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The Journal of Membrane Biology

, Volume 252, Issue 4–5, pp 261–272 | Cite as

Membrane Composition Modulates Fusion by Altering Membrane Properties and Fusion Peptide Structure

  • Geetanjali Meher
  • Hirak ChakrabortyEmail author
Article
Part of the following topical collections:
  1. Membrane and Receptor Dynamics

Abstract

Membrane fusion, one of the most essential processes in the life of eukaryotes, occurs when two separate lipid bilayers merge into a continuous bilayer and internal contents of two separated membranes mingle. There is a certain class of proteins that assist the binding of the viral envelope to the target host cell and catalyzing fusion. All class I viral fusion proteins contain a highly conserved 20–25 amino-acid amphipathic peptide at the N-terminus, which is essential for fusion activity and is termed as the ‘fusion peptide’. It has been shown that insertion of fusion peptides into the host membrane and the perturbation in the membrane generated thereby is crucial for membrane fusion. Significant efforts have been given in the last couple of decades to understand the lipid-dependence of structure and function of the fusion peptide in membranes to understand the role of lipid compositions in membrane fusion. In addition, the lipid compositions further change the membrane physical properties and alter the mechanism and extent of membrane fusion. Therefore, lipid compositions modulate membrane fusion by changing membrane physical properties and altering structure of the fusion peptide.

Keywords

Membrane fusion Fusion peptide Non-lamellar intermediate Lipid composition 

Notes

Acknowledgement

This work was supported by research grant from Science and Engineering Research Board, Department of Science and Technology (SERB-DST), New Delhi (File No. ECR/2015/000195). H. C. and G. M. thank the University Grants Commission for UGC-Assistant Professor position and UGC-BSR Research Fellowship, respectively. We acknowledge Department of Science and Technology, New Delhi, and UGC for providing instrument facility to the School of Chemistry, Sambalpur University under the FIST and DRS programs, respectively. We gratefully acknowledge the critical comments and discussions by Dr. S. N. Sahu and the members of Chakraborty laboratory.

Compliance with Ethical Standards

Conflict of interest

The authors declare that there is no conflict of interest.

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Authors and Affiliations

  1. 1.School of ChemistrySambalpur UniversityBurlaIndia

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