Viral Ion Channel Proteins in Model Membranes: a Comparative Study by X-ray Reflectivity

Overview

Journal Eur Biophys J

Specialty Biophysics

Date 2006 Oct 5

PMID 17019591

Citations 2

Authors

Z Khattari

E Arbely

I T Arkin

T Salditt

Affiliations

Soon will be listed here.

Abstract

We have investigated the effect of the transmembrane domain of three viral ion channel proteins on the lipid bilayer structure by X-ray reflectivity and scattering from oriented planar bilayers. The proteins show a similar effect on the lipid bilayer structural parameters: an increase in the lipid bilayer hydrophobic core, a decrease in the amplitude of the vertical density profile and a systematic change in the ordering of the acyl chains as a function of protein-to-lipid ratio. These results are discussed in a comparative view.

Citing Articles

Peptide model helices in lipid membranes: insertion, positioning, and lipid response on aggregation studied by X-ray scattering.

Schneggenburger P, Beerlink A, Weinhausen B, Salditt T, Diederichsen U Eur Biophys J. 2010; 40(4):417-36.

PMID: 21181143 PMC: 3070074. DOI: 10.1007/s00249-010-0645-4.

Viral channel-forming proteins.

Fischer W, Kruger J Int Rev Cell Mol Biol. 2009; 275:35-63.

PMID: 19491052 PMC: 7104957. DOI: 10.1016/S1937-6448(09)75002-6.

References

Kukol A, Arkin I . vpu transmembrane peptide structure obtained by site-specific fourier transform infrared dichroism and global molecular dynamics searching. Biophys J. 1999; 77(3):1594-601. PMC: 1300447. DOI: 10.1016/S0006-3495(99)77007-4. View

Schubert U, Ferrer-Montiel A, Henklein P, Strebel K, Montal M . Identification of an ion channel activity of the Vpu transmembrane domain and its involvement in the regulation of virus release from HIV-1-infected cells. FEBS Lett. 1996; 398(1):12-8. DOI: 10.1016/s0014-5793(96)01146-5. View

Zhang Y, LEWIS R, Henry G, Sykes B, Hodges R, McElhaney R . Peptide models of helical hydrophobic transmembrane segments of membrane proteins. 1. Studies of the conformation, intrabilayer orientation, and amide hydrogen exchangeability of Ac-K2-(LA)12-K2-amide. Biochemistry. 1995; 34(7):2348-61. DOI: 10.1021/bi00007a031. View

Munster C, Lu J, Bechinger B, Salditt T . Grazing incidence X-ray diffraction of highly aligned phospholipid membranes containing the antimicrobial peptide magainin 2. Eur Biophys J. 2000; 28(8):683-8. DOI: 10.1007/s002490050008. View

Salditt T . Lipid-peptide interaction in oriented bilayers probed by interface-sensitive scattering methods. Curr Opin Struct Biol. 2003; 13(4):467-78. DOI: 10.1016/s0959-440x(03)00113-1. View

Poutanen S, Low D, Henry B, Finkelstein S, Rose D, Green K . Identification of severe acute respiratory syndrome in Canada. N Engl J Med. 2003; 348(20):1995-2005. DOI: 10.1056/NEJMoa030634. View

Arbely E, Khattari Z, Brotons G, Akkawi M, Salditt T, Arkin I . A highly unusual palindromic transmembrane helical hairpin formed by SARS coronavirus E protein. J Mol Biol. 2004; 341(3):769-79. PMC: 7134595. DOI: 10.1016/j.jmb.2004.06.044. View

Wu Y, He K, Ludtke S, Huang H . X-ray diffraction study of lipid bilayer membranes interacting with amphiphilic helical peptides: diphytanoyl phosphatidylcholine with alamethicin at low concentrations. Biophys J. 1995; 68(6):2361-9. PMC: 1282146. DOI: 10.1016/S0006-3495(95)80418-2. View

Killian J, Salemink I, de Planque M, LINDBLOM G, Koeppe 2nd R, Greathouse D . Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane alpha-helical peptides: importance of hydrophobic mismatch and proposed role of tryptophans. Biochemistry. 1996; 35(3):1037-45. DOI: 10.1021/bi9519258. View

10.

Wilson L, McKinlay C, Gage P, Ewart G . SARS coronavirus E protein forms cation-selective ion channels. Virology. 2004; 330(1):322-31. PMC: 7111769. DOI: 10.1016/j.virol.2004.09.033. View

11.

Sugrue R, Hay A . Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel. Virology. 1991; 180(2):617-24. PMC: 7131614. DOI: 10.1016/0042-6822(91)90075-m. View

12.

Sharpe S, Yau W, Tycko R . Structure and dynamics of the HIV-1 Vpu transmembrane domain revealed by solid-state NMR with magic-angle spinning. Biochemistry. 2006; 45(3):918-33. DOI: 10.1021/bi051766k. View

13.

Tian C, Gao P, Pinto L, Lamb R, Cross T . Initial structural and dynamic characterization of the M2 protein transmembrane and amphipathic helices in lipid bilayers. Protein Sci. 2003; 12(11):2597-605. PMC: 2366949. DOI: 10.1110/ps.03168503. View

14.

Duff K, Ashley R . The transmembrane domain of influenza A M2 protein forms amantadine-sensitive proton channels in planar lipid bilayers. Virology. 1992; 190(1):485-9. DOI: 10.1016/0042-6822(92)91239-q. View

15.

Chen F, Lee M, Huang H . Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation. Biophys J. 2003; 84(6):3751-8. PMC: 1302957. DOI: 10.1016/S0006-3495(03)75103-0. View

16.

Vijayvergiya V, Wilson R, Chorak A, Gao P, Cross T, Busath D . Proton conductance of influenza virus M2 protein in planar lipid bilayers. Biophys J. 2004; 87(3):1697-704. PMC: 1304574. DOI: 10.1529/biophysj.104.043018. View

17.

Sakaguchi T, Tu Q, Pinto L, Lamb R . The active oligomeric state of the minimalistic influenza virus M2 ion channel is a tetramer. Proc Natl Acad Sci U S A. 1997; 94(10):5000-5. PMC: 24620. DOI: 10.1073/pnas.94.10.5000. View

18.

Pinto L, Dieckmann G, Gandhi C, Papworth C, Braman J, Shaughnessy M . A functionally defined model for the M2 proton channel of influenza A virus suggests a mechanism for its ion selectivity. Proc Natl Acad Sci U S A. 1997; 94(21):11301-6. PMC: 23448. DOI: 10.1073/pnas.94.21.11301. View

19.

Kukol A, Adams P, Rice L, Brunger A, Arkin T . Experimentally based orientational refinement of membrane protein models: A structure for the Influenza A M2 H+ channel. J Mol Biol. 1999; 286(3):951-62. DOI: 10.1006/jmbi.1998.2512. View

20.

Schubert U, Bour S, Ferrer-Montiel A, Montal M, Maldarell F, Strebel K . The two biological activities of human immunodeficiency virus type 1 Vpu protein involve two separable structural domains. J Virol. 1996; 70(2):809-19. PMC: 189883. DOI: 10.1128/JVI.70.2.809-819.1996. View