Doxycycline stops Prion Protein Infections

Topics with scientific, medical or general health related information and discussion that is not specifically related to Lyme disease.
Pandora
Posts: 252
Joined: Tue 20 Mar 2012 14:58

Re: Doxycycline stops Prion Protein Infections

Post by Pandora » Thu 20 Feb 2014 0:35

Vaccine damaged kids.----------Syndrome sufferers and Morgellons sufferers-----
Exogenous amyloidogenic proteins function as seeds in amyloid β-protein aggregation
April 2014
Kenjiro Ono | Ryoichi Takahashi | Tokuhei Ikeda | Mineyuki Mizuguchi | Tsuyoshi Hamaguchi | Masahito Yamada

Abstract: Amyloid β-protein (Aβ) aggregation is considered to be a critical step in the neurodegeneration of Alzheimer's disease (AD).

In addition to Aβ, many proteins aggregate into the amyloid state,

in which they form elongated fibers with spines comprising stranded β-sheets.

However, the cross-seeding effects of other protein aggregates on Aβ aggregation pathways are not completely clear. To investigate the cross-seeding effects of exogenous and human non-CNS amyloidogenic proteins on Aβ aggregation pathways, we examined whether and how sonicated fibrils of casein, fibroin, sericin, actin, and islet amyloid polypeptide affected Aβ40 and Aβ42 aggregation pathways using the thioflavin T assay and electron microscopy.

Interestingly, the fibrillar seeds of all amyloidogenic proteins functioned as seeds.

The cross-seeding effect of actin was stronger but that of fibroin was weaker than that of other proteins.

Furthermore, our nuclear magnetic resonance spectroscopic studies identified the binding sites of Aβ with the amyloidogenic proteins.

Our results indicate that the amyloidogenic proteins,

+++including those contained in foods and cosmetics,+++

contribute to Aβ aggregation by binding to Aβ, suggesting their possible roles in the propagation of Aβ amyloidosis.
http://www.sciencedirect.com/science/ar ... 3914000064
-----------
By expressing carboxypeptidase Y (CPY; an enzyme localized at the vacuoles), as an EGFP (Enhanced Green Fluorescenct Protein) fusion protein

in Aspergillus oryzae, we succeeded in visualizing the vacuoles (Fig.1).

Many vacuoles were located even in the conidia suggesting that vacuoles play a certain role in conidium.

Moreover, we found out that in addition to the spherical shape,

sometimes vacuole has a tubular shape or ring-like shape

peculiar to filamentous fungi.
http://park.itc.u-tokyo.ac.jp/Lab_Micro ... ole-E.html
------------
Spirochetal/Fungal recombinations. What is OspA used in vaccines--GMO--Makeup's and skin products?
http://www.morgellons-research.org/morg ... oscop3.htm

Stealth Infected Parasites
http://www.lymeneteurope.org/forum/view ... 246#p36246

admin
Site Admin
Posts: 342
Joined: Wed 25 Jul 2007 21:06

Re: Doxycycline stops Prion Protein Infections

Post by admin » Mon 24 Feb 2014 14:13

Pandora wrote:Spirochetal/Fungal recombinations. What is OspA used in vaccines--GMO--Makeup's and skin products?
http://www.morgellons-research.org/morg ... oscop3.htm
That website is not an acceptable reference here in the "Science"-section.

As a general rule the references should be medical science publications which can be found in PubMed, or articles about (e.g. news article) and/or supported by such publications.

Pandora
Posts: 252
Joined: Tue 20 Mar 2012 14:58

Re: Doxycycline stops Prion Protein Infections

Post by Pandora » Mon 24 Feb 2014 23:42

Since when is MORGELLONS SPIROCHETAL DISEASE not in the science section?

Let us know WHEN THE RECOMBINATIONS OF SPIROCHETAL OSP'S IS GOING TO BE INCLUDED IN THE SCIENCE SECTION?

Biophysical and morphological studies on the dual interaction of non-octarepeat prion protein peptides with copper and nucleic acids.
http://www.ncbi.nlm.nih.gov/pubmed/24557708
J Biol Inorg Chem. 2014 Feb 21. [Epub ahead of print]

Chaves JA1, Sanchez-López C, Gomes MP, Sisnande T, Macedo B, de Oliveira VE, Braga CA, Rangel LP, Silva JL, Quintanar L, Cordeiro Y.
Author information
Abstract

Conversion of prion protein (PrP) to an altered conformer,

the scrapie PrP (PrPSc), is a critical step in the development of transmissible spongiform encephalopathies. Both Cu(II) and nucleic acid molecules have been implicated in this conversion.

