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Membrane permeabilization of the African horse sickness virus VP5 protein is mediated by two N-termi...

Membrane permeabilization of the African horse sickness virus VP5 protein is mediated by two N-termi...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_859490126

Membrane permeabilization of the African horse sickness virus VP5 protein is mediated by two N-terminal amphipathic α-helices

About this item

Full title

Membrane permeabilization of the African horse sickness virus VP5 protein is mediated by two N-terminal amphipathic α-helices

Publisher

Vienna: Springer Vienna

Journal title

Archives of virology, 2011-04, Vol.156 (4), p.711-715

Language

English

Formats

Publication information

Publisher

Vienna: Springer Vienna

More information

Scope and Contents

Contents

The VP5 outer capsid protein of African horse sickness virus (AHSV) is cytotoxic when expressed in
Spodoptera frugiperda
(Sf-9) cells. Secondary structure analysis of the VP5 amino acid sequence of AHSV-9 identified two N-terminal amphipathic α-helices within the first 43 amino acids. Baculovirus expression of N- and C-terminal truncated VP5...

Alternative Titles

Full title

Membrane permeabilization of the African horse sickness virus VP5 protein is mediated by two N-terminal amphipathic α-helices

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_859490126

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_859490126

Other Identifiers

ISSN

0304-8608

E-ISSN

1432-8798

DOI

10.1007/s00705-010-0897-4

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