IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v7y2016i1d10.1038_ncomms11544.html
   My bibliography  Save this article

Most neutralizing human monoclonal antibodies target novel epitopes requiring both Lassa virus glycoprotein subunits

Author

Listed:
  • James E. Robinson

    (Section of Infectious Disease, Tulane University School of Medicine)

  • Kathryn M. Hastie

    (Scripps Research Institute)

  • Robert W. Cross

    (University of Texas Medical Branch at Galveston)

  • Rachael E. Yenni

    (Tulane University School of Medicine)

  • Deborah H. Elliott

    (Section of Infectious Disease, Tulane University School of Medicine)

  • Julie A. Rouelle

    (Section of Infectious Disease, Tulane University School of Medicine)

  • Chandrika B. Kannadka

    (Section of Infectious Disease, Tulane University School of Medicine)

  • Ashley A. Smira

    (Section of Infectious Disease, Tulane University School of Medicine)

  • Courtney E. Garry

    (Section of Infectious Disease, Tulane University School of Medicine
    Autoimmune Technologies, LLC, 1010 Common St #1705)

  • Benjamin T. Bradley

    (Section of Infectious Disease, Tulane University School of Medicine)

  • Haini Yu

    (Section of Infectious Disease, Tulane University School of Medicine)

  • Jeffrey G. Shaffer

    (Tulane School of Public Health and Tropical Medicine)

  • Matt L. Boisen

    (Corgenix, Inc.)

  • Jessica N. Hartnett

    (Tulane University School of Medicine)

  • Michelle A. Zandonatti

    (Scripps Research Institute)

  • Megan M. Rowland

    (Zalgen Labs, LLC)

  • Megan L. Heinrich

    (Zalgen Labs, LLC)

  • Luis Martínez-Sobrido

    (University of Rochester)

  • Benson Cheng

    (University of Rochester)

  • Juan C. de la Torre

    (Scripps Research Institute)

  • Kristian G. Andersen

    (Scripps Research Institute)

  • Augustine Goba

    (Viral Hemorrhagic Fever Program, Kenema Government Hospital)

  • Mambu Momoh

    (Viral Hemorrhagic Fever Program, Kenema Government Hospital
    Department of Laboratory Sciences Polytechnic College)

  • Mohamed Fullah

    (Viral Hemorrhagic Fever Program, Kenema Government Hospital
    Department of Laboratory Sciences Polytechnic College)

  • Michael Gbakie

    (Viral Hemorrhagic Fever Program, Kenema Government Hospital)

  • Lansana Kanneh

    (Viral Hemorrhagic Fever Program, Kenema Government Hospital)

  • Veronica J. Koroma

    (Viral Hemorrhagic Fever Program, Kenema Government Hospital)

  • Richard Fonnie

    (Viral Hemorrhagic Fever Program, Kenema Government Hospital)

  • Simbirie C. Jalloh

    (Viral Hemorrhagic Fever Program, Kenema Government Hospital)

  • Brima Kargbo

    (Ministry of Health and Sanitation)

  • Mohamed A. Vandi

    (Viral Hemorrhagic Fever Program, Kenema Government Hospital
    Ministry of Health and Sanitation)

  • Momoh Gbetuwa

    (Viral Hemorrhagic Fever Program, Kenema Government Hospital
    Ministry of Health and Sanitation)

  • Odia Ikponmwosa

    (Institute of Lassa Fever Research and Control, Irrua Specialist Teaching Hospital)

  • Danny A. Asogun

    (Institute of Lassa Fever Research and Control, Irrua Specialist Teaching Hospital)

  • Peter O. Okokhere

    (Institute of Lassa Fever Research and Control, Irrua Specialist Teaching Hospital)

  • Onikepe A. Follarin

    (Institute of Lassa Fever Research and Control, Irrua Specialist Teaching Hospital
    College of Natural Sciences, Redeemer’s University
    African Center of Excellence for Genomics of Infectious Disease (ACEGID), Redeemer’s University)

  • John S. Schieffelin

    (Section of Infectious Disease, Tulane University School of Medicine
    Section of Infectious Disease, Tulane University School of Medicine)

  • Kelly R. Pitts

    (Corgenix, Inc.)

