Transient domains induced by influenza haemagglutinin during membrane fusion

References

• Wilson I. A., Skehel J. J., Wiley D. C. Structure of the hemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature 1981; 289: 366–373
   PubMed Web of Science ®Google Scholar
• White J., Kielian M., Helenius A. Membrane fusion proteins of enveloped animal viruses. Quarterly Review of Biophysics 1983; 16: 151–195
   PubMed Web of Science ®Google Scholar
• Blumenthal R., Schoch C., Puri A., Clague M. J. A dissection of steps leading to viral envelope protein-mediated membrane fusion. Annals of the New York Academy of Sciences 1991; 635: 285–296
   PubMed Web of Science ®Google Scholar
• Clague M. J., Schoch C., Blumenthal R. Delay time for influenza hemagglutinin-induced membrane fusion depends on the hemagglutinin surface density. Journal of Virology 1991; 65: 2402–2407
   PubMed Web of Science ®Google Scholar
• Schoch C., Blumenthal R. Role of the fusion peptide sequence in initial stages of influenza hemagglutinin-induced cell fusion. Journal of Biological Chemistry 1993; 268: 9267–9274
   PubMed Web of Science ®Google Scholar
• Lowy R. J., Sarkar D. P., Chen Y., Blumenthal R. Observation of single influenza virus-cell fusion and measurement by fluorescence video microsopy. Proceedings of the National Academy of Sciences, USA 1990; 87: 1850–1854
   PubMed Web of Science ®Google Scholar
• Sarkar D. P., Morris S. J., Eidelman O., Zimerberg J., Blumenthal R. Initial stages of influenza hemagglutinin-induced cell fusion monitored simultaneously by two fluorescent events: cytoplasmic continuity and lipid mixing. Journal of Cell Biology 1989; 109: 113–122
   PubMed Web of Science ®Google Scholar
• Kaplan D., Zimmerberg J., Puri A., Sarkar D. P., Blumenthal R. Single cell fusion events induced by influenza hemagglutinin: studies with rapid-flow, quantitative fluorescence microscopy. Experimental Cell Research 1991; 195: 137–144
   PubMed Web of Science ®Google Scholar
• Aimers W., Tse F. W. Transmitter release from synapses: does a preassembled fusion pore initiate exocytosis. Neuron 1990; 4: 813–818
   PubMedGoogle Scholar
• Zimmerberg J., Curran M., Cohen F. S. A lipid/protein hypothesis for exocytotic fusion pore formation. Annals of the New York Academy of Sciences 1991; 635: 307–317
   PubMed Web of Science ®Google Scholar
• Monck J. R., Fernandez J. M. The exocytotic fusion pore. Journal of Cell Biology 1992; 119: 1395–1404
   PubMed Web of Science ®Google Scholar
• Aloia R. C., Curtain C. C. Advances in Membrane Fluidity. Wiley-Liss, New York 1992; Vol. 6: 283–303
   Google Scholar
• Bukrinskaya Molotkovsky A. G., Vodovozova E. L, Manevich Y. M., Bergelson L. D. The molecular organization of the influenza virus surface. Studies using photoreactive and fluorescent labeled phospholipid probes. Biochemica et Biophysica Acta 1987; 897: 285–292
   PubMedGoogle Scholar
• Slepushkin V. A., Starov A. I., Bukrinksaya A. G., Imbs A. M., Martynova M. A., Kogtev L. S., Vodovozova E., Timofeeva N. G., Molotkovsky J. G., Bergelson L. D. Interaction of influenza virus with gangliosides and liposomes containing gangliosides. European Journal of Biochemistry 1988; 173: 599–605
   PubMedGoogle Scholar
• Wiley D. C., Skehel J. J. The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annual Review of Biochemistry 1987; 563: 365–394
   Google Scholar
• Stegmann T., Booy F. P., Wilschut J. Effects of low pH on influenza virus. Activation and inactivation of the membrane fusion capacity of the hemagglutinin. Journal of Biological Chemistry 1987; 262: 17744–17749
   PubMed Web of Science ®Google Scholar
• White J. M., Wilson I. A. Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin. Journal of Cell Biology 1987; 56: 365–394
   Google Scholar
• Guy H. R., Durell S. R., Schoch C., Blumenthal R. Analyzing the fusion process influenza hemagglutinin by mutagenesis and molecular modeling. Biophysical Journal 1992; 62: 113–115
   Google Scholar
• Ruigrok R. W., Hewat E. A., Wade R. H. Low pH deforms the influenza virus envelope. Journal of General Virology 1992; 73: 995–998
   PubMedGoogle Scholar
• Junankar P. R., Cherry R. J. Temperature and pH dependence of the haemolytic activity of influenza virus and of the rotational mobility of the spike glycoproteins. Biochimica et Biophysica Acta 1986; 854: 198–206
   PubMedGoogle Scholar
• Aroeti B., Jovin T. M., Henis Y. I. Rotational mobility of Sendai virus glycoproteins in membranes of fused human erythrocytes and in the envelopes of cell-bound virions. Biochemistry 1990; 29: 9119–9125
