An alternate conformation of HCV E2 neutralizing face as an additional vaccine target

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

An alternate conformation of HCV E2 neutralizing face as an additional vaccine target. / Tzarum, Netanel; Giang, Erick; Kadam, Rameshwar U.; Chen, Fang; Nagy, Kenna; Augestad, Elias H.; Velázquez-Moctezuma, Rodrigo; Keck, Zhen Yong; Hua, Yuanzi; Stanfield, Robyn L.; Dreux, Marlene; Prentoe, Jannick; Foung, Steven K.H.; Bukh, Jens; Wilson, Ian A.; Law, Mansun.

In: Science Advances, Vol. 6, No. 30, abb5642, 2020.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Tzarum, N, Giang, E, Kadam, RU, Chen, F, Nagy, K, Augestad, EH, Velázquez-Moctezuma, R, Keck, ZY, Hua, Y, Stanfield, RL, Dreux, M, Prentoe, J, Foung, SKH, Bukh, J, Wilson, IA & Law, M 2020, 'An alternate conformation of HCV E2 neutralizing face as an additional vaccine target', Science Advances, vol. 6, no. 30, abb5642. https://doi.org/10.1126/sciadv.abb5642

APA

Tzarum, N., Giang, E., Kadam, R. U., Chen, F., Nagy, K., Augestad, E. H., Velázquez-Moctezuma, R., Keck, Z. Y., Hua, Y., Stanfield, R. L., Dreux, M., Prentoe, J., Foung, S. K. H., Bukh, J., Wilson, I. A., & Law, M. (2020). An alternate conformation of HCV E2 neutralizing face as an additional vaccine target. Science Advances, 6(30), [abb5642]. https://doi.org/10.1126/sciadv.abb5642

Vancouver

Tzarum N, Giang E, Kadam RU, Chen F, Nagy K, Augestad EH et al. An alternate conformation of HCV E2 neutralizing face as an additional vaccine target. Science Advances. 2020;6(30). abb5642. https://doi.org/10.1126/sciadv.abb5642

Author

Tzarum, Netanel ; Giang, Erick ; Kadam, Rameshwar U. ; Chen, Fang ; Nagy, Kenna ; Augestad, Elias H. ; Velázquez-Moctezuma, Rodrigo ; Keck, Zhen Yong ; Hua, Yuanzi ; Stanfield, Robyn L. ; Dreux, Marlene ; Prentoe, Jannick ; Foung, Steven K.H. ; Bukh, Jens ; Wilson, Ian A. ; Law, Mansun. / An alternate conformation of HCV E2 neutralizing face as an additional vaccine target. In: Science Advances. 2020 ; Vol. 6, No. 30.

Bibtex

@article{880d401bfef145b78dd7f048e7666ecf,
title = "An alternate conformation of HCV E2 neutralizing face as an additional vaccine target",
abstract = "To achieve global elimination of hepatitis C virus (HCV), an effective cross-genotype vaccine is needed. The HCV envelope glycoprotein E2 is the main target for neutralizing antibodies (nAbs), which aid in HCV clearance and protection. E2 is structurally flexible and functions in engaging host receptors. Many nAbs bind to the “neutralizing face” on E2, including several broadly nAbs encoded by the VH1-69 germline gene family that bind to a similar conformation (A) of this face. Here, a previously unknown conformation (B) of the neutralizing face is revealed in crystal structures of two of four additional E2-VH1-69 nAb complexes. In this conformation, the E2 front-layer region is displaced upon antibody binding, exposing residues in the back layer for direct antibody interaction. This E2 B structure may represent another conformational state in the viral entry process that is susceptible to antibody neutralization and thus provide a new target for rational vaccine development.",
author = "Netanel Tzarum and Erick Giang and Kadam, {Rameshwar U.} and Fang Chen and Kenna Nagy and Augestad, {Elias H.} and Rodrigo Vel{\'a}zquez-Moctezuma and Keck, {Zhen Yong} and Yuanzi Hua and Stanfield, {Robyn L.} and Marlene Dreux and Jannick Prentoe and Foung, {Steven K.H.} and Jens Bukh and Wilson, {Ian A.} and Mansun Law",
year = "2020",
doi = "10.1126/sciadv.abb5642",
language = "English",
volume = "6",
journal = "Science advances",
issn = "2375-2548",
publisher = "American Association for the Advancement of Science",
number = "30",

}

RIS

TY - JOUR

T1 - An alternate conformation of HCV E2 neutralizing face as an additional vaccine target

AU - Tzarum, Netanel

AU - Giang, Erick

AU - Kadam, Rameshwar U.

AU - Chen, Fang

AU - Nagy, Kenna

AU - Augestad, Elias H.

AU - Velázquez-Moctezuma, Rodrigo

AU - Keck, Zhen Yong

AU - Hua, Yuanzi

AU - Stanfield, Robyn L.

AU - Dreux, Marlene

AU - Prentoe, Jannick

AU - Foung, Steven K.H.

AU - Bukh, Jens

AU - Wilson, Ian A.

AU - Law, Mansun

PY - 2020

Y1 - 2020

N2 - To achieve global elimination of hepatitis C virus (HCV), an effective cross-genotype vaccine is needed. The HCV envelope glycoprotein E2 is the main target for neutralizing antibodies (nAbs), which aid in HCV clearance and protection. E2 is structurally flexible and functions in engaging host receptors. Many nAbs bind to the “neutralizing face” on E2, including several broadly nAbs encoded by the VH1-69 germline gene family that bind to a similar conformation (A) of this face. Here, a previously unknown conformation (B) of the neutralizing face is revealed in crystal structures of two of four additional E2-VH1-69 nAb complexes. In this conformation, the E2 front-layer region is displaced upon antibody binding, exposing residues in the back layer for direct antibody interaction. This E2 B structure may represent another conformational state in the viral entry process that is susceptible to antibody neutralization and thus provide a new target for rational vaccine development.

AB - To achieve global elimination of hepatitis C virus (HCV), an effective cross-genotype vaccine is needed. The HCV envelope glycoprotein E2 is the main target for neutralizing antibodies (nAbs), which aid in HCV clearance and protection. E2 is structurally flexible and functions in engaging host receptors. Many nAbs bind to the “neutralizing face” on E2, including several broadly nAbs encoded by the VH1-69 germline gene family that bind to a similar conformation (A) of this face. Here, a previously unknown conformation (B) of the neutralizing face is revealed in crystal structures of two of four additional E2-VH1-69 nAb complexes. In this conformation, the E2 front-layer region is displaced upon antibody binding, exposing residues in the back layer for direct antibody interaction. This E2 B structure may represent another conformational state in the viral entry process that is susceptible to antibody neutralization and thus provide a new target for rational vaccine development.

U2 - 10.1126/sciadv.abb5642

DO - 10.1126/sciadv.abb5642

M3 - Journal article

C2 - 32754640

AN - SCOPUS:85089131003

VL - 6

JO - Science advances

JF - Science advances

SN - 2375-2548

IS - 30

M1 - abb5642

ER -

ID: 249772599