  • Joan B. Geisbert

    (University of Texas Medical Branch at Galveston)

  • Peter C. Kulakoski

    (Autoimmune Technologies, LLC, 1010 Common St #1705)

  • Russell B. Wilson

    (Autoimmune Technologies, LLC, 1010 Common St #1705)

  • Christian T. Happi

    (Institute of Lassa Fever Research and Control, Irrua Specialist Teaching Hospital
    College of Natural Sciences, Redeemer’s University
    African Center of Excellence for Genomics of Infectious Disease (ACEGID), Redeemer’s University)

  • Pardis C. Sabeti

    (Center for Systems Biology, Harvard University
    Center for Systems Biology, Broad Institute of Massachusetts Institute of Technology (MIT) and Harvard
    Harvard School of Public Health)

  • Sahr M. Gevao

    (University of Sierra Leone)

  • S. Humarr Khan

    (Viral Hemorrhagic Fever Program, Kenema Government Hospital
    Ministry of Health and Sanitation)

  • Donald S. Grant

    (Viral Hemorrhagic Fever Program, Kenema Government Hospital
    Ministry of Health and Sanitation)

  • Thomas W. Geisbert

    (University of Texas Medical Branch at Galveston)

  • Erica Ollmann Saphire

    (Scripps Research Institute
    The Skaggs Institute for Chemical Biology, The Scripps Research Institute)

  • Luis M. Branco

    (Zalgen Labs, LLC)

  • Robert F. Garry

    (Tulane University School of Medicine
    Zalgen Labs, LLC)

Abstract

Lassa fever is a severe multisystem disease that often has haemorrhagic manifestations. The epitopes of the Lassa virus (LASV) surface glycoproteins recognized by naturally infected human hosts have not been identified or characterized. Here we have cloned 113 human monoclonal antibodies (mAbs) specific for LASV glycoproteins from memory B cells of Lassa fever survivors from West Africa. One-half bind the GP2 fusion subunit, one-fourth recognize the GP1 receptor-binding subunit and the remaining fourth are specific for the assembled glycoprotein complex, requiring both GP1 and GP2 subunits for recognition. Notably, of the 16 mAbs that neutralize LASV, 13 require the assembled glycoprotein complex for binding, while the remaining 3 require GP1 only. Compared with non-neutralizing mAbs, neutralizing mAbs have higher binding affinities and greater divergence from germline progenitors. Some mAbs potently neutralize all four LASV lineages. These insights from LASV human mAb characterization will guide strategies for immunotherapeutic development and vaccine design.

Suggested Citation

  • James E. Robinson & Kathryn M. Hastie & Robert W. Cross & Rachael E. Yenni & Deborah H. Elliott & Julie A. Rouelle & Chandrika B. Kannadka & Ashley A. Smira & Courtney E. Garry & Benjamin T. Bradley &, 2016. "Most neutralizing human monoclonal antibodies target novel epitopes requiring both Lassa virus glycoprotein subunits," Nature Communications, Nature, vol. 7(1), pages 1-14, September.
  • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11544
    DOI: 10.1038/ncomms11544
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms11544
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/ncomms11544?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Adam J. Ronk & Nicole M. Lloyd & Min Zhang & Caroline Atyeo & Hailee R. Perrett & Chad E. Mire & Kathryn M. Hastie & Rogier W. Sanders & Philip J. M. Brouwer & Erica Olmann Saphire & Andrew B. Ward & , 2023. "A Lassa virus mRNA vaccine confers protection but does not require neutralizing antibody in a guinea pig model of infection," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    2. Jason Gorman & Crystal Sao-Fong Cheung & Zhijian Duan & Li Ou & Maple Wang & Xuejun Chen & Cheng Cheng & Andrea Biju & Yaping Sun & Pengfei Wang & Yongping Yang & Baoshan Zhang & Jeffrey C. Boyington , 2024. "Cleavage-intermediate Lassa virus trimer elicits neutralizing responses, identifies neutralizing nanobodies, and reveals an apex-situated site-of-vulnerability," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11544. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.