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Glycosylation profiling to evaluate glycoprotein immunogens against HIV-1.

Glycosylation profiling to evaluate glycoprotein immunogens against HIV-1.
Author Information (click to view)

Behrens AJ, Struwe WB, Crispin M,


Behrens AJ, Struwe WB, Crispin M, (click to view)

Behrens AJ, Struwe WB, Crispin M,

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Expert review of proteomics 2017 09 05() doi 10.1080/14789450.2017.1376658

Abstract

Introduction Much of the efforts to develop a vaccine against the human immunodeficiency virus (HIV) have focused on the design of recombinant mimics of the viral attachment glycoprotein (Env). The leading immunogens exhibit native-like antigenic properties and are being investigated for their ability to induce broadly neutralizing antibodies (bNAbs). Understanding the relative abundance of glycans at particular glycosylation sites on these immunogens is important as most bNAbs have evolved to recognize or evade the dense coat of glycans that masks much of the protein surface. Understanding the glycan structures on candidate immunogens enables triaging between native-like conformations and immunogens lacking key structural features as steric constraints limit glycan processing. The sensitivity of the processing state of a particular glycan to its structural environment has led to the need for quantitative glycan profiling and site-specific analysis to probe the structural integrity of immunogens. Areas covered We review analytical methodologies for HIV immunogen evaluation and discuss how these studies have led to a greater understanding of the structural constraints that control the glycosylation state of the HIV attachment and fusion spike. Expert commentary Total composition and site-specific glycosylation profiling are emerging as standard methods in the evaluation of Env-based immunogen candidates.

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