O-GlcNAc modification of the coat protein of the potyvirus Plum pox virus enhances viral infection

José de Jesús Pérez; Namrata D. Udeshi; Jeffrey Shabanowitz; Sergio Ciordia; Silvia Juárez; Cheryl L. Scott; Neil E. Olszewski; Donald F. Hunt; Juan Antonio García

doi:10.1016/j.virol.2013.03.029

O-GlcNAc modification of the coat protein of the potyvirus Plum pox virus enhances viral infection

José de Jesús Pérez
, Namrata D. Udeshi
, Jeffrey Shabanowitz
, Sergio Ciordia
, Silvia Juárez
, Cheryl L. Scott
, Neil E. Olszewski
, Donald F. Hunt
, Juan Antonio García

Research output: Contribution to journal › Article › peer-review

40 Scopus citations

Abstract

O-GlcNAcylation is a dynamic protein modification which has been studied mainly in metazoans. We reported previously that an Arabidopsis thaliana O-GlcNAc transferase modifies at least two threonine residues of the Plum pox virus (PPV) capsid protein (CP). Now, six additional residues were shown to be involved in O-GlcNAc modification of PPV CP. CP O-GlcNAcylation was abolished in the PPV CP7-T/A mutant, in which seven threonines were mutated. PPV CP7-T/A infected Nicotiana clevelandii, Nicotiana benthamiana, and Prunus persica without noticeable defects. However, defects in infection of A. thaliana were readily apparent. In mixed infections of wild-type arabidopsis, the CP7-T/A mutant was outcompeted by wild-type virus. These results indicate that CP O-GlcNAcylation has a major role in the infection process. O-GlcNAc modification may have a role in virion assembly and/or stability as the CP of PPV CP7-T/A was more sensitive to protease digestion than that of the wild-type virus.

Original language	English (US)
Pages (from-to)	122-131
Number of pages	10
Journal	Virology
Volume	442
Issue number	2
DOIs	https://doi.org/10.1016/j.virol.2013.03.029
State	Published - Aug 1 2013

Bibliographical note

Funding Information:
We thank Elvira Domínguez and Beatriz García García for technical assistance. This work was supported by Grants BIO2010-18541 from Spanish MCINN, SAL/0185/2006 from Comunidad de Madrid, and KBBE-204429 (SharCo) from the European Union to JAG, 2005×747_3 from the Spanish National Proteomics Institute (ProteoRed-ISC III) to SC and SJ, MCB-0112826 from National Science Foundation and DE-FG02-02ER15353 from US Department of Energy to NEO, and GM037537 from U.S. Public Health Service to DFH.

Keywords

Capsid protein
Mass spectrometry
O-GlcNAcylation
Plum pox virus
Potyvirus

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10.1016/j.virol.2013.03.029

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title = "O-GlcNAc modification of the coat protein of the potyvirus Plum pox virus enhances viral infection",

abstract = "O-GlcNAcylation is a dynamic protein modification which has been studied mainly in metazoans. We reported previously that an Arabidopsis thaliana O-GlcNAc transferase modifies at least two threonine residues of the Plum pox virus (PPV) capsid protein (CP). Now, six additional residues were shown to be involved in O-GlcNAc modification of PPV CP. CP O-GlcNAcylation was abolished in the PPV CP7-T/A mutant, in which seven threonines were mutated. PPV CP7-T/A infected Nicotiana clevelandii, Nicotiana benthamiana, and Prunus persica without noticeable defects. However, defects in infection of A. thaliana were readily apparent. In mixed infections of wild-type arabidopsis, the CP7-T/A mutant was outcompeted by wild-type virus. These results indicate that CP O-GlcNAcylation has a major role in the infection process. O-GlcNAc modification may have a role in virion assembly and/or stability as the CP of PPV CP7-T/A was more sensitive to protease digestion than that of the wild-type virus.",

keywords = "Capsid protein, Mass spectrometry, O-GlcNAcylation, Plum pox virus, Potyvirus",

author = "P{\'e}rez, \{Jos{\'e} de Jes{\'u}s\} and Udeshi, \{Namrata D.\} and Jeffrey Shabanowitz and Sergio Ciordia and Silvia Ju{\'a}rez and Scott, \{Cheryl L.\} and Olszewski, \{Neil E.\} and Hunt, \{Donald F.\} and Garc{\'i}a, \{Juan Antonio\}",

note = "Funding Information: We thank Elvira Dom{\'i}nguez and Beatriz Garc{\'i}a Garc{\'i}a for technical assistance. This work was supported by Grants BIO2010-18541 from Spanish MCINN, SAL/0185/2006 from Comunidad de Madrid, and KBBE-204429 (SharCo) from the European Union to JAG, 2005×747\_3 from the Spanish National Proteomics Institute (ProteoRed-ISC III) to SC and SJ, MCB-0112826 from National Science Foundation and DE-FG02-02ER15353 from US Department of Energy to NEO, and GM037537 from U.S. Public Health Service to DFH. ",

