Imperial College London
Alternate

ProfessorJillGilmour

Faculty of Medicine, Department of Infectious Disease

Honorary Principal Research Fellow 
 
 
 
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Contact

 

+44 (0)20 3315 5098j.gilmour

 
 
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Location

 

J.2.3 Immunology DepartmentChelsea and Westminster HospitalChelsea and Westminster Campus

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Summary

 

Publications

Citation

BibTex format

@article{Huettner:2022:10.1016/j.celrep.2022.110611,
author = {Huettner, I and Krumm, SA and Serna, S and Brzezicka, K and Monaco, S and Walpole, S and van, Diepen A and Allan, F and Hicks, T and Kimuda, S and Emery, AM and IAVI, Protocol C Investigators & The IAVI African HIV Research Network and Landais, E and Hokke, CH and Angulo, J and Reichardt, N and Doores, KJ},
doi = {10.1016/j.celrep.2022.110611},
journal = {Cell Rep},
title = {Cross-reactivity of glycan-reactive HIV-1 broadly neutralizing antibodies with parasite glycans.},
url = {http://dx.doi.org/10.1016/j.celrep.2022.110611},
volume = {38},
year = {2022}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - The HIV-1 Envelope glycoprotein (Env) is the sole target for broadly neutralizing antibodies (bnAbs). Env is heavily glycosylated with host-derived N-glycans, and many bnAbs bind to, or are dependent upon, Env glycans for neutralization. Although glycan-binding bnAbs are frequently detected in HIV-infected individuals, attempts to elicit them have been unsuccessful because of the poor immunogenicity of Env N-glycans. Here, we report cross-reactivity of glycan-binding bnAbs with self- and non-self N-glycans and glycoprotein antigens from different life-stages of Schistosoma mansoni. Using the IAVI Protocol C HIV infection cohort, we examine the relationship between S. mansoni seropositivity and development of bnAbs targeting glycan-dependent epitopes. We show that the unmutated common ancestor of the N332/V3-specific bnAb lineage PCDN76, isolated from an HIV-infected donor with S. mansoni seropositivity, binds to S. mansoni cercariae while lacking reactivity to gp120. Overall, these results present a strategy for elicitation of glycan-reactive bnAbs which could be exploited in HIV-1 vaccine development.
AU  - Huettner,I
AU  - Krumm,SA
AU  - Serna,S
AU  - Brzezicka,K
AU  - Monaco,S
AU  - Walpole,S
AU  - van,Diepen A
AU  - Allan,F
AU  - Hicks,T
AU  - Kimuda,S
AU  - Emery,AM
AU  - IAVI,Protocol C Investigators & The IAVI African HIV Research Network
AU  - Landais,E
AU  - Hokke,CH
AU  - Angulo,J
AU  - Reichardt,N
AU  - Doores,KJ
DO  - 10.1016/j.celrep.2022.110611
PY  - 2022///
TI  - Cross-reactivity of glycan-reactive HIV-1 broadly neutralizing antibodies with parasite glycans.
T2  - Cell Rep
UR  - http://dx.doi.org/10.1016/j.celrep.2022.110611
UR  - https://www.ncbi.nlm.nih.gov/pubmed/35354052
VL  - 38
ER  -
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