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Discovery of a tyrosine-rich sporocyst wall protein in Eimeria tenella

Identifieur interne : 003216 ( Ncbi/Checkpoint ); précédent : 003215; suivant : 003217

Discovery of a tyrosine-rich sporocyst wall protein in Eimeria tenella

Auteurs : Robert A. Walker [Suisse] ; Alisson Niepceron [France] ; Chandra Ramakrishnan [Suisse] ; Laura Sedano [France] ; Adrian B. Hehl [Suisse] ; Fabien Brossier [France] ; Nicholas C. Smith

Source :

RBID : PMC:4776368

Descripteurs français

English descriptors

Abstract

Background

Eimeria is an important genus of apicomplexan parasites. A defining feature of these parasites is the oocyst, which is transmitted into the environment via the faeces of definitive hosts. The oocyst wall contains cross-linked, tyrosine-rich proteins and protects eight infectious sporozoites, housed in pairs within a second walled structure, the sporocyst. The biochemical basis for sporocyst wall formation is not known.

Findings

Here, we report the discovery of a novel tyrosine-rich protein, EtSWP1, in Eimeria tenella. Like the tyrosine-rich proteins of the oocyst wall, EtSWP1 is an intrinsically disordered protein with the tyrosine residues concentrated in a specific region of the protein, located immediately following the region of intrinsic disorder. We engineered E. tenella to express mCherry-tagged EtSWP1 and showed that the tagged protein localises specifically to sporocyst walls, indicating that the biochemistry of sporocyst wall assembly is analagous to that of oocyst walls.

Conclusions

Tyrosine-rich proteins are known to be key components of the oocyst wall and we now demonstrate, using gene and protein analyses combined with genetic manipulation, that a novel tyrosine-rich protein is specific for the sporocyst wall. This finding is important because it shows that the biochemistry of these two distinct walls is similar and, hence, brings targeted disruption of sporulation and, therefore, potential neutralisation of oocysts in the environment, a step closer.

Electronic supplementary material

The online version of this article (doi:10.1186/s13071-016-1410-z) contains supplementary material, which is available to authorized users.


Url:
DOI: 10.1186/s13071-016-1410-z
PubMed: 26935317
PubMed Central: 4776368


Affiliations:


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PMC:4776368

Le document en format XML

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<term>Cell Wall (chemistry)</term>
<term>Cell Wall (genetics)</term>
<term>Eimeria tenella (chemistry)</term>
<term>Eimeria tenella (genetics)</term>
<term>Oocysts (chemistry)</term>
<term>Protozoan Proteins (genetics)</term>
<term>Protozoan Proteins (isolation & purification)</term>
<term>Tyrosine (analysis)</term>
<term>Tyrosine (genetics)</term>
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<term>Eimeria tenella ()</term>
<term>Eimeria tenella (génétique)</term>
<term>Oocystes ()</term>
<term>Paroi cellulaire ()</term>
<term>Paroi cellulaire (génétique)</term>
<term>Protéines de protozoaire (génétique)</term>
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<term>Tyrosine (génétique)</term>
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<term>Tyrosine</term>
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<term>Tyrosine</term>
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<term>Cell Wall</term>
<term>Eimeria tenella</term>
<term>Oocysts</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en">
<term>Cell Wall</term>
<term>Eimeria tenella</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr">
<term>Eimeria tenella</term>
<term>Paroi cellulaire</term>
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<term>Protéines de protozoaire</term>
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<term>Eimeria tenella</term>
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<sec>
<title>Background</title>
<p>
<italic>Eimeria </italic>
is an important genus of apicomplexan parasites. A defining feature of these parasites is the oocyst, which is transmitted into the environment
<italic>via</italic>
the faeces of definitive hosts. The oocyst wall contains cross-linked, tyrosine-rich proteins and protects eight infectious sporozoites, housed in pairs within a second walled structure, the sporocyst. The biochemical basis for sporocyst wall formation is not known.</p>
</sec>
<sec>
<title>Findings</title>
<p>Here, we report the discovery of a novel tyrosine-rich protein,
<italic>Et</italic>
SWP1, in
<italic>Eimeria tenella</italic>
. Like the tyrosine-rich proteins of the oocyst wall,
<italic>Et</italic>
SWP1 is an intrinsically disordered protein with the tyrosine residues concentrated in a specific region of the protein, located immediately following the region of intrinsic disorder. We engineered
<italic>E. tenella</italic>
to express mCherry-tagged
<italic>Et</italic>
SWP1 and showed that the tagged protein localises specifically to sporocyst walls
<italic>,</italic>
indicating that the biochemistry of sporocyst wall assembly is analagous to that of oocyst walls.</p>
</sec>
<sec>
<title>Conclusions</title>
<p>Tyrosine-rich proteins are known to be key components of the oocyst wall and we now demonstrate, using gene and protein analyses combined with genetic manipulation, that a novel tyrosine-rich protein is specific for the sporocyst wall. This finding is important because it shows that the biochemistry of these two distinct walls is similar and, hence, brings targeted disruption of sporulation and, therefore, potential neutralisation of oocysts in the environment, a step closer.</p>
</sec>
<sec>
<title>Electronic supplementary material</title>
<p>The online version of this article (doi:10.1186/s13071-016-1410-z) contains supplementary material, which is available to authorized users.</p>
</sec>
</div>
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<author>
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<name sortKey="Zhang, Y" uniqKey="Zhang Y">Y Zhang</name>
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</author>
<author>
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</analytic>
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<name sortKey="Yang, J" uniqKey="Yang J">J Yang</name>
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<li>France</li>
<li>Suisse</li>
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<li>Canton de Zurich</li>
<li>Centre-Val de Loire</li>
<li>Région Centre</li>
</region>
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<li>Tours</li>
<li>Zurich</li>
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<name sortKey="Ramakrishnan, Chandra" sort="Ramakrishnan, Chandra" uniqKey="Ramakrishnan C" first="Chandra" last="Ramakrishnan">Chandra Ramakrishnan</name>
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<name sortKey="Sedano, Laura" sort="Sedano, Laura" uniqKey="Sedano L" first="Laura" last="Sedano">Laura Sedano</name>
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