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

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, Erik Georgeson, Michael Kubitz, Yumiko Adachi, Dennis R. Burton, William R. Schief, John R. Yates and James C. Paulson ()
Additional contact information
Liwei Cao: The Scripps Research Institute
Jolene K. Diedrich: The Scripps Research Institute
Daniel W. Kulp: The Scripps Research Institute
Matthias Pauthner: The Scripps Research Institute
Lin He: The Scripps Research Institute
Sung-Kyu Robin Park: The Scripps Research Institute
Devin Sok: 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
William R. Schief: The Scripps Research Institute
John R. Yates: The Scripps Research Institute
James C. Paulson: The Scripps Research Institute

Nature Communications, 2017, vol. 8, issue 1, 1-13

Abstract: 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.

Date: 2017
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DOI: 10.1038/ncomms14954

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