   PubMedGoogle Scholar
• Lowry R. J., Sarkar D. P., Whitnall M. H., Blumenthal R. Differences in dispersion of influenza virus lipids and proteins during fusion. Experimental Cell Research 1995, in press
   Google Scholar
• Morris S. J., Sarkar D. P., White J. M., Blumenthal R. Kinetics of pH-dependent fusion between 3T3 fibroblasts expressing influenza hemagglutinin and red blood cells. Journal of Biological Chemistry 1989; 264: 3972–3978
   PubMed Web of Science ®Google Scholar
• Henis Y. I., Herman-Barhom B., Aroeti B., Gutman O. Lateral mobility of both envelope proteins (F and HN) of Sendai virus in the cell membrane is essential for cell-cell fusion. Journal of Biological Chemistry 1989; 264: 17119–17125
   PubMedGoogle Scholar
• Aroeti B., Henis Y. I. Accumulation of Sendai virus glycoprotein in cell-cell contact regions and its role in cell fusion. Journal of Biological Chemistry 1991; 266: 15845–15849
   PubMedGoogle Scholar
• Pak C. C., Krumbiegel M., Blumenthal R., Raviv Y. Detection of influenza hemagglutinin interaction with biological membranes by photosensitized activation of [125I]iodonaphthyl-azide. Journal of Biological Chemistry 1994; 269: 14614–14619
   PubMed Web of Science ®Google Scholar
• Raviv Y., Bercovici T., Gitler C., Salomon Y. Detection of nearest neighbors to specific fluorescently tagged ligands in the rod outer segment and lymphocyte plasma membranes by photosensitization of 5-iodonaphthyl-azid. Biochemistry 1989; 28: 1313–1319
   PubMedGoogle Scholar
• Raviv Y., Pollard H. B., Bruggemann E. P., Pastan I., Gottesman M. M. Photosensitized labeling of a functional multidrug transporter in living drug-resistant tumor cells. Journal of Biological Chemistry 1990; 265: 3975–3980
   PubMed Web of Science ®Google Scholar
• Eidelman O., Cabantchik Z. I. Fluorescence methods for continuous monitoring of transport in cells and vesicles. Methods in Enzymology 1989; 172: 122–135
   PubMedGoogle Scholar
• Anderson R. G., Kamen B. A., Rothberg K. G., Lacey S. W. Potocytosis: sequestration and transport of small molecules by caveolae. Science 1992; 255: 410–411
   PubMed Web of Science ®Google Scholar
• Spruce A. E., Iwata A., White J. M., Aimers W. Patch clamp studies of single cell-fusion events mediated by a viral fusion protein. Nature 1989; 342: 555–558
   PubMed Web of Science ®Google Scholar
• Tse F. W., Iwata A., Aimers W. Membrane flux through the pore formed by a fusogenic viral envelope protein during cell fusion. Journal of Cell Biology 1993; 121: 543–552
   PubMed Web of Science ®Google Scholar
• Zimmerberg J., Blumenthal R., Sarker D. P., Curran M., Morris S. J. Restricted movement of lipid and aqueous dyes through pores formed by influenza hemagglutinin during cell fusion. Journal of Cell Biology 1995, in press
   Google Scholar
• Morris S. J., Zimmerberg J., Sarker D. P., Blumenthal R. Kinetics of cell fusion mediated by viral spike glycoproteins. Methods in Enzymology 1993; 221: 42–58
   PubMed Web of Science ®Google Scholar
• Morris S. J., Wiegmann T. B., Welling L. W., Chronwall B. M. Rapid simultaneous estimation of intracellular calcium and pH. Methods in Cell Biology 1994; 40: 666–777
   Google Scholar
• Song L, Ahkong Q. F., Georgescauld G., Lucy J. A. Membrane fusion without cytoplasmic fusion (hemi-fusion) in erythrocytes that are subjected to electrical breakdown. Biochimica et Biophysica Acta 1991; 1065: 54–62
   PubMed Web of Science ®Google Scholar
• Kemble G. W., Danieli T., White J. M. Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion. Cell 1994; 76: 383–391
   PubMed Web of Science ®Google Scholar
• Stegmann T., Delfino J. M., Richards F. M., Helenius A. The HA2 subunit of influenza hemagglutinin inserts into the target membrane prior to fusion. Journal of Biological Chemistry 1991; 266: 18404–18410
   PubMed Web of Science ®Google Scholar
• Chandler D. E., Heuser J. E. Membrane fusion during secretion. Cortical granule exocytosis in sea urchin eggs as studied by quick freezing and freeze-fracture. Journal of Cell Biology 1979; 83: 91–108
   PubMed Web of Science ®Google Scholar
• Bergelson L. D., Molotkovsky J. G., Manevich Y. M. Lipid-specific fluorescent probes in studies of biological membranes. Chemistry and Physics of Lipids 1985; 37: 165–195
   PubMedGoogle Scholar
• Harter C., James P., Bachi T., Semenza G., Brunner J. Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the ‘fusion peptide’. Journal of Biological Chemistry 1989; 264: 6459–6464
   PubMed Web of Science ®Google Scholar