Membrane activity of an amphiphilic alpha-helical membrane-proximal cytoplasmic domain of the MoMuLV envelope glycoprotein.

Experimental and Molecular Pathology
R M EpandYanina Rozenberg-Adler

Abstract

In the Moloney murine leukemia virus (MoMuLV) envelope glycoprotein (Env) we identified a membrane-proximal cytoplasmic domain (residues 598-616) that facilitates the Env incorporation into virions and Env-mediated fusion [Rozenberg, Y., Conner, J., Aguilar-Carreno, H., Chakraborti, S., Dimiter, D.S., Anderson, W.F., 2008. Viral entry: membrane-proximal cytoplasmic domain of MoMuLV envelope tail facilitates fusion. In the same issue. (accompanying paper)]. By biophysical methods (CD, EPR) a corresponding peptide (membrane-proximal peptide, 598-616) was demonstrated to form a membrane-parallel amphiphilic alpha-helix in the presence of membranes. Electrophysiological studies with planar bilayers and liposomes indicate that the membrane-proximal peptide is membrane destabilizing. This peptide and the fusion peptide from the MoMuLV transmembrane (TM) ectodomain were tested for their effect on the bilayer for hexagonal phase transition temperature of dipalmitoleoylphosphatidylethanolamine (T(H)). Importantly, the external fusion peptide and the internal membrane-proximal peptides of MoMuLV env exert opposite effects on membrane curvature. The fusion peptide lowers T(H) while the membrane proximal peptide raises it. These effects on...Continue Reading

References

Oct 19, 1979·Biochimica Et Biophysica Acta·F OlsonD Papahadjopoulos
Jan 1, 1978·Annual Review of Biochemistry·P Y Chou, G D Fasman
Dec 1, 1992·Photochemistry and Photobiology·Z T FarahbakhshW L Hubbell
Sep 1, 1988·Protein Engineering·V BiouJ Garnier
Jun 13, 1986·Biochimica Et Biophysica Acta·L D MayerP R Cullis
Jun 18, 1985·Biochemistry·H EllensF C Szoka
May 5, 1982·Journal of Molecular Biology·J Kyte, R F Doolittle
Jul 7, 1981·Biochemistry·D K StruckR E Pagano
Mar 1, 1994·Proceedings of the National Academy of Sciences of the United States of America·C AltenbachW L Hubbell
Apr 1, 1993·Proteins·Y V VenkatachalapathiG M Anantharamaiah
May 1, 1996·Nature Structural Biology·D FassP S Kim
Jan 1, 1996·Methods in Enzymology·J GarnierB Robson
Jul 15, 1996·Chemistry and Physics of Lipids·L Chernomordik
Dec 1, 1995·Nature Structural Biology·M LuP S Kim
Jan 3, 1997·The Journal of Biological Chemistry·M C LinB L Kagan
May 1, 1997·Trends in Biochemical Sciences·R BrasseurM Rosseneu
Feb 7, 1998·Proceedings of the National Academy of Sciences of the United States of America·A ChanturiyaJ Zimmerberg
Oct 6, 1998·The Journal of General Physiology·V I RazinkovF S Cohen
Nov 7, 1998·Biochimica Et Biophysica Acta·R M Epand
Jan 23, 1999·Methods in Enzymology·T A MirzabekovB L Kagan
Nov 11, 1999·Biochimica Et Biophysica Acta·A SilbersteinY Rozenberg
Nov 9, 2000·Cell Biology International·B P Jena
Jun 28, 2001·Bioscience Reports·R M Epand
Mar 27, 2004·Nature Reviews. Microbiology·Dimiter S Dimitrov
Apr 10, 2004·Science·Alicia E Smith, Ari Helenius
Dec 22, 2004·Current Topics in Microbiology and Immunology·L J EarpJ M White

❮ Previous
Next ❯

Citations

Feb 13, 2009·Journal of the American Chemical Society·Rachel S Signarvic, William F Degrado
Jan 29, 2008·Experimental and Molecular Pathology·Yanina Rozenberg-AdlerW French Anderson
Jul 11, 2013·PloS One·Sanath Kumar JanakaMarc C Johnson

❮ Previous
Next ❯

Related Concepts

Related Feeds

Cajal Bodies & Gems

Cajal bodies or coiled bodies are dense foci of coilin protein. Gemini of Cajal bodies, or gems, are microscopically similar to Cajal bodies. It is believed that Cajal bodies play important roles in RNA processing while gems assist the Cajal bodies. Find the latest research on Cajal bodies and gems here.