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Abstract
The icosahedral Polio virus capsid consists of 60 copies of each of the coat proteins VP1, VP2, VP3 and myristolyated VP4 (myrVP4). Catalyzed by the host cell receptor the Polio virus enters the host cell via externalization of myrVP4 and the N terminal part of VP1. There are several assumptions about the individual role of both of the proteins in the mechanism of membrane attachment and genome injection. We use the first 32 N terminal amino acids of VP1 and applied molecular dynamics simulations to assess its mechanism of function when attached and inserted into hydrated lipid membranes (POPC). Helical models are placed in various positions in regard to the lipid membrane to start with. As a comparison, the first 33 amino acids of the fusion peptide of gp41 of HIV-1 are simulated under identical conditions. Computational data support the idea that VP1 is not penetrating into the membrane to form a pore; it rather lays on the membrane surface and only perturbs the membrane. Furthermore, this idea is strengthened by channel recordings of both peptides showing irregular openings.
Acknowledgements
We thank Yechiel Shai (Rehovot, IL, USA) for valuable discussions and critically reading the manuscript. WBF thanks the NYMU and the government of Taiwan for financial support (Aim of Excellence Program) and the National Center for High-Performance Computing for providing computer time. This work was supported by the National Science Council (NSC) of Taiwan (NSC98-2112-M-010-002-MY3). JK acknowledges a fellowship granted by the Alexander von Humboldt-Foundation and the NSC. CPC acknowledges a fellowship of the DAAD and a Taiwan-German Scholarship.
Declaration of interest: The authors report no conflicts of interest. The authors alone are responsible for the content and writing of the paper.