatitis C virus (HCV), molecular studies have only recently begun to unveil how such dynamics of the envelope protein heterodimer, E1/E2, are linked to viral entry and NAb evasion. Here, we review data suggesting that E1/E2 exists in an equilibrium between theoretical {\textquoteleft}open{\textquoteright} (NAb-sensitive) and {\textquoteleft}closed{\textquoteright} (NAb-resistant) conformational states. We describe how this equilibrium is influenced by viral sequence polymorphisms and that it is critically dependent on the N-terminal region of E2, termed hypervariable region 1 (HVR1). Finally, we discuss how it appears that the virus binding site for the HCV entry co-receptor CD81 is less available in {\textquoteleft}closed{\textquoteright} E1/E2 states and that NAb-resistant viruses require a more intricate entry pathway involving also the entry co-receptor, SR-BI.",

author = "Augestad, {Elias H.} and Jens Bukh and Jannick Prentoe",

note = "Publisher Copyright: {\textcopyright} 2021 The Author(s)",

year = "2021",

doi = "10.1016/j.coviro.2021.07.006",

language = "English",

volume = "50",

pages = "69--75",

journal = "Current Opinion in Virology",

issn = "1879-6257",

publisher = "Elsevier Ltd. * Current Opinion Journals",

}

RIS

TY - JOUR

T1 - Hepatitis C virus envelope protein dynamics and the link to hypervariable region 1

AU - Augestad, Elias H.

AU - Bukh, Jens

AU - Prentoe, Jannick

PY - 2021

Y1 - 2021

N2 - Conformational dynamics of viral envelope proteins seem to be involved in mediating evasion from neutralizing antibodies (NAbs) by mechanisms that limit exposure of conserved protein motifs. For hepatitis C virus (HCV), molecular studies have only recently begun to unveil how such dynamics of the envelope protein heterodimer, E1/E2, are linked to viral entry and NAb evasion. Here, we review data suggesting that E1/E2 exists in an equilibrium between theoretical ‘open’ (NAb-sensitive) and ‘closed’ (NAb-resistant) conformational states. We describe how this equilibrium is influenced by viral sequence polymorphisms and that it is critically dependent on the N-terminal region of E2, termed hypervariable region 1 (HVR1). Finally, we discuss how it appears that the virus binding site for the HCV entry co-receptor CD81 is less available in ‘closed’ E1/E2 states and that NAb-resistant viruses require a more intricate entry pathway involving also the entry co-receptor, SR-BI.

AB - Conformational dynamics of viral envelope proteins seem to be involved in mediating evasion from neutralizing antibodies (NAbs) by mechanisms that limit exposure of conserved protein motifs. For hepatitis C virus (HCV), molecular studies have only recently begun to unveil how such dynamics of the envelope protein heterodimer, E1/E2, are linked to viral entry and NAb evasion. Here, we review data suggesting that E1/E2 exists in an equilibrium between theoretical ‘open’ (NAb-sensitive) and ‘closed’ (NAb-resistant) conformational states. We describe how this equilibrium is influenced by viral sequence polymorphisms and that it is critically dependent on the N-terminal region of E2, termed hypervariable region 1 (HVR1). Finally, we discuss how it appears that the virus binding site for the HCV entry co-receptor CD81 is less available in ‘closed’ E1/E2 states and that NAb-resistant viruses require a more intricate entry pathway involving also the entry co-receptor, SR-BI.

U2 - 10.1016/j.coviro.2021.07.006

DO - 10.1016/j.coviro.2021.07.006

M3 - Review

C2 - 34403905

AN - SCOPUS:85112419329

VL - 50

SP - 69

EP - 75

JO - Current Opinion in Virology

JF - Current Opinion in Virology

SN - 1879-6257

ER -

ID: 276651880