Native conformation and canonical disulfide bond formation are interlinked properties of HIV-1 Env glycoproteins Academic Article uri icon

Overview

MeSH Major

  • Disulfides
  • HIV-1
  • env Gene Products, Human Immunodeficiency Virus

abstract

  • It is widely thought that a successful HIV-1 vaccine will include a recombinant form of the Env protein, a trimer located on the virion surface. To increase yield and simplify purification, Env proteins are often made in truncated, soluble forms. A consequence, however, can be the loss of the native conformation concomitant with the virion-associated trimer. Moreover, some soluble recombinant Env proteins contain aberrant disulfide bonds that are not expected to be present in the native trimer. To assess whether these observations are linked, to determine the extent of disulfide bond scrambling, and to understand why scrambling occurs, we determined the disulfide bond profiles of two soluble Env proteins with different designs that are being assessed as vaccine candidates. We found that uncleaved gp140 forms heterogeneous mixtures in which aberrant disulfide bonds abound. In contrast, BG505 SOSIP.664 trimers are more homogeneous, native-like entities that contain predominantly the native disulfide bond profile.

publication date

  • January 2016

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed Central ID

  • PMC4810632

Digital Object Identifier (DOI)

  • 10.1128/JVI.01953-15

PubMed ID

  • 26719247

Additional Document Info

start page

  • 2884

end page

  • 94

volume

  • 90

number

  • 6