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- Publisher Website: 10.1016/j.virol.2010.12.050
- Scopus: eid_2-s2.0-79952538098
- PMID: 21262514
- WOS: WOS:000288778200010
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Article: Dengue virus PrM/M proteins fail to show pH-dependent ion channel activity in Xenopus oocytes
Title | Dengue virus PrM/M proteins fail to show pH-dependent ion channel activity in Xenopus oocytes |
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Authors | |
Keywords | Dengue virus Ion channels M protein PrM Xenopus oocytes |
Issue Date | 2011 |
Citation | Virology, 2011, v. 412, n. 1, p. 83-90 How to Cite? |
Abstract | The transmembrane domains (TMDs) of dengue virus type-1 M protein (DENV-1M) were reported to form cation-selective channels in artificial lipid bilayers. We further explored this observation using the two-electrode voltage clamp (TEVC) method on the Xenopus laevis oocytes expressing DENV PrM and M proteins. Using myc epitope tagged M proteins, M was first shown to adopt its predicted native topology in mammalian cells when expressed on its own. The recombinant proteins were then successfully expressed on the surface of Xenopus oocytes. Using influenza A M2 (Inf A/M2) protein as a control, we measured the conductance of oocytes expressing DENV proteins under hyperpolarized or low-pH conditions. Inf A/M2 showed pH-dependent, amantadine-sensitive channel activity that was consistent with previously published reports. However, no activity was detected for DENV proteins. We conclude that DENV PrM and M proteins do not show pH-activated ion channel activity. © 2011 Elsevier Inc. |
Persistent Identifier | http://hdl.handle.net/10722/311923 |
ISSN | 2023 Impact Factor: 2.8 2023 SCImago Journal Rankings: 0.838 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Wong, Sook San | - |
dc.contributor.author | Chebib, Mary | - |
dc.contributor.author | Haqshenas, Gholamreza | - |
dc.contributor.author | Loveland, Bruce | - |
dc.contributor.author | Gowans, Eric J. | - |
dc.date.accessioned | 2022-04-06T04:31:46Z | - |
dc.date.available | 2022-04-06T04:31:46Z | - |
dc.date.issued | 2011 | - |
dc.identifier.citation | Virology, 2011, v. 412, n. 1, p. 83-90 | - |
dc.identifier.issn | 0042-6822 | - |
dc.identifier.uri | http://hdl.handle.net/10722/311923 | - |
dc.description.abstract | The transmembrane domains (TMDs) of dengue virus type-1 M protein (DENV-1M) were reported to form cation-selective channels in artificial lipid bilayers. We further explored this observation using the two-electrode voltage clamp (TEVC) method on the Xenopus laevis oocytes expressing DENV PrM and M proteins. Using myc epitope tagged M proteins, M was first shown to adopt its predicted native topology in mammalian cells when expressed on its own. The recombinant proteins were then successfully expressed on the surface of Xenopus oocytes. Using influenza A M2 (Inf A/M2) protein as a control, we measured the conductance of oocytes expressing DENV proteins under hyperpolarized or low-pH conditions. Inf A/M2 showed pH-dependent, amantadine-sensitive channel activity that was consistent with previously published reports. However, no activity was detected for DENV proteins. We conclude that DENV PrM and M proteins do not show pH-activated ion channel activity. © 2011 Elsevier Inc. | - |
dc.language | eng | - |
dc.relation.ispartof | Virology | - |
dc.subject | Dengue virus | - |
dc.subject | Ion channels | - |
dc.subject | M protein | - |
dc.subject | PrM | - |
dc.subject | Xenopus oocytes | - |
dc.title | Dengue virus PrM/M proteins fail to show pH-dependent ion channel activity in Xenopus oocytes | - |
dc.type | Article | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1016/j.virol.2010.12.050 | - |
dc.identifier.pmid | 21262514 | - |
dc.identifier.scopus | eid_2-s2.0-79952538098 | - |
dc.identifier.volume | 412 | - |
dc.identifier.issue | 1 | - |
dc.identifier.spage | 83 | - |
dc.identifier.epage | 90 | - |
dc.identifier.eissn | 1096-0341 | - |
dc.identifier.isi | WOS:000288778200010 | - |