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Global site-specific N-glycosylation analysis of HIV envelope glycoprotein

Author

Listed:
  • Liwei Cao

    (The Scripps Research Institute)

  • Jolene K. Diedrich

    (The Scripps Research Institute)

  • Daniel W. Kulp

    (The Scripps Research Institute
    The Scripps Research Institute)

  • Matthias Pauthner

    (The Scripps Research Institute
    The Scripps Research Institute)

  • Lin He

    (The Scripps Research Institute)

  • Sung-Kyu Robin Park

    (The Scripps Research Institute)

  • Devin Sok

    (The Scripps Research Institute
    The Scripps Research Institute)

  • Ching Yao Su

    (The Scripps Research Institute)

  • Claire M. Delahunty

    (The Scripps Research Institute)

  • Sergey Menis

    (The Scripps Research Institute)

  • Raiees Andrabi

    (The Scripps Research Institute)

  • Javier Guenaga

    (The Scripps Research Institute)

  • Erik Georgeson

    (The Scripps Research Institute)

  • Michael Kubitz

    (The Scripps Research Institute)

  • Yumiko Adachi

    (The Scripps Research Institute)

  • Dennis R. Burton

    (The Scripps Research Institute
    The Scripps Research Institute)

  • William R. Schief

    (The Scripps Research Institute
    The Scripps Research Institute)

  • John R. Yates III

    (The Scripps Research Institute)

  • James C. Paulson

    (The Scripps Research Institute
    The Scripps Research Institute
    The Scripps Research Institute)

Abstract

HIV-1 envelope glycoprotein (Env) is the sole target for broadly neutralizing antibodies (bnAbs) and the focus for design of an antibody-based HIV vaccine. The Env trimer is covered by ∼90N-linked glycans, which shield the underlying protein from immune surveillance. bNAbs to HIV develop during infection, with many showing dependence on glycans for binding to Env. The ability to routinely assess the glycan type at each glycosylation site may facilitate design of improved vaccine candidates. Here we present a general mass spectrometry-based proteomics strategy that uses specific endoglycosidases to introduce mass signatures that distinguish peptide glycosites that are unoccupied or occupied by high-mannose/hybrid or complex-type glycans. The method yields >95% sequence coverage for Env, provides semi-quantitative analysis of the glycosylation status at each glycosite. We find that most glycosites in recombinant Env trimers are fully occupied by glycans, varying in the proportion of high-mannose/hybrid and complex-type glycans.

Suggested Citation

  • Liwei Cao & Jolene K. Diedrich & Daniel W. Kulp & Matthias Pauthner & Lin He & Sung-Kyu Robin Park & Devin Sok & Ching Yao Su & Claire M. Delahunty & Sergey Menis & Raiees Andrabi & Javier Guenaga & E, 2017. "Global site-specific N-glycosylation analysis of HIV envelope glycoprotein," Nature Communications, Nature, vol. 8(1), pages 1-13, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14954
    DOI: 10.1038/ncomms14954
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    Cited by:

    1. Wen-Han Yu & Peng Zhao & Monia Draghi & Claudia Arevalo & Christina B Karsten & Todd J Suscovich & Bronwyn Gunn & Hendrik Streeck & Abraham L Brass & Michael Tiemeyer & Michael Seaman & John R Mascola, 2018. "Exploiting glycan topography for computational design of Env glycoprotein antigenicity," PLOS Computational Biology, Public Library of Science, vol. 14(4), pages 1-28, April.

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