» Articles » PMID: 17229713

Targeting of the Sendai Virus C Protein to the Plasma Membrane Via a Peptide-only Membrane Anchor

Overview
Journal J Virol
Date 2007 Jan 19
PMID 17229713
Citations 13
Authors
Affiliations
Soon will be listed here.
Abstract

Several cellular proteins are synthesized in the cytosol on free ribosomes and then associate with membranes due to the presence of short peptide sequences. These membrane-targeting sequences contain sites to which lipid chains are attached, which help direct the protein to a particular membrane domain and anchor it firmly in the bilayer. The intracellular concentration of these proteins in particular cellular compartments, where their interacting partners are also concentrated, is essential to their function. This paper reports that the apparently unmodified N-terminal sequence of the Sendai virus C protein (MPSFLKKILKLRGRR . . .; letters in italics represent hydrophobic residues; underlined letters represent basic residues, which has a strong propensity to form an amphipathic alpha-helix in a hydrophobic environment) also function as a membrane targeting signal and membrane anchor. Moreover, the intracellular localization of the C protein at the plasma membrane is essential for inducing the interferon-independent phosphorylation of Stat1 as part of the viral program to prevent the cellular antiviral response.

Citing Articles

C Proteins: Controllers of Orderly Paramyxovirus Replication and of the Innate Immune Response.

Siering O, Cattaneo R, Pfaller C Viruses. 2022; 14(1).

PMID: 35062341 PMC: 8778822. DOI: 10.3390/v14010137.


Structural Insight into the Interaction of Sendai Virus C Protein with Alix To Stimulate Viral Budding.

Oda K, Matoba Y, Sugiyama M, Sakaguchi T J Virol. 2021; 95(19):e0081521.

PMID: 34287046 PMC: 8428403. DOI: 10.1128/JVI.00815-21.


Structural analysis of the STAT1:STAT2 heterodimer revealed the mechanism of Sendai virus C protein-mediated blockade of type 1 interferon signaling.

Oda K, Oda T, Matoba Y, Sato M, Irie T, Sakaguchi T J Biol Chem. 2017; 292(48):19752-19766.

PMID: 28978648 PMC: 5712616. DOI: 10.1074/jbc.M117.786285.


Degradation, Promoter Recruitment and Transactivation Mediated by the Extreme N-Terminus of MHC Class II Transactivator CIITA Isoform III.

Beaulieu Y, Leon Machado J, Ethier S, Gaudreau L, Steimle V PLoS One. 2016; 11(2):e0148753.

PMID: 26871568 PMC: 4752451. DOI: 10.1371/journal.pone.0148753.


Evolution and structural organization of the C proteins of paramyxovirinae.

Lo M, Sogaard T, Karlin D PLoS One. 2014; 9(2):e90003.

PMID: 24587180 PMC: 3934983. DOI: 10.1371/journal.pone.0090003.


References
1.
Arbuzova A, Wang L, Wang J, Murray D, Honig B, McLaughlin S . Membrane binding of peptides containing both basic and aromatic residues. Experimental studies with peptides corresponding to the scaffolding region of caveolin and the effector region of MARCKS. Biochemistry. 2000; 39(33):10330-9. DOI: 10.1021/bi001039j. View

2.
Boggs J . Myelin basic protein: a multifunctional protein. Cell Mol Life Sci. 2006; 63(17):1945-61. PMC: 11136439. DOI: 10.1007/s00018-006-6094-7. View

3.
Abrami L, Fivaz M, van der Goot F . Surface dynamics of aerolysin on the plasma membrane of living cells. Int J Med Microbiol. 2000; 290(4-5):363-7. DOI: 10.1016/S1438-4221(00)80042-9. View

4.
Sen G . Viruses and interferons. Annu Rev Microbiol. 2001; 55:255-81. DOI: 10.1146/annurev.micro.55.1.255. View

5.
Dyson H, Wright P . Coupling of folding and binding for unstructured proteins. Curr Opin Struct Biol. 2002; 12(1):54-60. DOI: 10.1016/s0959-440x(02)00289-0. View