First Look: FIBONACCI-Numbers and LUCAS-Numbers and Ebola Virus (Orthoebolavirus): A Very Reasonable Fit
The first Fibonacci-numbers and Lucas-numbers:
1. Wikipedia https://de.wikipedia.org/wiki/Orthoebolavirus
| Description | English: (A) Schematic representation of mature Ebola virion consisting of two main components—the nucleocapsid and envelope. The matrix comprising the virion proteins VP24 and VP40 is located between the nucleocapsid and envelope. Glycoprotein (GP) spikes are located on the surface of the envelope (B) The genome contains 7 genes which encode the six structural proteins and one non-structural protein [79]. The gene order is 5′-NTR-NP (nucleoprotein)-VP35-VP40 (Major matrix protein)-GP/sGP (Glycoprotein)-VP30-VP24 (Minor matrix protein)-RNA-dependent RNA polymerase (l)-3′-NTR [80]. |
| Date | |
| Source | https://www.mdpi.com/1422-0067/20/18/4657/htm |
| Author | Madiiha Bibi Mandary, Malihe Masomian, and Chit Laa Pooh |
Figure 4 by
TY - JOUR
AU - Beniac, Daniel R.
AU - Booth, Timothy F.
PY - 2017
DA - 2017/04/11
TI - Structure of the Ebola virus
glycoprotein spike within the virion envelope at 11 Å resolution
JO - Scientific Reports
SP - 46374
VL - 7
IS - 1
AB - We present the structure of the
surface Ebola virus (EBOV) trimeric glycoprotein (GP) spike at 11 Å resolution, in situ within the viral plasma
membrane of purified virus particles. GP functions in cellular attachment,
endosomal entry, and membrane fusion to initiate infection, and is a key
therapeutic target. Nevertheless, only about half of the GP molecule has yet
been solved to atomic resolution, excluding the mucin-like and transmembrane
domains, and some of the glycans. Fitting of the atomic resolution X-ray data
from expressed, truncated deletion constructs within our 11 Å structure of the entire molecule
demonstrates the relationship between the GP1-GP2 domains, the mucin-like and
transmembrane domains, and the bilaminar lipid envelope. We show that the
mucin-like domain covers the glycan cap and partially occludes the receptor
binding sites prior to proteolytic cleavage. Our structure is also consistent
with key antibody neutralisation sites on GP being accessible prior to
proteolysis. Based on the findings of us and others, GP-mediated binding may
create an angle of 18 degrees between the planes of viral and endosomal
membranes.
SN - 2045-2322
UR -
https://doi.org/10.1038/srep46374
DO - 10.1038/srep46374
ID - Beniac2017
ER -
Kommentare
Kommentar veröffentlichen