Skip to main content
Advertisement

< Back to Article

Effect of Glycosylation on an Immunodominant Region in the V1V2 Variable Domain of the HIV-1 Envelope gp120 Protein

Fig 14

Effects of glycosylation on V1V2 peptide region in the context of the BG505 Env trimeric spike.

(A) Root mean square fluctuation of the backbone atoms corresponding to residues 129–134 and 152–184 (HBX2 numbering) and computed for either the glycosylated (black line) and non-glycosylated (red line) protein. Error bars were estimated from calculation in each of the independent protomers. (B) Cumulative configurational entropy for the backbone atoms corresponding to the same residues as in panel A. Values were estimated by considering the total entropy from the three promoters. (C) Total interaction energy from the representative sequence as in B. The energy corresponds to the total value calculated among the three protomers and during 1us trajectory simulation. (D) Secondary structural percentage as computed from 1us MD simulations of the full Env spike. Four stretches were considered for the analysis, each featuring disulfide bonds and glycosylation sites. Computed secondary structure percentage for amino acid stretches that contain glycans adjacent to Cysteins (HXB2 numbering): 131–157 (analogous to the V1V2 peptide), 385–418 and 296–331. It further demonstrates, in the context of Env trimer, that glycosylation decreases the amount of alpha-helix, beta strands, bridge and turns in these regions.

Fig 14

doi: https://doi.org/10.1371/journal.pcbi.1005094.g014