Piron vs Porin Proteins

prion proteinaceous infectious particle

porin alphaproteobacteria intracellular endosymbiont

DNA/DDS
DNA Digital Data Storage
Synthetic DNA Genomics
Caulobacter Crescentus
Alphaproteobacteria

Nanopore
Nanopore Sequencing
Beta Barrel
Porin Protein
Mycobacterial Porin

Porin (Protein)

Sixteen- or eighteen-stranded up-and-down beta barrel structures occur in porins, which function as transporters for ions and small molecules that cannot diffuse across a cellular membrane. Such structures appear in the outer membranes of gram-negative bacteria, chloroplast, and mitochondria. The central pore of the protein, sometimes known as the eyelet, is lined with charged residues arranged so that the positive and negative charges appear on opposite sides of the pore. A long loop between two beta strands partially occludes the central channel; the exact size and conformation of the loop helps in discriminating between molecules passing through the transporter.

Preprotein Translocases

Beta barrels also function within endosymbiont derived organelles such as mitochondria and chloroplast to transport proteins. Within the mitochondrion two complexes exist with beta barrels serving as the pore forming subunit, Tom40 of the Translocase of the outer membrane, and Sam50 of the Sorting and assembly machinery. The chloroplast also has functionally similar beta barrel containing complexes, the best characterised of which is Toc75 of the TOC complex (Translocon at the outer envelope membrane of chloroplast).

Lipocalin

Lipocalins are typically eight-stranded up-and-down beta barrel proteins that are secreted into the extracellular environment. A distinctive feature is their ability to bind and transport small hydrophobic molecules in the barrel calyx. Examples of the family include retinol binding proteins (RBPs) and major urinary proteins (Mups). RBP binds and transports retinol (vitamin A), while Mups bind a number of small, organic pheromones, including 2-sec-butyl-4,5-dihydrothiazole (abbreviated as SBT or DHT), 6-hydroxy-6-methyl-3-heptanone (HMH) and 2,3 dihydro-exo-brevicomin (DHB).

..

Hacking the host: exploitation of macrophage polarization by intracellular bacterial pathogens

https://academic.oup.com/femspd/article/78/1/ftaa009/5739920?login=false

..

Bioelectric batteries using Graphene, synthetic DNA & biological computers, is made by synthetic Alphaproteobacteria.

DNA Digital Data Storage
Synthetic DNA Genomics
Caulobacter Crescentus
Alphaproteobacteria

they are manufacturing exotic or synthetic minimal genome extremophile bacteria to hack cellular functions, making synthetic messenger RNA/DNA spike proteins.

Antiparasitic Drugs that utilize Ionophore Metallation of Electron Bonding should have no effect on a virus, unless it was a parasite.

..

request the identification of Alphaproteobacteria Endosymbionts, specifically Vent Tube Worm, or any Exotic Extremophile variants.

also check for Mycoplasma Incognitus or Laboratorium, both can be classified as Stealth Pathogen & Minimal Genome.

the concern is that Alphaproteobacteria Endosymbionts can infect both Cell Nucleus & Mitochondria, and Mycoplasma as Bacteriophage.

acting in conjunction as Russian Dolls, the Mycoplasma offers the membrane for Endosymbiont.

misfolding proteins & reprogramming cellular Messenger RNA/DNA.

..

MT-RNR2

MT-RNR2 gene also encodes the Humanin polypeptide that has been the target of Alzheimer's disease research.

https://en.m.wikipedia.org/wiki/MT-RNR2

https://en.m.wikipedia.org/wiki/16S_ribosomal_RNA

..

New rRNA Gene-Based Phylogenies of the Alphaproteobacteria Provide Perspective on Major Groups, Mitochondrial Ancestry and Phylogenetic
Instability

Bacteria in the class Alphaproteobacteria have a wide variety of lifestyles and physiologies. They include pathogens
of humans and livestock, agriculturally valuable strains, and several highly abundant marine groups. The ancestor of
mitochondria also originated in this clade. Despite significant effort to investigate the phylogeny of the Alphaproteobacteria with a variety of methods, there remains considerable disparity in the placement of several groups. Recent emphasis on phylogenies derived from multiple protein-coding genes remains contentious due to
disagreement over appropriate gene selection and the potential influences of systematic error.

The key nodes in the alphaproteobacterial tree, such as the branch leading to modern mitochondria, are very ancient (dating 2 billion years ago). We chose to revisit the debate over alphaproteobacterial phylogeny using rRNA
genes. Being universally conserved and under strong structural
and functional constraints, we assert that the rRNA genes are ideal for shedding light on the relationships between the major groups. The 16S rRNA gene remains the gold standard for microbial taxonomy and current ecological studies depend on classifying organisms based on this marker.