Detection of influenza hemagglutinin interaction with biological membranes by photosensitized activation of [125I]iodonaphthylazide - PubMed (original) (raw)
. 1994 May 20;269(20):14614-9.
Affiliations
- PMID: 8182068
Free article
Detection of influenza hemagglutinin interaction with biological membranes by photosensitized activation of [125I]iodonaphthylazide
C C Pak et al. J Biol Chem. 1994.
Free article
Abstract
Fusion of influenza virus with cells is triggered by a pH-dependent conformational change in the viral envelope protein, hemagglutinin, which results in exposure of the fusion peptide and its insertion into the target membrane. We have investigated the association of hemagglutinin with erythrocyte membranes by photosensitized labeling with [125I]iodonaphthylazide. This technique relies on the collisional energy transfer from a photosensitizing chromophore to [125I]iodonaphthylazide, which selectively labels proteins in the vicinity of the chromophore. Incubation of influenza virus with erythrocyte membranes containing chromophore and [125I]iodonaphthylazide results in labeling of hemagglutinin under fusogenic conditions (pH 5 and 37 degrees C). We also examined photosensitized labeling of hemagglutinin upon incubation of the X31 strain of influenza virus with labeled erythrocyte membranes in a pre-fusion state (pH 5 and 4 degrees C). There was little hemagglutinin labeling under these conditions, although incubation of bromelain-cleaved hemagglutinin, which lacks the transmembrane region, resulted in rapid labeling. Hemagglutinin was also labeled by [125I]iodonaphthylazide photosensitized by a fluorescent substrate transported through the erythrocyte band 3 sialoglycoprotein. Hemagglutinin labeling decreased after an initial rapid rise, suggesting that the fusion site is close to the sialoglycoprotein and that [125I]iodonaphthylazide photosensitized labeling may be used to assay protein movement during fusion.
Similar articles
- Evidence for H(+)-induced insertion of influenza hemagglutinin HA2 N-terminal segment into viral membrane.
Weber T, Paesold G, Galli C, Mischler R, Semenza G, Brunner J. Weber T, et al. J Biol Chem. 1994 Jul 15;269(28):18353-8. J Biol Chem. 1994. PMID: 8034580 - Structural characterization of viral fusion proteins.
Hughson FM. Hughson FM. Curr Biol. 1995 Mar 1;5(3):265-74. doi: 10.1016/s0960-9822(95)00057-1. Curr Biol. 1995. PMID: 7780737 Review. - Mechanisms of membrane fusion.
Zimmerberg J, Vogel SS, Chernomordik LV. Zimmerberg J, et al. Annu Rev Biophys Biomol Struct. 1993;22:433-66. doi: 10.1146/annurev.bb.22.060193.002245. Annu Rev Biophys Biomol Struct. 1993. PMID: 8347997 Review. No abstract available.
Cited by
- Characterization of the effects of aryl-azido compounds and UVA irradiation on the viral proteins and infectivity of human immunodeficiency virus type 1.
Belanger JM, Raviv Y, Viard M, Jason de la Cruz M, Nagashima K, Blumenthal R. Belanger JM, et al. Photochem Photobiol. 2010 Sep-Oct;86(5):1099-108. doi: 10.1111/j.1751-1097.2010.00780.x. Photochem Photobiol. 2010. PMID: 20630026 Free PMC article. - Photo-activation of the hydrophobic probe iodonaphthylazide in cells alters membrane protein function leading to cell death.
Viard M, Garg H, Blumenthal R, Raviv Y. Viard M, et al. BMC Cell Biol. 2009 Mar 26;10:21. doi: 10.1186/1471-2121-10-21. BMC Cell Biol. 2009. PMID: 19323821 Free PMC article. - Hydrophobic inactivation of influenza viruses confers preservation of viral structure with enhanced immunogenicity.
Raviv Y, Blumenthal R, Tompkins SM, Humberd J, Hogan RJ, Viard M. Raviv Y, et al. J Virol. 2008 May;82(9):4612-9. doi: 10.1128/JVI.02233-07. Epub 2008 Feb 27. J Virol. 2008. PMID: 18305038 Free PMC article. - HIV-1 envelope glycoprotein-mediated fusion and pathogenesis: implications for therapy and vaccine development.
Jacobs A, Garg H, Viard M, Raviv Y, Puri A, Blumenthal R. Jacobs A, et al. Vaccine. 2008 Jun 6;26(24):3026-35. doi: 10.1016/j.vaccine.2007.12.026. Epub 2008 Jan 10. Vaccine. 2008. PMID: 18242797 Free PMC article. - Photoinduced reactivity of the HIV-1 envelope glycoprotein with a membrane-embedded probe reveals insertion of portions of the HIV-1 Gp41 cytoplasmic tail into the viral membrane.
Viard M, Ablan SD, Zhou M, Veenstra TD, Freed EO, Raviv Y, Blumenthal R. Viard M, et al. Biochemistry. 2008 Feb 19;47(7):1977-83. doi: 10.1021/bi701920f. Epub 2008 Jan 17. Biochemistry. 2008. PMID: 18198900 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources