First Look: FIBONACCI-Numbers and LUCAS-Numbers and Ebola Virus (Orthoebolavirus): A Very Reasonable Fit

First Look: FIBONACCI-Numbers and LUCAS-Numbers and Ebola Virus (Orthoebolavirus): A Very Reasonable Fit
by Stefan Geier

The mumber of relevant genes and proteins (3′-NP-VP35-VP40-GP-VP30-VP24-L-5′) of Ebola Virus (Orthoebolavirus) is seven. 7 is the 4th Lucas number L(4). Further studies would be very relevant.

The first Fibonacci-numbers and Lucas-numbers:

Fibonacci F(n): 0, 1, 1, 2, 3, 5, 8, 13, 21, 34, 55, ...
Lucas L(n): 2, 1, 3, 4, 7, 11, 18, 29, 47, 76, 123, ...

The above provides an at least very reasonable association of the Ebola Virus (Orthoebolavirus) with the GEIER programme based on GEIER's Equations and FIBOBACCI-Numbers and LUCAS-Numbers.

In addition, the surface Ebola virus (EBOV) trimeric glycoprotein (GP) spike shows trimerous structure similar to 3-merous flowers fitting F(4) as well as L(2). (Please, compare with the tetramerous structure of hantavirus spikes; https://humanistischebetrachtungen1.blogspot.com/2026/05/first-look-fibobacci-numbers-and-lucas.html.)
Furthermore, an angle of 18° between the planes of viral and endosomal membranes fits GEIER's 6°xn Rule with n=3 (see below).

Evidence:
1. Wikipedia https://de.wikipedia.org/wiki/Orthoebolavirus


Wikipedia today:
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
Sourcehttps://www.mdpi.com/1422-0067/20/18/4657/htm
AuthorMadiiha 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 11Å 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  - 
 


Yours sincerely,
Stefan Geier
Gerhart-Hauptmann-Str.6
83071 Haidholzen, Germany

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