Glycosylation profiling to evaluate glycoprotein immunogens against HIV-1.

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

SUBMITTER: Behrens AJ 

PROVIDER: S-EPMC5846109 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature