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Volume10, Issue 12 (Suppl) J Proteomics Bioinform, an open access journal
ISSN: 0974-276X
Page 32
conferenceseries.com
World Biomarkers & Pharma Biotech 2017
December 07-09, 2017
December 07-09, 2017 | Madrid, Spain
&
20th International Conference on
PHARMACEUTICAL BIOTECHNOLOGY
9th WORLD BIOMARKERS CONGRESS
JOINT EVENT ON
Targeting viral membrane proteins in silico
Wolfgang B Fischer
National Yang-Ming University, Taiwan
Many viral membrane proteins interact withmembrane proteins of the host to steer the cell for a successful mass production
of novel virions. The viral proteins rely on selective interactions of their transmembrane domains (TMDs) with those of
the host protein. An understanding of the modalities of recognizing the proper host target, on the revers, can be turned against
the virus. Getting insights into the specificity of binding, the interaction of oncoprotein E5 of Human papillomavirus-16 (HPV-
16), an 83-amino acid membrane protein containing 3 TMDS, with a peptide corresponding to the fourth TMD (TMD4) of
the 16 kDa subunit of the ATP6V0C is investigated as an example. HPV-16 is the major cause of cervical cancer diagnosed
today. E5 is a membrane protein which is expressed at an early (hence the letter E) stage of the infectivity cycle when the virus
turns the cell malignant. The protein interacts with a series of host factors, but has also been identified experimentally to allow
channel activity when most likely in a hexameric assembled form. Computational modeling suggests a weak selectivity of the
channel. Docking approaches as well as coarse grained molecular dynamics (CGMD) simulations of the peptides within a
hydrated lipid membrane specify the mode of binding of TMD4 with either E5 protein or its individual TMDs. From potential
of mean force calculations (PMF) and statistical analysis enthalpy and entropy contributions are attributed of TMD4 binding
to TMD3 and TMD2 of E5, respectively.
Recent Publications:
1. Fischer W B, Li L-H, Mahato D R, Wang Y T and Chen C P (2014) Viral channel proteins in intracellular protein -
protein communication: Vpu of HIV-1, E5 of HPV16 and p7 of HCV. Biochim. Biophys. Acta. 1838:1113-1121.
2. Mahato D R and Fischer W B (2016) Weak selectivity predicted for modeled bundles of the viral channel forming
protein E5 of human papillomavirus-16. J. Phys. Chem. B. 120: 13076-13085.
3. Fischer W B, Kalita M M and Heermann D (2016) Viral Channel forming proteins - how to assemble and depolarize
lipid membranes in silico. Biochim. Biophys. Acta. 1858: 1710-1721.
Biography
Wolfgang B Fischer is Professor at the Institute of Biophotonics, School of Biomedical Science and Engineering, National Yang-Ming University, Taipei, Taiwan.
He has obtained his PhD in Chemistry at Heidelberg University, Germany, working in the field of vibrational spectroscopy in 1991. After years in the US, he
has completed his Postdoctoral, working on bacteriorhodopsin using vibrational spectroscopy in Boston University, Germany. Then he has worked in Analytical
Chemistry, working on ion channels as potential biosensors, UK (Oxford University as EU Marie Curie Research Fellow and later as Lecturer, working on viral
ion channels using bilayer recordings and molecular dynamics simulations. He has moved to Taiwan. The field of research is on biophysical aspects describing
dynamics and energetic of protein-protein interactions (PPIs) of membrane proteins. The focus is on the development of computational platform technologies to
support drug discovery and design as well as materials sciences.
Wolfgang B Fischer, J Proteomics Bioinform 2017, 10:12(Suppl)
DOI: 10.4172/0974-276X-C1-109