Imperial College London
Alternate

Emeritus Professor Howard R. Morris FRS

Faculty of Natural Sciences, Department of Life Sciences

Senior Research Investigator
 
 
 
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Contact

 

+44 (0)20 7594 5221h.morris

 
 
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Assistant

 

Miss Cathy Thomas +44 (0)20 7594 5220

 
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Location

 

103Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Panico:2016:10.1038/srep32956,
author = {Panico, M and Bouché, L and Binet, D and O'Connor, MJ and Rahman, D and Pang, PC and Canis, K and North, SJ and Desrosiers, RC and Chertova, E and Keele, BF and Bess, JW and Lifson, JD and Haslam, SM and Dell, A and Morris, HR},
doi = {10.1038/srep32956},
journal = {Scientific Reports},
pages = {1--17},
title = {Mapping the complete glycoproteome of virion-derived HIV-1 gp120 provides insights into broadly neutralizing antibody binding},
url = {http://dx.doi.org/10.1038/srep32956},
volume = {6},
year = {2016}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - The surface envelope glycoprotein (SU) of Human immunodeficiency virus type 1 (HIV-1), gp120SU plays an essential role in virus binding to target CD4+ T-cells and is a major vaccine target. Gp120 has remarkably high levels of N-linked glycosylation and there is considerable evidence that this “glycan shield” can help protect the virus from antibody-mediated neutralization. In recent years, however, it has become clear that gp120 glycosylation can also be included in the targets of recognition by some of the most potent broadly neutralizing antibodies. Knowing the site-specific glycosylation of gp120 can facilitate the rational design of glycopeptide antigens for HIV vaccine development. While most prior studies have focused on glycan analysis of recombinant forms of gp120, here we report the first systematic glycosylation site analysis of gp120 derived from virions produced by infected T lymphoid cells and show that a single site is exclusively substituted with complex glycans. These results should help guide the design of vaccine immunogens.
AU  - Panico,M
AU  - Bouché,L
AU  - Binet,D
AU  - O'Connor,MJ
AU  - Rahman,D
AU  - Pang,PC
AU  - Canis,K
AU  - North,SJ
AU  - Desrosiers,RC
AU  - Chertova,E
AU  - Keele,BF
AU  - Bess,JW
AU  - Lifson,JD
AU  - Haslam,SM
AU  - Dell,A
AU  - Morris,HR
DO  - 10.1038/srep32956
EP  - 17
PY  - 2016///
SN  - 2045-2322
SP  - 1
TI  - Mapping the complete glycoproteome of virion-derived HIV-1 gp120 provides insights into broadly neutralizing antibody binding
T2  - Scientific Reports
UR  - http://dx.doi.org/10.1038/srep32956
UR  - https://www.nature.com/articles/srep32956
UR  - http://hdl.handle.net/10044/1/40033
VL  - 6
ER  -
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