Aarhus University Seal / Aarhus Universitets segl

Nick Stub Laursen

Antibody recognition of the pandemic H1N1 Influenza virus hemagglutinin receptor binding site

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Standard

Antibody recognition of the pandemic H1N1 Influenza virus hemagglutinin receptor binding site. / Hong, Minsun; Lee, Peter S; Hoffman, Ryan M B; Zhu, Xueyong; Krause, Jens C; Laursen, Nick S; Yoon, Sung-Il; Song, Langzhou; Tussey, Lynda; Crowe, James E; Ward, Andrew B; Wilson, Ian A.

In: Journal of Virology, Vol. 87, No. 22, 11.2013, p. 12471-12480.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Hong, M, Lee, PS, Hoffman, RMB, Zhu, X, Krause, JC, Laursen, NS, Yoon, S-I, Song, L, Tussey, L, Crowe, JE, Ward, AB & Wilson, IA 2013, 'Antibody recognition of the pandemic H1N1 Influenza virus hemagglutinin receptor binding site', Journal of Virology, vol. 87, no. 22, pp. 12471-12480. https://doi.org/10.1128/JVI.01388-13

APA

Hong, M., Lee, P. S., Hoffman, R. M. B., Zhu, X., Krause, J. C., Laursen, N. S., Yoon, S-I., Song, L., Tussey, L., Crowe, J. E., Ward, A. B., & Wilson, I. A. (2013). Antibody recognition of the pandemic H1N1 Influenza virus hemagglutinin receptor binding site. Journal of Virology, 87(22), 12471-12480. https://doi.org/10.1128/JVI.01388-13

CBE

Hong M, Lee PS, Hoffman RMB, Zhu X, Krause JC, Laursen NS, Yoon S-I, Song L, Tussey L, Crowe JE, Ward AB, Wilson IA. 2013. Antibody recognition of the pandemic H1N1 Influenza virus hemagglutinin receptor binding site. Journal of Virology. 87(22):12471-12480. https://doi.org/10.1128/JVI.01388-13

MLA

Vancouver

Hong M, Lee PS, Hoffman RMB, Zhu X, Krause JC, Laursen NS et al. Antibody recognition of the pandemic H1N1 Influenza virus hemagglutinin receptor binding site. Journal of Virology. 2013 Nov;87(22):12471-12480. https://doi.org/10.1128/JVI.01388-13

Author

Hong, Minsun ; Lee, Peter S ; Hoffman, Ryan M B ; Zhu, Xueyong ; Krause, Jens C ; Laursen, Nick S ; Yoon, Sung-Il ; Song, Langzhou ; Tussey, Lynda ; Crowe, James E ; Ward, Andrew B ; Wilson, Ian A. / Antibody recognition of the pandemic H1N1 Influenza virus hemagglutinin receptor binding site. In: Journal of Virology. 2013 ; Vol. 87, No. 22. pp. 12471-12480.

Bibtex

@article{6df35c5edb4f43209b34eae6e393186b,
title = "Antibody recognition of the pandemic H1N1 Influenza virus hemagglutinin receptor binding site",
abstract = "Influenza virus is a global health concern due to its unpredictable pandemic potential. This potential threat was realized in 2009 when an H1N1 virus emerged that resembled the 1918 virus in antigenicity but fortunately was not nearly as deadly. 5J8 is a human antibody that potently neutralizes a broad spectrum of H1N1 viruses, including the 1918 and 2009 pandemic viruses. Here, we present the crystal structure of 5J8 Fab in complex with a bacterially expressed and refolded globular head domain from the hemagglutinin (HA) of the A/California/07/2009 (H1N1) pandemic virus. 5J8 recognizes a conserved epitope in and around the receptor binding site (RBS), and its HCDR3 closely mimics interactions of the sialic acid receptor. Electron microscopy (EM) reconstructions of 5J8 Fab in complex with an HA trimer from a 1986 H1 strain and with an engineered stabilized HA trimer from the 2009 H1 pandemic virus showed a similar mode of binding. As for other characterized RBS-targeted antibodies, 5J8 uses avidity to extend its breadth and affinity against divergent H1 strains. 5J8 selectively interacts with HA insertion residue 133a, which is conserved in pandemic H1 strains and has precluded binding of other RBS-targeted antibodies. Thus, the RBS of divergent HAs is targeted by 5J8 and adds to the growing arsenal of common recognition motifs for design of therapeutics and vaccines. Moreover, consistent with previous studies, the bacterially expressed H1 HA properly refolds, retaining its antigenic structure, and presents a low-cost and rapid alternative for engineering and manufacturing candidate flu vaccines.",
keywords = "Antibodies, Viral, Antibody Affinity, Antigens, Viral, Binding Sites, Antibody, Crystallography, X-Ray, Hemagglutinin Glycoproteins, Influenza Virus, Humans, Influenza A Virus, H1N1 Subtype, Influenza, Human, Models, Molecular, Pandemics, Protein Conformation, Receptors, Virus, United States",
author = "Minsun Hong and Lee, {Peter S} and Hoffman, {Ryan M B} and Xueyong Zhu and Krause, {Jens C} and Laursen, {Nick S} and Sung-Il Yoon and Langzhou Song and Lynda Tussey and Crowe, {James E} and Ward, {Andrew B} and Wilson, {Ian A}",
year = "2013",
month = nov,
doi = "10.1128/JVI.01388-13",
language = "English",
volume = "87",
pages = "12471--12480",
journal = "Journal of Virology",
issn = "0022-538X",
publisher = "American Society for Microbiology",
number = "22",

}

RIS

TY - JOUR

T1 - Antibody recognition of the pandemic H1N1 Influenza virus hemagglutinin receptor binding site

AU - Hong, Minsun

AU - Lee, Peter S

AU - Hoffman, Ryan M B

AU - Zhu, Xueyong

AU - Krause, Jens C

AU - Laursen, Nick S

AU - Yoon, Sung-Il

AU - Song, Langzhou

AU - Tussey, Lynda

AU - Crowe, James E

AU - Ward, Andrew B

AU - Wilson, Ian A

PY - 2013/11

Y1 - 2013/11

N2 - Influenza virus is a global health concern due to its unpredictable pandemic potential. This potential threat was realized in 2009 when an H1N1 virus emerged that resembled the 1918 virus in antigenicity but fortunately was not nearly as deadly. 5J8 is a human antibody that potently neutralizes a broad spectrum of H1N1 viruses, including the 1918 and 2009 pandemic viruses. Here, we present the crystal structure of 5J8 Fab in complex with a bacterially expressed and refolded globular head domain from the hemagglutinin (HA) of the A/California/07/2009 (H1N1) pandemic virus. 5J8 recognizes a conserved epitope in and around the receptor binding site (RBS), and its HCDR3 closely mimics interactions of the sialic acid receptor. Electron microscopy (EM) reconstructions of 5J8 Fab in complex with an HA trimer from a 1986 H1 strain and with an engineered stabilized HA trimer from the 2009 H1 pandemic virus showed a similar mode of binding. As for other characterized RBS-targeted antibodies, 5J8 uses avidity to extend its breadth and affinity against divergent H1 strains. 5J8 selectively interacts with HA insertion residue 133a, which is conserved in pandemic H1 strains and has precluded binding of other RBS-targeted antibodies. Thus, the RBS of divergent HAs is targeted by 5J8 and adds to the growing arsenal of common recognition motifs for design of therapeutics and vaccines. Moreover, consistent with previous studies, the bacterially expressed H1 HA properly refolds, retaining its antigenic structure, and presents a low-cost and rapid alternative for engineering and manufacturing candidate flu vaccines.

AB - Influenza virus is a global health concern due to its unpredictable pandemic potential. This potential threat was realized in 2009 when an H1N1 virus emerged that resembled the 1918 virus in antigenicity but fortunately was not nearly as deadly. 5J8 is a human antibody that potently neutralizes a broad spectrum of H1N1 viruses, including the 1918 and 2009 pandemic viruses. Here, we present the crystal structure of 5J8 Fab in complex with a bacterially expressed and refolded globular head domain from the hemagglutinin (HA) of the A/California/07/2009 (H1N1) pandemic virus. 5J8 recognizes a conserved epitope in and around the receptor binding site (RBS), and its HCDR3 closely mimics interactions of the sialic acid receptor. Electron microscopy (EM) reconstructions of 5J8 Fab in complex with an HA trimer from a 1986 H1 strain and with an engineered stabilized HA trimer from the 2009 H1 pandemic virus showed a similar mode of binding. As for other characterized RBS-targeted antibodies, 5J8 uses avidity to extend its breadth and affinity against divergent H1 strains. 5J8 selectively interacts with HA insertion residue 133a, which is conserved in pandemic H1 strains and has precluded binding of other RBS-targeted antibodies. Thus, the RBS of divergent HAs is targeted by 5J8 and adds to the growing arsenal of common recognition motifs for design of therapeutics and vaccines. Moreover, consistent with previous studies, the bacterially expressed H1 HA properly refolds, retaining its antigenic structure, and presents a low-cost and rapid alternative for engineering and manufacturing candidate flu vaccines.

KW - Antibodies, Viral

KW - Antibody Affinity

KW - Antigens, Viral

KW - Binding Sites, Antibody

KW - Crystallography, X-Ray

KW - Hemagglutinin Glycoproteins, Influenza Virus

KW - Humans

KW - Influenza A Virus, H1N1 Subtype

KW - Influenza, Human

KW - Models, Molecular

KW - Pandemics

KW - Protein Conformation

KW - Receptors, Virus

KW - United States

U2 - 10.1128/JVI.01388-13

DO - 10.1128/JVI.01388-13

M3 - Journal article

C2 - 24027321

VL - 87

SP - 12471

EP - 12480

JO - Journal of Virology

JF - Journal of Virology

SN - 0022-538X

IS - 22

ER -