The extensive post-translational modifications of the envelope spikes of the human immunodeficiency virus (HIV) present considerable challenges and opportunities for HIV vaccine design. These oligomeric glycoproteins typically have over 30 disulfide bonds and around a 100 N-linked glycosylation sites, and are functionally dependent on protease cleavage within the secretory system. The resulting mature structure adopts a compact fold with the vast majority of its surface obscured by a protective shield of glycans which can be targeted by broadly neutralizing antibodies (bnAbs). Despite the notorious heterogeneity of glycosylation, rare B-cell lineages can evolve to utilize and cope with viral glycan diversity, and these structures therefore present promising targets for vaccine design. The latest generation of recombinant envelope spike mimetics contains re-engineered post-translational modifications to present stable antigens to guide the development of bnAbs by vaccination.
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June 2018
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The structure of a Nucleosome, in which DNA is wrapped around a histone core. In this issue of Biochemical Society Transactions, Taniguchi et al. review recent advances in exploring Nucleosome-level 3D organization of the genome; for details see pages 491–501.
Review Article|
May 21 2018
Harnessing post-translational modifications for next-generation HIV immunogens
Joel D. Allen;
Joel D. Allen
1Centre for Biological Sciences and Institute for Life Sciences, University of Southampton, Southampton SO17 1BJ, U.K.
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Rogier W. Sanders;
Rogier W. Sanders
2Amsterdam Infection and Immunity Institute (AI&II), Laboratory of Experimental Virology, Department of Medical Microbiology, Academic Medical Center of the University of Amsterdam, 1105 AZ Amsterdam, The Netherlands
3Department of Microbiology and Immunology, Weill Cornell Medical College, New York, NY 10021, U.S.A.
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Katie J. Doores;
Katie J. Doores
4Department of Infectious Diseases, King's College London, Guy's Hospital, London SE1 9RT, U.K.
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Max Crispin
1Centre for Biological Sciences and Institute for Life Sciences, University of Southampton, Southampton SO17 1BJ, U.K.
Correspondence: Max Crispin (max.crispin@soton.ac.uk)
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Publisher: Portland Press Ltd
Received:
February 06 2018
Revision Received:
April 10 2018
Accepted:
April 17 2018
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2018 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society
2018
Biochem Soc Trans (2018) 46 (3): 691–698.
Article history
Received:
February 06 2018
Revision Received:
April 10 2018
Accepted:
April 17 2018
Citation
Joel D. Allen, Rogier W. Sanders, Katie J. Doores, Max Crispin; Harnessing post-translational modifications for next-generation HIV immunogens. Biochem Soc Trans 19 June 2018; 46 (3): 691–698. doi: https://doi.org/10.1042/BST20170394
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