Selected article for: "cell surface and low ph"
Author: Qiao, Hui; Pelletier, Sandra L.; Hoffman, Lucas; Hacker, Jill; Armstrong, R. Todd; White, Judith M.
Title: Specific Single or Double Proline Substitutions in the “Spring-loaded” Coiled-Coil Region of the Influenza Hemagglutinin Impair or Abolish Membrane Fusion Activity
  • Document date: 1998_6_15
    • ID: 78fjem8s_28
    Snippet: In this study, we asked two questions. Is the spring-loaded conformational change in the influenza virus HA, the loop to helix transition of HA2 residues 55-76, required for fusion, and if so, for what stage of the process? Formally, the spring-loaded conformational change could be required for hemifusion, the mixing of the outer leaflet lipids, or for full fusion, the mixing of aqueous contents. Alternatively, it might lead to a postfusion confo.....
    Document: In this study, we asked two questions. Is the spring-loaded conformational change in the influenza virus HA, the loop to helix transition of HA2 residues 55-76, required for fusion, and if so, for what stage of the process? Formally, the spring-loaded conformational change could be required for hemifusion, the mixing of the outer leaflet lipids, or for full fusion, the mixing of aqueous contents. Alternatively, it might lead to a postfusion conformation. We addressed these questions by analyzing nine single and one double point mutant in HA2 54-81, the region of high coiled-coil propensity (Ward and Dopheide, 1980; Carr and Kim, 1993) . We then assessed the effects of each mutation on structural features and cell surface expression of HA, on its ability to undergo low pH-induced conformational changes, and on its ability to mediate membrane fusion.

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