Full-length PrP can bind up to six copper ions;

four Cu(II) binding sites are located in the octarepeat domain (residues 60-91), and His-96 and His-111 coordinate two additional copper ions.

Experimental evidence shows that PrP binds different molecules,

resulting in diverse cellular signaling events.

However, there is little information about the interaction of macromolecular ligands with Cu(II)-bound PrP.

++++++++++Both RNA and DNA sequences can bind PrP,+++++++++++++++++

and this interaction results in reciprocal conformational changes.

Here, we investigated the interaction of Cu(II) and nucleic acids with amyloidogenic non-octarepeat PrP peptide models (comprising human PrP residues 106-126 and hamster PrP residues 109-149) that retain His-111 as the copper-anchoring residue.

The effect of Cu(II) and DNA or RNA sequences in the aggregation, conformation, and toxicity of PrP domains was investigated at low and neutral pH.

++++++++++Circular dichroism and EPR spectroscopy data++++++++++ indicate that interaction of the PrP peptides with Cu(II) and DNA occurs at pH 7.

This dual interaction +++++++++++induces conformational changes in the peptides, modulating their aggregation, and affecting the morphology of the aggregated species,+++++++++++++++++++

resulting in different cytotoxic effects. These results provide new insights into the role of Cu(II) and nucleic acid sequences in the structural conversion and aggregation of PrP, which are both critical events related to prion pathogenesis.
----------------------
It is cross species aggregation and gross morphologies that result.....What it looks like growing in us....
http://www.morgellons-research.org/.../morgellons...

And its NOT just growing in our skin--BUT ALSO OUR GUTS, AND BRAINS-----Its WHY all the Autism babies and people suffering lies of SYNDROMES cannot tolerate junk gene GMO gluten grains.
http://www.lymeneteurope.org/forum/viewtopic.php?f=6...

AND YOU SAY THIS IS NOT SCIENCE? THEN WHAT IS IT? I CAN PRODUCE AN EXIT IN ALL SUFFERING THEIR SYNDROMES. IS THAT NOW NOT SCIENCE? DO YOU CONCLUDE THE RESEARCH IS JUST LYING TO US?
The case for involvement of spiroplasma in the pathogenesis of transmissible spongiform encephalopathies.

http://www.ncbi.nlm.nih.gov/pubmed/24423635
J Neuropathol Exp Neurol. 2014 Feb;73(2):104-14. doi: 10.1097/NEN.0000000000000033.

Bastian FO.
Author information
Abstract
Spiroplasma biofilm formation explains the role of these +++++++wall-less bacteria+++++++++ in the pathogenesis of transmissible spongiform encephalopathies (TSEs).

Spiroplasma embedded in the biofilm polysaccharide matrix

are markedly resistant to physical and chemical treatment, simulating the biologic properties of the TSE agent. Microcolonies of spiroplasma embedded in biofilm bound to clay are the likely mechanism of lateral transmission of scrapie in sheep and chronic wasting disease in deer via soil ingestion. Spiroplasma in biofilm bound to the stainless steel of surgical instruments may also cause iatrogenic transmission of Creutzfeldt-Jakob disease. Sessile spiroplasma in biofilm attach to the surface by curli-like fibrils, a functional amyloid that is important for spiroplasma entering cells. Curli fibers have been shown to interact with host proteins and initiate formation of a potentially toxic amyloid that multiplies by self-assembly. In TSE, this mechanism may explain how spiroplasma trigger the formation of prion amyloid.

This possibility is supported by experiments that show spiroplasma produce α-synuclein in mammalian tissue cultures.

The data linking spiroplasma to neurodegenerative diseases provide a rationale for developing diagnostic tests for TSE based on the presence of spiroplasma-specific proteins or nucleic acid.

++++++++++ Research efforts should focus on this bacterium for development of therapeutic regimens for Creutzfeldt-Jakob disease.+++++++++++++
-----------------------
http://www.ncbi.nlm.nih.gov/pubmed/23846702
Bpur, the Lyme disease spirochete's PUR domain protein: identification as a ++++++++transcriptional modulator++++++ and characterization of nucleic acid interactions.

Bpur, binds with high affinity to double-stranded DNA adjacent to the erp transcriptional promoter.

Bpur was found to enhance the effects of the erp repressor protein, BpaB.

