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Harnessing post-translational modifications for next-generation HIV immunogens

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Harnessing post-translational modifications for next-generation HIV immunogens. / Allen, Joel D; Sanders, Rogier W; Doores, Katie J; Crispin, Max.

In: Biochemical Society Transactions, Vol. 46, No. 3, 06.2018, p. 691-698.

Research output: Contribution to journalReview article

Harvard

Allen, JD, Sanders, RW, Doores, KJ & Crispin, M 2018, 'Harnessing post-translational modifications for next-generation HIV immunogens', Biochemical Society Transactions, vol. 46, no. 3, pp. 691-698. https://doi.org/10.1042/BST20170394

APA

Allen, J. D., Sanders, R. W., Doores, K. J., & Crispin, M. (2018). Harnessing post-translational modifications for next-generation HIV immunogens. Biochemical Society Transactions, 46(3), 691-698. https://doi.org/10.1042/BST20170394

Vancouver

Allen JD, Sanders RW, Doores KJ, Crispin M. Harnessing post-translational modifications for next-generation HIV immunogens. Biochemical Society Transactions. 2018 Jun;46(3):691-698. https://doi.org/10.1042/BST20170394

Author

Allen, Joel D ; Sanders, Rogier W ; Doores, Katie J ; Crispin, Max. / Harnessing post-translational modifications for next-generation HIV immunogens. In: Biochemical Society Transactions. 2018 ; Vol. 46, No. 3. pp. 691-698.

Bibtex Download

@article{08c56d4e9be740f9ad76409108ccac24,
title = "Harnessing post-translational modifications for next-generation HIV immunogens",
abstract = "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.",
author = "Allen, {Joel D} and Sanders, {Rogier W} and Doores, {Katie J} and Max Crispin",
note = "{\circledC} 2018 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.",
year = "2018",
month = "6",
doi = "10.1042/BST20170394",
language = "English",
volume = "46",
pages = "691--698",
journal = "Biochemical Society Transactions",
issn = "0300-5127",
publisher = "Portland Press Ltd.",
number = "3",

}

RIS (suitable for import to EndNote) Download

TY - JOUR

T1 - Harnessing post-translational modifications for next-generation HIV immunogens

AU - Allen, Joel D

AU - Sanders, Rogier W

AU - Doores, Katie J

AU - Crispin, Max

N1 - © 2018 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.

PY - 2018/6

Y1 - 2018/6

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85048949035&partnerID=8YFLogxK

U2 - 10.1042/BST20170394

DO - 10.1042/BST20170394

M3 - Review article

C2 - 29784645

VL - 46

SP - 691

EP - 698

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

SN - 0300-5127

IS - 3

ER -

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