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Science 14 October 1994:
Vol. 266. no. 5183, pp. 274 - 276
DOI: 10.1126/science.7939662
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Articles

Science, Vol 266, Issue 5183, 274-276
Copyright © 1994 by American Association for the Advancement of Science

articles

Insertion of a coiled-coil peptide from influenza virus hemagglutinin into membranes

YG Yu, DS King, and YK Shin

Department of Chemistry, University of California, Berkeley.

The trimeric protein hemagglutinin (HA) of the influenza viral envelope is essential for cell entry. To investigate the interaction of HA with membranes, two 40-residue, cysteine-substituted peptides comprising the loop region and the first part of the coiled-coil stem were synthesized and modified with a nitroxide spin label. Electron paramagnetic resonance analysis revealed that the peptide inserts reversibly into phospholipid vesicles under endosomal pH conditions. This result suggests that some or all of the long coiled-coil trimer of HA may insert into membranes, which could bring the viral and cell membranes closer together and facilitate fusion.


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