Different forms of African cassava mosaic virus capsid protein within plants 
and virions

Hipp, Katharina; Zikeli, Kerstin; Kepp, Gabi; Schmid, Lena; Shoeman, Robert L.; P.Jurkowski, Tomasz; Kleinow, Tatjana; Jeske, Holger

doi:10.1016/j.virol.2019.01.018

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Different forms of African cassava mosaic virus capsid protein within plants and virions

MPS-Authors

/persons/resource/persons95345

Shoeman, Robert L.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;
Coherent diffractive imaging, Max Planck Institute for Medical Research, Max Planck Society;
Analytical Protein Biochemistry, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

https://www.sciencedirect.com/science/article/pii/S0042682219300182/pdfft?md5=49161a2dad749bd00262ff511bfa9992&pid=1-s2.0-S0042682219300182-main.pdf
(Any fulltext)

https://doi.org/10.1016/j.virol.2019.01.018
(Any fulltext)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Hipp, K., Zikeli, K., Kepp, G., Schmid, L., Shoeman, R. L., P.Jurkowski, T., et al. (2019). Different forms of African cassava mosaic virus capsid protein within plants and virions. Virology, 529, 81-90. doi:10.1016/j.virol.2019.01.018.

Cite as: https://hdl.handle.net/21.11116/0000-0003-7624-0

Abstract

One geminiviral gene encodes the capsid protein (CP), which can appear as several bands after electrophoresis depending on virus and plant. African cassava mosaic virus-Nigeria CP in Nicotiana benthamiana, however, yielded one band (~ 30 kDa) in total protein extracts and purified virions, although its expression in yeast yielded two bands (~ 30, 32 kDa). Mass spectrometry of the complete protein and its tryptic fragments from virions is consistent with a cleaved start M1, acetylated S2, and partial phosphorylation at T12, S25 and S62. Mutants for additional potentially modified sites (N223A; C235A) were fully infectious and formed geminiparticles. Separation in triton acetic acid urea gels confirmed charge changes of the CP between plants and yeast indicating differential phosphorylation. If the CP gene alone was expressed in plants, multiple bands were observed like in yeast. A high turnover rate indicates that post-translational modifications promote CP decay probably via the ubiquitin-triggered proteasomal pathway.