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Recombinant protein subunit vaccine synthesis in microbes: a role for yeast?

Identifieur interne : 000913 ( Istex/Corpus ); précédent : 000912; suivant : 000914

Recombinant protein subunit vaccine synthesis in microbes: a role for yeast?

Auteurs : Roslyn M. Bill

Source :

RBID : ISTEX:F6E11952D083724F50B9D5C02407D6ED37EEEB39

Abstract

Objectives: Recombinant protein subunit vaccines are formulated using protein antigens that have been synthesized in heterologous host cells. Several host cells are available for this purpose, ranging from Escherichia coli to mammalian cell lines. This article highlights the benefits of using yeast as the recombinant host. Key findings: The yeast species, Saccharomyces cerevisiae and Pichia pastoris, have been used to optimize the functional yields of potential antigens for the development of subunit vaccines against a wide range of diseases caused by bacteria and viruses. Saccharomyces cerevisiae has also been used in the manufacture of 11 approved vaccines against hepatitis B virus and one against human papillomavirus; in both cases, the recombinant protein forms highly immunogenic virus‐like particles. Summary: Advances in our understanding of how a yeast cell responds to the metabolic load of producing recombinant proteins will allow us to identify host strains that have improved yield properties and enable the synthesis of more challenging antigens that cannot be produced in other systems. Yeasts therefore have the potential to become important host organisms for the production of recombinant antigens that can be used in the manufacture of subunit vaccines or in new vaccine development.

Url:
DOI: 10.1111/jphp.12353

Links to Exploration step

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<title type="shortAuthors">Roslyn
<fc>M</fc>
.
<fc>B</fc>
ill</title>
<title type="main">Recombinant protein subunit vaccine synthesis in microbes: a role for yeast?</title>
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<familyName>Bill</familyName>
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<orgDiv>School of Life and Health Sciences</orgDiv>
<orgName>Aston University</orgName>
<address>
<city>Birmingham</city>
<country>UK</country>
</address>
</affiliation>
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<keyword xml:id="jphp12353-kwd-0001">
<fc>
<i>P</i>
</fc>
<i>ichia pastoris</i>
</keyword>
<keyword xml:id="jphp12353-kwd-0002">recombinant antigen</keyword>
<keyword xml:id="jphp12353-kwd-0003">
<fc>
<i>S</i>
</fc>
<i>accharomyces cerevisiae</i>
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<keyword xml:id="jphp12353-kwd-0004">yeast</keyword>
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<abstract type="main">
<title type="main">Abstract</title>
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<title type="main">Objectives</title>
<p>Recombinant protein subunit vaccines are formulated using protein antigens that have been synthesized in heterologous host cells. Several host cells are available for this purpose, ranging from
<fc>
<i>E</i>
</fc>
<i>scherichia coli</i>
to mammalian cell lines. This article highlights the benefits of using yeast as the recombinant host.</p>
</section>
<section xml:id="jphp12353-sec-1002">
<title type="main">Key findings</title>
<p>The yeast species,
<fc>
<i>S</i>
</fc>
<i>accharomyces cerevisiae</i>
and
<fc>
<i>P</i>
</fc>
<i>ichia pastoris</i>
, have been used to optimize the functional yields of potential antigens for the development of subunit vaccines against a wide range of diseases caused by bacteria and viruses.
<fc>
<i>S</i>
</fc>
<i>accharomyces cerevisiae</i>
has also been used in the manufacture of 11 approved vaccines against hepatitis
<fc>B</fc>
virus and one against human papillomavirus; in both cases, the recombinant protein forms highly immunogenic virus‐like particles.</p>
</section>
<section xml:id="jphp12353-sec-1003">
<title type="main">Summary</title>
<p>Advances in our understanding of how a yeast cell responds to the metabolic load of producing recombinant proteins will allow us to identify host strains that have improved yield properties and enable the synthesis of more challenging antigens that cannot be produced in other systems. Yeasts therefore have the potential to become important host organisms for the production of recombinant antigens that can be used in the manufacture of subunit vaccines or in new vaccine development.</p>
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<title>Recombinant protein subunit vaccine synthesis in microbes: a role for yeast?</title>
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<title>Recombinant protein subunit vaccines</title>
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<title>Recombinant protein subunit vaccine synthesis in microbes: a role for yeast?</title>
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<name type="personal">
<namePart type="given">Roslyn M.</namePart>
<namePart type="family">Bill</namePart>
<affiliation>School of Life and Health Sciences, Aston University, Birmingham, UK</affiliation>
<affiliation>Roslyn M. Bill, School of Life and Health Sciences, Aston University, Aston Triangle, B4 7ET Birmingham, UK.E‐mail:</affiliation>
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<abstract>Objectives: Recombinant protein subunit vaccines are formulated using protein antigens that have been synthesized in heterologous host cells. Several host cells are available for this purpose, ranging from Escherichia coli to mammalian cell lines. This article highlights the benefits of using yeast as the recombinant host. Key findings: The yeast species, Saccharomyces cerevisiae and Pichia pastoris, have been used to optimize the functional yields of potential antigens for the development of subunit vaccines against a wide range of diseases caused by bacteria and viruses. Saccharomyces cerevisiae has also been used in the manufacture of 11 approved vaccines against hepatitis B virus and one against human papillomavirus; in both cases, the recombinant protein forms highly immunogenic virus‐like particles. Summary: Advances in our understanding of how a yeast cell responds to the metabolic load of producing recombinant proteins will allow us to identify host strains that have improved yield properties and enable the synthesis of more challenging antigens that cannot be produced in other systems. Yeasts therefore have the potential to become important host organisms for the production of recombinant antigens that can be used in the manufacture of subunit vaccines or in new vaccine development.</abstract>
<subject>
<genre>keywords</genre>
<topic>Pichia pastoris</topic>
<topic>recombinant antigen</topic>
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<identifier type="DOI">10.1111/(ISSN)2042-7158</identifier>
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