4.4 Article

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

期刊

VIROLOGY
卷 442, 期 2, 页码 122-131

出版社

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2013.03.029

关键词

O-GlcNAcylation; Plum pox virus; Potyvirus; Capsid protein; Mass spectrometry

类别

资金

  1. Spanish MCINN [BIO2010-18541]
  2. Comunidad de Madrid [SAL/0185/2006]
  3. European Union [KBBE-204429]
  4. Spanish National Proteomics Institute (ProteoRed-ISC III) [2005 x 747_3]
  5. National Science Foundation [MCB-0112826]
  6. US Department of Energy [DE-FG02-02ER15353]
  7. U.S. Public Health Service [GM037537]

向作者/读者索取更多资源

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 out-competed 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. (C) 2013 Elsevier Inc. All rights reserved.

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