The C-terminal domain of the MERS coronavirus M protein contains a trans-Golgi network localization signal
Identifieur interne : 000353 ( Main/Exploration ); précédent : 000352; suivant : 000354The C-terminal domain of the MERS coronavirus M protein contains a trans-Golgi network localization signal
Auteurs : Anabelle Perrier [France] ; Ariane Bonnin [France] ; Lowiese Desmarets [France] ; Adeline Danneels [France] ; Anne Goffard [France] ; Yves Rouillé [France] ; Jean Dubuisson [France] ; Sandrine Belouzard [France]Source :
- The Journal of Biological Chemistry [ 0021-9258 ] ; 2019.
English descriptors
- mix :
Abstract
Coronavirus M proteins represent the major protein component of the viral
envelope. They play an essential role during viral assembly by interacting with
all of the other structural proteins. Coronaviruses bud into the endoplasmic
reticulum (ER)–Golgi intermediate compartment (ERGIC), but the mechanisms
by which M proteins are transported from their site of synthesis, the ER, to the
budding site remain poorly understood. Here, we investigated the intracellular
trafficking of the Middle East respiratory syndrome coronavirus (MERS-CoV) M
protein. Subcellular localization analyses revealed that the MERS-CoV M protein
is retained intracellularly in the
Url:
DOI: 10.1074/jbc.RA119.008964
PubMed: 31399512
PubMed Central: 6768645
Affiliations:
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Le document en format XML
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-Golgi network localization signal</title>
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-Golgi network localization signal</title>
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<author><name sortKey="Goffard, Anne" sort="Goffard, Anne" uniqKey="Goffard A" first="Anne" last="Goffard">Anne Goffard</name>
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<author><name sortKey="Rouille, Yves" sort="Rouille, Yves" uniqKey="Rouille Y" first="Yves" last="Rouillé">Yves Rouillé</name>
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<author><name sortKey="Dubuisson, Jean" sort="Dubuisson, Jean" uniqKey="Dubuisson J" first="Jean" last="Dubuisson">Jean Dubuisson</name>
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<author><name sortKey="Belouzard, Sandrine" sort="Belouzard, Sandrine" uniqKey="Belouzard S" first="Sandrine" last="Belouzard">Sandrine Belouzard</name>
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<series><title level="j">The Journal of Biological Chemistry</title>
<idno type="ISSN">0021-9258</idno>
<idno type="eISSN">1083-351X</idno>
<imprint><date when="2019">2019</date>
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<profileDesc><textClass><keywords scheme="mix" xml:lang="en"><term>Middle East respiratory syndrome</term>
<term>Viral protein</term>
<term>coronavirus</term>
<term>endoplasmic reticulum</term>
<term>intracellular trafficking</term>
<term>plasma membrane</term>
<term>protein motif</term>
<term>protein sorting</term>
<term>trans- Golgi network localization</term>
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<front><div type="abstract" xml:lang="en"><p>Coronavirus M proteins represent the major protein component of the viral
envelope. They play an essential role during viral assembly by interacting with
all of the other structural proteins. Coronaviruses bud into the endoplasmic
reticulum (ER)–Golgi intermediate compartment (ERGIC), but the mechanisms
by which M proteins are transported from their site of synthesis, the ER, to the
budding site remain poorly understood. Here, we investigated the intracellular
trafficking of the Middle East respiratory syndrome coronavirus (MERS-CoV) M
protein. Subcellular localization analyses revealed that the MERS-CoV M protein
is retained intracellularly in the <italic>trans</italic>
-Golgi network (TGN),
and we identified two motifs in the distal part of the C-terminal domain as
being important for this specific localization. We identified the first motif as
a functional diacidic DxE ER export signal, because substituting Asp-211 and
Glu-213 with alanine induced retention of the MERS-CoV M in the ER. The second
motif, <sup>199</sup>
KxGxYR<sup>204</sup>
, was responsible for retaining the M
protein in the TGN. Substitution of this motif resulted in MERS-CoV M leakage
toward the plasma membrane. We further confirmed the role of
<sup>199</sup>
KxGxYR<sup>204</sup>
as a TGN retention signal by using
chimeras between MERS-CoV M and the M protein of infectious bronchitis virus
(IBV). Our results indicated that the C-terminal domains of both proteins
determine their specific localization, namely TGN and
ERGIC/<italic>cis</italic>
-Golgi for MERS-M and IBV-M, respectively. Our
findings indicate that MERS-CoV M protein localizes to the TGN because of the
combined presence of an ER export signal and a TGN retention motif.</p>
</div>
</front>
<back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Masters, P X0a S" uniqKey="Masters P">P.
S. Masters</name>
</author>
</analytic>
</biblStruct>
<biblStruct><analytic><author><name sortKey="Perlman, S" uniqKey="Perlman S">S. Perlman</name>
</author>
<author><name sortKey="Netland, J" uniqKey="Netland J">J. Netland</name>
</author>
</analytic>
</biblStruct>
<biblStruct><analytic><author><name sortKey="Corman, V X0a M" uniqKey="Corman V">V.
M. Corman</name>
</author>
<author><name sortKey="Muth, D" uniqKey="Muth D">D. Muth</name>
</author>
<author><name sortKey="Niemeyer, D" uniqKey="Niemeyer D">D. Niemeyer</name>
</author>
<author><name sortKey="Drosten, C" uniqKey="Drosten C">C. Drosten</name>
</author>
</analytic>
</biblStruct>
<biblStruct><analytic><author><name sortKey="Belouzard, S" uniqKey="Belouzard S">S. Belouzard</name>
</author>
<author><name sortKey="Millet, J X0a K" uniqKey="Millet J">J.
K. Millet</name>
</author>
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</biblStruct>
<biblStruct><analytic><author><name sortKey="Heald Sargent, T" uniqKey="Heald Sargent T">T. Heald-Sargent</name>
</author>
<author><name sortKey="Gallagher, T" uniqKey="Gallagher T">T. Gallagher</name>
</author>
</analytic>
</biblStruct>
<biblStruct><analytic><author><name sortKey="Ruch, T X0a R" uniqKey="Ruch T">T.
R. Ruch</name>
</author>
<author><name sortKey="Machamer, C X0a E" uniqKey="Machamer C">C.
E. Machamer</name>
</author>
</analytic>
</biblStruct>
<biblStruct><analytic><author><name sortKey="Nieto Torres, J X0a L" uniqKey="Nieto Torres J">J.
L. Nieto-Torres</name>
</author>
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