Author | dc.contributor.author | Sotelo, Pablo H. | |
Author | dc.contributor.author | Schümann, Michael | es_CL |
Author | dc.contributor.author | Krause, Eberhard | es_CL |
Author | dc.contributor.author | Chnaiderman Figueroa, Jonás | es_CL |
Admission date | dc.date.accessioned | 2010-07-02T14:23:23Z | |
Available date | dc.date.available | 2010-07-02T14:23:23Z | |
Publication date | dc.date.issued | 2010 | |
Cita de ítem | dc.identifier.citation | Virus Research 149 (2010) 104–108 | en_US |
Identifier | dc.identifier.other | doi:10.1016/j.virusres.2009.12.006 | |
Identifier | dc.identifier.uri | https://repositorio.uchile.cl/handle/2250/128667 | |
Abstract | dc.description.abstract | Genomic replication and partial assembly of Rotavirus takes place in cytoplasmic viral structures called
viroplasms. NSP5 is a viral phosphoprotein localized in viroplasms and its expression is imperative for
viral cycle progress. During infection three isoforms of NSP5 can be observed by SDS-PAGE (26, 28 and
33–35 kDa) and previous reports suggested that they differ in their phosphorylation patterns. In this study
we obtained NSP5 from infected cells and by mass spectrometry we were able to identify nine phosphorylation
sites. We detected that in all the isoforms the same residues can be found either phosphorylated
or unmodified. Quantitative analysis showed that the 28 kDa isoform has a higher phosphorylation level
than the 26 kDa isoform suggesting that migration properties depend on the total number of phosphorylated
residues. Moreover, we identified two not previously described modifications for this protein: an
N-acetylation in Serine-2 and an intramolecular disulfide bond in a highly conserved motif, CXXC which
is located between two charged alpha-helix motifs. | en_US |
Patrocinador | dc.description.sponsorship | This work was supported by Fundación ANDES and VRID from
Universidad de Chile. P.S.wassupported by aDAADdoctoral fellowship.
Anti-NSP5 antibody was kindly provided by Dr. John Patton
(NIAID, NIH, USA). | en_US |
Lenguage | dc.language.iso | en | en_US |
Publisher | dc.publisher | ELSEVIER | en_US |
Keywords | dc.subject | Rotavirus NSP5 | en_US |
Título | dc.title | Analysis of rotavirus non-structural protein NSP5 by mass spectrometry reveals a complex phosphorylation pattern | en_US |
Document type | dc.type | Artículo de revista | |