dc.contributor.author | Pakkanen, Kirsi | |
dc.contributor.author | Karttunen, Jenni | |
dc.contributor.author | Virtanen, Salla | |
dc.contributor.author | Vuento, Matti | |
dc.date.accessioned | 2015-11-03T11:15:31Z | |
dc.date.available | 2015-11-03T11:15:31Z | |
dc.date.issued | 2008 | |
dc.identifier.citation | Pakkanen, K., Karttunen, J., Virtanen, S., & Vuento, M. (2008). Sphingomyelin induces structural alteration in canine parvovirus capsid. <i>Virus Research</i>, <i>132</i>, 187-191. <a href="https://doi.org/10.1016/j.virusres.2007.10.008" target="_blank">https://doi.org/10.1016/j.virusres.2007.10.008</a> | |
dc.identifier.other | CONVID_17289195 | |
dc.identifier.other | TUTKAID_27938 | |
dc.identifier.uri | https://jyx.jyu.fi/handle/123456789/47553 | |
dc.description.abstract | One of the essential steps in canine parvovirus (CPV) infection, the release from endosomal vesicles, is dominated by interactions between the
virus capsid and the endosomal membranes. In this study, the effect of sphingomyelin and phosphatidyl serine on canine parvovirus capsid and
on the phospholipase A2 (PLA2) activity of CPV VP1 unique N-terminus was analyzed. Accordingly, a significant (P ≤ 0.05) shift of tryptophan
fluorescence emission peak was detected at pH 5.5 in the presence of sphingomyelin, whereas at pH 7.4 a similar but minor shift was observed. This
effect may relate to the exposure of VP1 N-terminus in acidic pH as well as to interactions between sphingomyelin and CPV. When the phenomenon
was further characterized using circular dichroism spectroscopy, differences in CPV capsid CD spectra with and without sphingomyelin and
phosphatidyl serine were detected, corresponding to data obtained with tryptophan fluorescence. However, when the enzymatic activity of CPV
PLA2 was tested in the presence of sphingomyelin, no significant effect in the function of the enzyme was detected. Thus, the structural changes
observed with spectroscopic techniques appear not to manipulate the activity of CPV PLA2, and may therefore implicate alternative interactions
between CPV capsid and sphingomyelin. | |
dc.language.iso | eng | |
dc.publisher | Elsevier B.V. | |
dc.relation.ispartofseries | Virus Research | |
dc.subject.other | koiran parvovirus | |
dc.subject.other | sfingomyeliini | |
dc.subject.other | tryptofaanifluoresenssi | |
dc.title | Sphingomyelin induces structural alteration in canine parvovirus capsid | |
dc.type | article | |
dc.identifier.urn | URN:NBN:fi:jyu-201511023566 | |
dc.contributor.laitos | Bio- ja ympäristötieteiden laitos | fi |
dc.contributor.laitos | Department of Biological and Environmental Science | en |
dc.contributor.oppiaine | Solu- ja molekyylibiologia | fi |
dc.contributor.oppiaine | Cell and Molecular Biology | en |
dc.type.uri | http://purl.org/eprint/type/JournalArticle | |
dc.date.updated | 2015-11-02T10:15:12Z | |
dc.type.coar | http://purl.org/coar/resource_type/c_2df8fbb1 | |
dc.description.reviewstatus | peerReviewed | |
dc.format.pagerange | 187-191 | |
dc.relation.issn | 0168-1702 | |
dc.relation.volume | 132 | |
dc.type.version | acceptedVersion | |
dc.rights.copyright | © 2007 Elsevier B.V. This is a final draft version of an article whose final and definitive form has been published by Elsevier. Published in this repository with the kind permission of the publisher. | |
dc.rights.accesslevel | openAccess | fi |
dc.relation.doi | 10.1016/j.virusres.2007.10.008 | |
dc.type.okm | A1 | |