Membrane Penetration of Sendai Virus Glycoproteins During the Early Stages of Fusion with Liposomes As Determined by Hydrophobic Photoaffinity Labeling

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1988 Oct 1

PMID 2845406

Citations 22

Authors

S L Novick

D Hoekstra

Affiliations

Soon will be listed here.

Abstract

The hydrophobic photoaffinity label 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine was used to label Sendai virus proteins during fusion with cardiolipin and phosphatidylserine liposomes. Preferential labeling of the viral fusion protein during the initial stages of fusion demonstrated that this protein interacts with the hydrophobic core of the target membrane as an initiating event of virus-liposome fusion. Labeling showed time, temperature, and pH dependence consistent with earlier fluorescent measurements of fusion kinetics. The present method provides conclusive evidence supporting the hypothesis that hydrophobic interaction of the fusion protein with the target bilayer is an initial event in the fusion mechanism of viral membranes.

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References

Hoekstra D, Klappe K, de Boer T, Wilschut J . Characterization of the fusogenic properties of Sendai virus: kinetics of fusion with erythrocyte membranes. Biochemistry. 1985; 24(18):4739-45. DOI: 10.1021/bi00339a005. View

Hong K, Yoshimura T, Papahadjopoulos D . Interaction of clathrin with liposomes: pH-dependent fusion of phospholipid membranes induced by clathrin. FEBS Lett. 1985; 191(1):17-23. DOI: 10.1016/0014-5793(85)80985-6. View

Arvinte T, Hildenbrand K, Wahl P, Nicolau C . Lysozyme-induced fusion of liposomes with erythrocyte ghosts at acidic pH. Proc Natl Acad Sci U S A. 1986; 83(4):962-6. PMC: 322990. DOI: 10.1073/pnas.83.4.962. View

Kim J, Kim H . Fusion of phospholipid vesicles induced by alpha-lactalbumin at acidic pH. Biochemistry. 1986; 25(24):7867-74. DOI: 10.1021/bi00372a012. View

Klappe K, Wilschut J, Nir S, Hoekstra D . Parameters affecting fusion between Sendai virus and liposomes. Role of viral proteins, liposome composition, and pH. Biochemistry. 1986; 25(25):8252-60. DOI: 10.1021/bi00373a019. View

Lecompte M, Krishnaswamy S, Mann K, Nesheim M, Gitler C . Membrane penetration of bovine factor V and Va detected by labeling with 5-iodonaphthalene-1-azide. J Biol Chem. 1987; 262(5):1935-7. View

Schroit A, Madsen J, Ruoho A . Radioiodinated, photoactivatable phosphatidylcholine and phosphatidylserine: transfer properties and differential photoreactive interaction with human erythrocyte membrane proteins. Biochemistry. 1987; 26(7):1812-9. DOI: 10.1021/bi00381a004. View

Moscufo N, Gallina A, Schiavo G, Montecucco C, Tomasi M . Multiple lipid interactions of the Sendai virus fusogenic protein. J Biol Chem. 1987; 262(24):11490-6. View

Laemmli U . Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5. DOI: 10.1038/227680a0. View

10.

Scheid A, Choppin P . Two disulfide-linked polypeptide chains constitute the active F protein of paramyxoviruses. Virology. 1977; 80(1):54-66. DOI: 10.1016/0042-6822(77)90380-4. View

11.

Peterson G . A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal Biochem. 1977; 83(2):346-56. DOI: 10.1016/0003-2697(77)90043-4. View

12.

Markwell M, Fox C . Protein-protein interactions within paramyxoviruses identified by native disulfide bonding or reversible chemical cross-linking. J Virol. 1980; 33(1):152-66. PMC: 288533. DOI: 10.1128/JVI.33.1.152-166.1980. View

13.

Boggs J, Stollery J, Moscarello M . Effect of lipid environment on the motion of a spin-label covalently bound to myelin basic protein. Biochemistry. 1980; 19(6):1226-34. DOI: 10.1021/bi00547a029. View

14.

Choppin P, Scheid A . The role of viral glycoproteins in adsorption, penetration, and pathogenicity of viruses. Rev Infect Dis. 1980; 2(1):40-61. DOI: 10.1093/clinids/2.1.40. View

15.

Hsu M, Scheid A, Choppin P . Activation of the Sendai virus fusion protein (f) involves a conformational change with exposure of a new hydrophobic region. J Biol Chem. 1981; 256(7):3557-63. View

16.

Brunner J, Semenza G . Selective labeling of the hydrophobic core of membranes with 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine, a carbene-generating reagent. Biochemistry. 1981; 20(25):7174-82. DOI: 10.1021/bi00528a019. View

17.

Lee P, Cherry R, Bachi T . Correlation of rotational mobility and flexibility of Sendai virus spike glycoproteins with fusion activity. Virology. 1983; 128(1):65-76. DOI: 10.1016/0042-6822(83)90319-7. View

18.

White J, Kielian M, Helenius A . Membrane fusion proteins of enveloped animal viruses. Q Rev Biophys. 1983; 16(2):151-95. DOI: 10.1017/s0033583500005072. View

19.

Eidelman O, Schlegel R, Tralka T, Blumenthal R . pH-dependent fusion induced by vesicular stomatitis virus glycoprotein reconstituted into phospholipid vesicles. J Biol Chem. 1984; 259(7):4622-8. View

20.

Hoekstra D, de Boer T, Klappe K, Wilschut J . Fluorescence method for measuring the kinetics of fusion between biological membranes. Biochemistry. 1984; 23(24):5675-81. DOI: 10.1021/bi00319a002. View