Imperial College London
Alternate

ProfessorRobinShattock

Faculty of Medicine, Department of Infectious Disease

Chair in Mucosal Infection and Immunity
 
 
 
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Contact

 

+44 (0)20 7594 5206r.shattock

 
 
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Location

 

453Wright Fleming WingSt Mary's Campus

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Summary

 

Publications

Citation

BibTex format

@article{Sliepen:2019:10.1038/s41467-019-10262-5,
author = {Sliepen, K and Han, BW and Bontjer, I and Mooij, P and Garces, F and Behrens, A-J and Rantalainen, K and Kumar, S and Sarkar, A and Brouwer, PJM and Hua, Y and Tolazzi, M and Schermer, E and Torres, JL and Ozorowski, G and van, der Woude P and de, la Pena AT and van, Breemen MJ and Camacho-Sanchez, JM and Burger, JA and Medina-Ramirez, M and Gonzalez, N and Alcami, J and LaBranche, C and Scarlatti, G and van, Gils MJ and Crispin, M and Montefiori, DC and Ward, AB and Koopman, G and Moore, JP and Shattock, RJ and Bogers, WM and Wilson, IA and Sanders, RW},
doi = {10.1038/s41467-019-10262-5},
journal = {Nature Communications},
title = {Structure and immunogenicity of a stabilized HIV-1 envelope trimer based on a group-M consensus sequence},
url = {http://dx.doi.org/10.1038/s41467-019-10262-5},
volume = {10},
year = {2019}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Stabilized HIV-1 envelope glycoproteins (Env) that resemble the native Env are utilized in vaccination strategies aimed at inducing broadly neutralizing antibodies (bNAbs). To limit the exposure of rare isolate-specific antigenic residues/determinants we generated a SOSIP trimer based on a consensus sequence of all HIV-1 group M isolates (ConM). The ConM trimer displays the epitopes of most known bNAbs and several germline bNAb precursors. The crystal structure of the ConM trimer at 3.9 Å resolution resembles that of the native Env trimer and its antigenic surface displays few rare residues. The ConM trimer elicits strong NAb responses against the autologous virus in rabbits and macaques that are significantly enhanced when it is presented on ferritin nanoparticles. The dominant NAb specificity is directed against an epitope at or close to the trimer apex. Immunogens based on consensus sequences might have utility in engineering vaccines against HIV-1 and other viruses.
AU  - Sliepen,K
AU  - Han,BW
AU  - Bontjer,I
AU  - Mooij,P
AU  - Garces,F
AU  - Behrens,A-J
AU  - Rantalainen,K
AU  - Kumar,S
AU  - Sarkar,A
AU  - Brouwer,PJM
AU  - Hua,Y
AU  - Tolazzi,M
AU  - Schermer,E
AU  - Torres,JL
AU  - Ozorowski,G
AU  - van,der Woude P
AU  - de,la Pena AT
AU  - van,Breemen MJ
AU  - Camacho-Sanchez,JM
AU  - Burger,JA
AU  - Medina-Ramirez,M
AU  - Gonzalez,N
AU  - Alcami,J
AU  - LaBranche,C
AU  - Scarlatti,G
AU  - van,Gils MJ
AU  - Crispin,M
AU  - Montefiori,DC
AU  - Ward,AB
AU  - Koopman,G
AU  - Moore,JP
AU  - Shattock,RJ
AU  - Bogers,WM
AU  - Wilson,IA
AU  - Sanders,RW
DO  - 10.1038/s41467-019-10262-5
PY  - 2019///
SN  - 2041-1723
TI  - Structure and immunogenicity of a stabilized HIV-1 envelope trimer based on a group-M consensus sequence
T2  - Nature Communications
UR  - http://dx.doi.org/10.1038/s41467-019-10262-5
UR  - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000469320500002&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR  - https://www.nature.com/articles/s41467-019-10262-5
UR  - http://hdl.handle.net/10044/1/71979
VL  - 10
ER  -
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