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Immunogenetic and structural analysis of a class of HCV broadly neutralizing antibodies and their precursors.

Aleman F, Tzarum N, Kong L, Nagy K, Zhu J, Wilson IA, Law M
Proc Natl Acad Sci U S A 115 7569-7574 (2018)
Related entries: 6bzv, 6bzw, 6bzy

Cited: 12 times
EuropePMC logo PMID: 29954862

Abstract

Elicitation of broadly neutralizing antibodies (bnAbs) is a leading strategy in rational vaccine design against antigenically diverse pathogens. Here, we studied a panel of monoclonal antibodies (mAbs) from mice immunized with the hepatitis C virus (HCV) envelope glycoproteins E1E2. Six of the mAbs recognize the conserved E2 antigenic site 412-423 (AS412) and cross-neutralize diverse HCV genotypes. Immunogenetic and structural analysis revealed that the antibodies originated from two different germline (GL) precursors and bind AS412 in a β-hairpin conformation. Intriguingly, the anti-HCV activity of one antibody lineage is associated with maturation of the light chain (LC), whereas the other lineage is dependent on heavy-chain (HC) maturation. Crystal structures of GL precursors of the LC-dependent lineage in complex with AS412 offer critical insights into the maturation process of bnAbs to HCV, providing a scientific foundation for utilizing the mouse model to study AS412-targeting vaccine candidates.

Reviews - 6bzu mentioned but not cited (1)

  1. From Structural Studies to HCV Vaccine Design. Yechezkel I, Law M, Tzarum N. Viruses 13 833 (2021)

Articles - 6bzu mentioned but not cited (3)

  1. Flexibility and intrinsic disorder are conserved features of hepatitis C virus E2 glycoprotein. Stejskal L, Lees WD, Moss DS, Palor M, Bingham RJ, Shepherd AJ, Grove J. PLoS Comput Biol 16 e1007710 (2020)
  2. Immunogenetic and structural analysis of a class of HCV broadly neutralizing antibodies and their precursors. Aleman F, Tzarum N, Kong L, Nagy K, Zhu J, Wilson IA, Law M. Proc Natl Acad Sci U S A 115 7569-7574 (2018)
  3. In Silico Analysis of Neutralizing Antibody Epitopes on The Hepatitis C Virus Surface Glycoproteins. Zareh-Khoshchehreh R, Bamdad T, Arab SS, Behdani M, Biglar M. Cell J 25 62-72 (2023)


Reviews citing this publication (3)

  1. Hepatitis C Virus Envelope Glycoproteins: A Balancing Act of Order and Disorder. Yost SA, Wang Y, Marcotrigiano J. Front Immunol 9 1917 (2018)
  2. Antibody Responses in Hepatitis C Infection. Law M. Cold Spring Harb Perspect Med 11 a036962 (2021)
  3. Structural and Biophysical Characterization of the HCV E1E2 Heterodimer for Vaccine Development. Toth EA, Chagas A, Pierce BG, Fuerst TR. Viruses 13 1027 (2021)

Articles citing this publication (5)

  1. Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms. Billesbølle CB, Azumaya CM, Kretsch RC, Powers AS, Gonen S, Schneider S, Arvedson T, Dror RO, Cheng Y, Manglik A. Nature 586 807-811 (2020)
  2. Specific Antibodies Induced by Immunization with Hepatitis B Virus-Like Particles Carrying Hepatitis C Virus Envelope Glycoprotein 2 Epitopes Show Differential Neutralization Efficiency. Czarnota A, Offersgaard A, Pihl AF, Prentoe J, Bukh J, Gottwein JM, Bieńkowska-Szewczyk K, Grzyb K. Vaccines (Basel) 8 E294 (2020)
  3. Evaluation of a Series of Lipidated Tucaresol Adjuvants in a Hepatitis C Virus Vaccine Model. Belz TF, Olson ME, Giang E, Law M, Janda KD. ACS Med Chem Lett 11 2428-2432 (2020)
  4. Effect of Glycan Shift on Antibodies against Hepatitis C Virus E2 412-425 Epitope Elicited by Chimeric sHBsAg-Based Virus-Like Particles. Czarnota A, Offersgaard A, Owsianka A, Alzua GP, Bukh J, Gottwein JM, Patel AH, Bieńkowska-Szewczyk K, Grzyb K. Microbiol Spectr e0254622 (2023)
  5. Structure of engineered hepatitis C virus E1E2 ectodomain in complex with neutralizing antibodies. Metcalf MC, Janus BM, Yin R, Wang R, Guest JD, Pozharski E, Law M, Mariuzza RA, Toth EA, Pierce BG, Fuerst TR, Ofek G. Nat Commun 14 3980 (2023)


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