Rxivist logo

The HIV-1 envelope glycoprotein (Env) trimer is decorated with N-linked glycans, which are attached to asparagine residues in the amino acid sequon NxT/S by oligosaccharyltransferases (OST). Artificial glycan holes exist when a PNGS is under-occupied on recombinant Env-based vaccines, but not on their viral counterpart. Native-like SOSIP trimers, including clinical candidates, have these artificial holes in the glycan shield that induce strain-specific neutralizing antibodies (NAbs) or non-NAbs. To increase PNGS occupancy, eliminate artificial glycan holes, and mimic the glycosylation of native BG505 Env, we replaced all 12 NxS sequons on the BG505 SOSIP trimer with NxT, thereby increasing the affinity of the sequons for OST. All PNGS, except N133 and N160, were nearly fully occupied on the modified trimer. Occupancy of the N133 site could be increased by changing N133 to NxS, while occupancy of the N160 site could be restored by reverting the nearby N156 sequon to NxS. Hence, OST affinity can influence glycan occupancy when two PNGS are in close proximity. Increasing glycan occupancy should reduce off-target immune responses to artificial glycan holes on vaccine antigens. ### Competing Interest Statement R. W. S. and J. P. M. are listed on patents concerning stabilized Env trimers.

Download data

  • Downloaded 169 times
  • Download rankings, all-time:
    • Site-wide: 97,449 out of 118,977
    • In biochemistry: 2,885 out of 3,595
  • Year to date:
    • Site-wide: 51,971 out of 118,977
  • Since beginning of last month:
    • Site-wide: 42,957 out of 118,977

Altmetric data


Downloads over time

Distribution of downloads per paper, site-wide


PanLingua

Sign up for the Rxivist weekly newsletter! (Click here for more details.)


News