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doi = "10.1016/j.virol.2013.03.029",

language = "English (US)",

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T1 - O-GlcNAc modification of the coat protein of the potyvirus Plum pox virus enhances viral infection

AU - Pérez, José de Jesús

AU - Udeshi, Namrata D.

AU - Shabanowitz, Jeffrey

AU - Ciordia, Sergio

AU - Juárez, Silvia

AU - Scott, Cheryl L.

AU - Olszewski, Neil E.

AU - Hunt, Donald F.

AU - García, Juan Antonio

N1 - Funding Information: We thank Elvira Domínguez and Beatriz García García for technical assistance. This work was supported by Grants BIO2010-18541 from Spanish MCINN, SAL/0185/2006 from Comunidad de Madrid, and KBBE-204429 (SharCo) from the European Union to JAG, 2005×747_3 from the Spanish National Proteomics Institute (ProteoRed-ISC III) to SC and SJ, MCB-0112826 from National Science Foundation and DE-FG02-02ER15353 from US Department of Energy to NEO, and GM037537 from U.S. Public Health Service to DFH.

PY - 2013/8/1

Y1 - 2013/8/1

N2 - O-GlcNAcylation is a dynamic protein modification which has been studied mainly in metazoans. We reported previously that an Arabidopsis thaliana O-GlcNAc transferase modifies at least two threonine residues of the Plum pox virus (PPV) capsid protein (CP). Now, six additional residues were shown to be involved in O-GlcNAc modification of PPV CP. CP O-GlcNAcylation was abolished in the PPV CP7-T/A mutant, in which seven threonines were mutated. PPV CP7-T/A infected Nicotiana clevelandii, Nicotiana benthamiana, and Prunus persica without noticeable defects. However, defects in infection of A. thaliana were readily apparent. In mixed infections of wild-type arabidopsis, the CP7-T/A mutant was outcompeted by wild-type virus. These results indicate that CP O-GlcNAcylation has a major role in the infection process. O-GlcNAc modification may have a role in virion assembly and/or stability as the CP of PPV CP7-T/A was more sensitive to protease digestion than that of the wild-type virus.

AB - O-GlcNAcylation is a dynamic protein modification which has been studied mainly in metazoans. We reported previously that an Arabidopsis thaliana O-GlcNAc transferase modifies at least two threonine residues of the Plum pox virus (PPV) capsid protein (CP). Now, six additional residues were shown to be involved in O-GlcNAc modification of PPV CP. CP O-GlcNAcylation was abolished in the PPV CP7-T/A mutant, in which seven threonines were mutated. PPV CP7-T/A infected Nicotiana clevelandii, Nicotiana benthamiana, and Prunus persica without noticeable defects. However, defects in infection of A. thaliana were readily apparent. In mixed infections of wild-type arabidopsis, the CP7-T/A mutant was outcompeted by wild-type virus. These results indicate that CP O-GlcNAcylation has a major role in the infection process. O-GlcNAc modification may have a role in virion assembly and/or stability as the CP of PPV CP7-T/A was more sensitive to protease digestion than that of the wild-type virus.

KW - Capsid protein

KW - Mass spectrometry

KW - O-GlcNAcylation

KW - Plum pox virus

KW - Potyvirus

UR - https://www.scopus.com/pages/publications/84879154181

UR - https://www.scopus.com/pages/publications/84879154181#tab=citedBy

U2 - 10.1016/j.virol.2013.03.029

DO - 10.1016/j.virol.2013.03.029

M3 - Article

C2 - 23639873

AN - SCOPUS:84879154181

SN - 0042-6822

VL - 442

SP - 122

EP - 131

JO - Virology

JF - Virology

IS - 2

ER -

O-GlcNAc modification of the coat protein of the potyvirus Plum pox virus enhances viral infection

Abstract

Bibliographical note

Keywords

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