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Differential transport of Influenza A neuraminidase signal anchor peptides to the plasma membrane
- Source :
- FEBS Letters. 587:1411-1417
- Publication Year :
- 2013
- Publisher :
- Wiley, 2013.
-
Abstract
- Influenza A Neuraminidase is essential for virus release from the cell surface of host cells. Given differential structures of the N-terminal sequences including the transmembrane domains of neuraminidase subtypes, we investigated their contribution to transport and localization of subtypes N1, N2 and N8 to the plasma membrane. We generated consensus sequences from all protein entries available for these subtypes. We found that 40N-terminal the forty N-terminal amino acids are sufficient to confer plasma membrane localization of fusion proteins, albeit with different efficiencies. Strikingly, subtle differences in the primary structure of the part of the transmembrane domain that resides in the exoplasmic leaflet of the membrane have a major impact on transport efficiency, providing a potential target for the inhibition of virus release.
- Subjects :
- Models, Molecular
Molecular Sequence Data
Biophysics
Neuraminidase
Influenza A
Protein Sorting Signals
Biochemistry
Transmembrane domain
Protein structure
Structural Biology
Consensus Sequence
Genetics
Humans
Amino Acid Sequence
Molecular Biology
Peptide sequence
chemistry.chemical_classification
Trafficking
biology
Cell Membrane
Cell Biology
Fusion protein
Virus Release
Protein Structure, Tertiary
Transport protein
Cell biology
Amino acid
Protein Transport
chemistry
Influenza A virus
biology.protein
HeLa Cells
Subjects
Details
- ISSN :
- 18733468 and 00145793
- Volume :
- 587
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....6c4030e8a9004d198460be5860d5041c