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cGMP production and analysis of BG505 SOSIP.664, an extensively glycosylated, trimeric HIV-1 envelope glycoprotein vaccine candidate

cGMP production and analysis of BG505 SOSIP.664, an extensively glycosylated, trimeric HIV-1 envelope glycoprotein vaccine candidate
cGMP production and analysis of BG505 SOSIP.664, an extensively glycosylated, trimeric HIV-1 envelope glycoprotein vaccine candidate
We describe the properties of BG505 SOSIP.664 HIV-1 envelope glycoprotein trimers produced under current Good Manufacturing Practice (cGMP) conditions. These proteins are the first of a new generation of native-like trimers that are the basis for many structure-guided immunogen development programs aimed at devising how to induce broadly neutralizing antibodies (bNAbs) to HIV-1 by vaccination. The successful translation of this prototype demonstrates the feasibility of producing similar immunogens on an appropriate scale and of an acceptable quality for Phase I experimental medicine clinical trials. BG505 SOSIP.664 trimers are extensively glycosylated, contain numerous disulfide bonds and require proteolytic cleavage, all properties that pose a substantial challenge to cGMP production. Our strategy involved creating a stable CHO cell line that was adapted to serum-free culture conditions to produce envelope glycoproteins. The trimers were then purified by chromatographic methods using a 2G12 bNAb affinity column and size-exclusion chromatography. The chosen procedures allowed any adventitious viruses to be cleared from the final product to the required extent of >12 log10. The final cGMP production run yielded 3.52 g (peptidic mass) of fully purified trimers (Drug Substance) from a 200 L bioreactor, a notable yield for such a complex glycoprotein. The purified trimers were fully native-like as judged by negative-stain electron microscopy, and were stable over a multi-month period at room temperature or below and for at least 1 week at 50°C. Their antigenicity, disulfide bond patterns, and glycan composition were consistent with trimers produced on a research laboratory scale. The methods reported here should pave the way for the cGMP production of other native-like Env glycoprotein trimers of various designs and genotypes.
0006-3592
885–899
Dey, Antu K.
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Cupo, Albert
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Ozorowski, Gabriel
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Sharma, Vaneet K.
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Behrens, Anna-Janina
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Go, Eden P.
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Ketas, Thomas J.
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Yasmeen, Anila
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Klasse, Per J.
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Sayeed, Eddy
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Desaire, Heather
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Crispin, Max
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Wilson, Ian A.
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Sanders, Rogier W.
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Hassell, Thomas
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Ward, Andrew
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Moore, John P.
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Dey, Antu K.
3cfcd3d8-ef22-4bcb-bb73-b161d608f7ba
Cupo, Albert
aa9f476e-3296-4118-9231-0edc774b8335
Ozorowski, Gabriel
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Sharma, Vaneet K.
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Behrens, Anna-Janina
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Go, Eden P.
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Ketas, Thomas J.
be22ffd5-bef3-46c4-92fe-db4466a2a098
Yasmeen, Anila
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Klasse, Per J.
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Sayeed, Eddy
ffab4c39-c87b-4397-a492-a68a98ff5372
Desaire, Heather
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Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Wilson, Ian A.
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Sanders, Rogier W.
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Hassell, Thomas
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Ward, Andrew
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Moore, John P.
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Dey, Antu K., Cupo, Albert, Ozorowski, Gabriel, Sharma, Vaneet K., Behrens, Anna-Janina, Go, Eden P., Ketas, Thomas J., Yasmeen, Anila, Klasse, Per J., Sayeed, Eddy, Desaire, Heather, Crispin, Max, Wilson, Ian A., Sanders, Rogier W., Hassell, Thomas, Ward, Andrew and Moore, John P. (2018) cGMP production and analysis of BG505 SOSIP.664, an extensively glycosylated, trimeric HIV-1 envelope glycoprotein vaccine candidate. Biotechnology and Bioengineering, 115 (4), 885–899. (doi:10.1002/bit.26498).

Record type: Article

Abstract

We describe the properties of BG505 SOSIP.664 HIV-1 envelope glycoprotein trimers produced under current Good Manufacturing Practice (cGMP) conditions. These proteins are the first of a new generation of native-like trimers that are the basis for many structure-guided immunogen development programs aimed at devising how to induce broadly neutralizing antibodies (bNAbs) to HIV-1 by vaccination. The successful translation of this prototype demonstrates the feasibility of producing similar immunogens on an appropriate scale and of an acceptable quality for Phase I experimental medicine clinical trials. BG505 SOSIP.664 trimers are extensively glycosylated, contain numerous disulfide bonds and require proteolytic cleavage, all properties that pose a substantial challenge to cGMP production. Our strategy involved creating a stable CHO cell line that was adapted to serum-free culture conditions to produce envelope glycoproteins. The trimers were then purified by chromatographic methods using a 2G12 bNAb affinity column and size-exclusion chromatography. The chosen procedures allowed any adventitious viruses to be cleared from the final product to the required extent of >12 log10. The final cGMP production run yielded 3.52 g (peptidic mass) of fully purified trimers (Drug Substance) from a 200 L bioreactor, a notable yield for such a complex glycoprotein. The purified trimers were fully native-like as judged by negative-stain electron microscopy, and were stable over a multi-month period at room temperature or below and for at least 1 week at 50°C. Their antigenicity, disulfide bond patterns, and glycan composition were consistent with trimers produced on a research laboratory scale. The methods reported here should pave the way for the cGMP production of other native-like Env glycoprotein trimers of various designs and genotypes.

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Accepted/In Press date: 14 November 2017
e-pub ahead of print date: 11 December 2017
Published date: April 2018

Identifiers

Local EPrints ID: 416347
URI: http://eprints.soton.ac.uk/id/eprint/416347
ISSN: 0006-3592
PURE UUID: fd1adaaa-a41b-4ba9-9e83-f79378c41e32
ORCID for Max Crispin: ORCID iD orcid.org/0000-0002-1072-2694

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Date deposited: 13 Dec 2017 17:30
Last modified: 16 Mar 2024 05:57

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Contributors

Author: Antu K. Dey
Author: Albert Cupo
Author: Gabriel Ozorowski
Author: Vaneet K. Sharma
Author: Anna-Janina Behrens
Author: Eden P. Go
Author: Thomas J. Ketas
Author: Anila Yasmeen
Author: Per J. Klasse
Author: Eddy Sayeed
Author: Heather Desaire
Author: Max Crispin ORCID iD
Author: Ian A. Wilson
Author: Rogier W. Sanders
Author: Thomas Hassell
Author: Andrew Ward
Author: John P. Moore

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