Imperial College London
Alternate

Emeritus Professor Howard R. Morris FRS

Faculty of Natural Sciences, Department of Life Sciences

Senior Research Investigator
 
 
 
//

Contact

 

+44 (0)20 7594 5221h.morris

 
 
//

Assistant

 

Miss Cathy Thomas +44 (0)20 7594 5220

 
//

Location

 

103Sir Ernst Chain BuildingSouth Kensington Campus

//

Summary

 

Publications

Citation

BibTex format

@article{Stansell:2015:10.1371/journal.pone.0124784,
author = {Stansell, A},
doi = {10.1371/journal.pone.0124784},
journal = {PLOS ONE},
pages = {1--15},
title = {Gp120 on HIV-1 Virions Lacks O-Linked Carbohydrate},
url = {http://dx.doi.org/10.1371/journal.pone.0124784},
volume = {10},
year = {2015}
}
Download

RIS format (EndNote, RefMan)

TY  - JOUR
AB  - As HIV-1-encoded envelope protein traverses the secretory pathway, it may be modified with N- and O-linked carbohydrate. When the gp120s of HIV-1 NL4-3, HIV-1 YU2, HIV-1 Bal, HIV-1 JRFL, and HIV-1 JRCSF were expressed as secreted proteins, the threonine at consensus position 499 was found to be O-glycosylated. For SIVmac239, the corresponding threonine was also glycosylated when gp120 was recombinantly expressed. Similarly-positioned, highly-conserved threonines in the influenza A virus H1N1 HA1 and H5N1 HA1 envelope proteins were also found to carry O-glycans when expressed as secreted proteins. In all cases, the threonines were modified predominantly with disialylated core 1 glycans, together with related core 1 and core 2 structures. Secreted HIV-1 gp140 was modified to a lesser extent with mainly monosialylated core 1 O-glycans, suggesting that the ectodomain of the gp41 transmembrane component may limit the accessibility of Thr499 to glycosyltransferases. In striking contrast to these findings, gp120 on purified virions of HIV-1 Bal and SIV CP-MAC lacked any detectable O-glycosylation of the C-terminal threonine. Our results indicate the absence of O-linked carbohydrates on Thr499 as it exists on the surface of virions and suggest caution in the interpretation of analyses of post-translational modifications that utilize recombinant forms of envelope protein.
AU  - Stansell,A
DO  - 10.1371/journal.pone.0124784
EP  - 15
PY  - 2015///
SP  - 1
TI  - Gp120 on HIV-1 Virions Lacks O-Linked Carbohydrate
T2  - PLOS ONE
UR  - http://dx.doi.org/10.1371/journal.pone.0124784
UR  - https://doi.org/10.1371/journal.pone.0124784
UR  - http://hdl.handle.net/10044/1/41142
VL  - 10
ER  -
Download