Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex

BMC Biology
Ding-Kwo ChangYu-Tsan Liu

Abstract

To study the organization and interaction with the fusion domain (or fusion peptide, FP) of the transmembrane domain (TMD) of influenza virus envelope glycoprotein for its role in membrane fusion which is also essential in the cellular trafficking of biomolecules and sperm-egg fusion. The fluorescence and gel electrophoresis experiments revealed a tight self-assembly of TMD in the model membrane. A weak but non-random interaction between TMD and FP in the membrane was found. In the complex, the central TMD oligomer was packed by FP in an antiparallel fashion. FP insertion into the membrane was altered by binding to TMD. An infrared study exhibited an enhanced membrane perturbation by the complex formation. A model was built to illustrate the role of TMD in the late stages of influenza virus-mediated membrane fusion reaction. The TMD oligomer anchors the fusion protein in the membrane with minimal destabilization to the membrane. Upon associating with FP, the complex exerts a synergistic effect on the membrane perturbation. This effect is likely to contribute to the complete membrane fusion during the late phase of fusion protein-induced fusion cascade. The results presented in the work characterize the nature of the interaction...Continue Reading

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Citations

Oct 30, 2012·Journal of Chemical Information and Modeling·Bruno L VictorCláudio M Soares
Feb 16, 2011·Proceedings of the National Academy of Sciences of the United States of America·Jason E DonaldWilliam F DeGrado
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Methods Mentioned

BETA
nuclear magnetic resonance
electrophoresis
FRET

Software Mentioned

Peakfit

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