+++++++++++ Bpur also bound single-stranded DNA and RNA, ++++++++++++with relative affinities RNA > double-stranded DNA > single-stranded DNA.
--------------------
I really would like to hear your scientific explanation! I would also like to hear Europe's explanation for slaughtering 200 Million cattle and various assorted zoo animals and farm lots why they didn't bother to treat the infections that cause it!

admin
Site Admin
Posts: 342
Joined: Wed 25 Jul 2007 21:06

Re: Doxycycline stops Prion Protein Infections

Post by admin » Tue 25 Feb 2014 2:06

Pandora,

I repeat what I said:

The website morgellons-research.org is not an acceptable reference here in the "Science"-section. It is not based on published medical research.

BTW: the owner of that website is Marc Neumann. Here is some background on him:

http://scienceblogs.com/insolence/2010/ ... -rhetoric/
http://scienceblogs.com/insolence/2010/ ... orgellons/
http://scienceblogs.com/insolence/2010/ ... files-you/

Pandora
Posts: 252
Joined: Tue 20 Mar 2012 14:58

Re: Doxycycline stops Prion Protein Infections

Post by Pandora » Tue 25 Feb 2014 5:16

http://www.newhaven.edu/515835/
Evidence Mounting that Morgellons Disease is an Emerging Infectious Illness, Contrary to CDC Report
--
http://www.prweb.com/releases/2013/1/prweb10299034.htm
Laboratory Testing Confirms Infectious Process in Morgellons Disease (MD)
--
http://www.thecehf.org/morgellons-2014- ... mpaign=feb
--
http://www.thecehf.org/morgellons-disease-research.html
--
Abstract

Various conventional reactions in polymer chemistry have been translated to the supramolecular domain, yet it has remained challenging to devise living supramolecular polymerization.

To achieve this, self-organization occurring far from thermodynamic equilibrium-ubiquitously observed in nature-must take place.

++++++++++Prion infection is one example that can be observed in biological systems. ++++++++++++

Here, we present an 'artificial infection' process in which porphyrin-based monomers assemble

++++++ into nanoparticles,++++++

++++++++and are then converted into nanofibres+++++++++

in the presence of an aliquot of the nanofibre,

which acts as a 'pathogen'.

We have investigated the assembly phenomenon using isodesmic and cooperative models and found that it occurs through a delicate interplay of these two aggregation pathways.

Using this understanding of the mechanism taking place, we have designed a living supramolecular polymerization of the porphyrin-based monomers.
http://www.ncbi.nlm.nih.gov/pubmed/24557132
--
Now they will declare the JAPANESE are all just psych too to continue the criminal case of "Delusional Parasitosis".

Pandora
Posts: 252
Joined: Tue 20 Mar 2012 14:58

Re: Doxycycline stops Prion Protein Infections

Post by Pandora » Fri 28 Feb 2014 0:58

Stepwise Organization of the β-Structure Identifies Key Regions Essential for the Propagation and Cytotoxicity of Insulin Amyloid Fibrils.
http://www.ncbi.nlm.nih.gov/pubmed/24569992
J Biol Chem. 2014 Feb 25. [Epub ahead of print]

Chatani E1, Imamura H, Yamamoto N, Kato M.
Author information 1Kobe University, Japan;

Abstract
Amyloid fibrils are supramolecular assemblies,

the deposition of which is associated with many serious diseases

including Alzheimer's, prion, and Huntington's diseases.

Several smaller aggregates such as oligomers and protofibrils have been proposed to play a role in the early stages of the fibrillation process;

however, little is known about how these species contribute to the formation of mature amyloid fibrils with a rigid cross-β structure.

Here, we identified a new pathway for the formation of insulin amyloid fibrils

at a high concentration of salt in which mature fibrils were formed in a stepwise manner via a prefibrillar intermediate:

minute prefibrillar species initially accumulated,

followed by the subsequent formation of thicker amyloid fibrils.

FTIR spectra suggested the sequential formation of two types of β-sheets

with different strength hydrogen bonds,

one of which developed concomitantly with the mutual assembly of the prefibrillar intermediate to form mature fibrils.

Interestingly, fibril propagation and cellular cytotoxicity appeared only after the later step of structural organization,

and a comparison of β-sheet regions between the prefibrillar intermediate and mature fibrils using proteolysis led to the proposal of specific regions essential for the manifestation of these properties.

=========
Elife. 2014 Jan 1;3:e01489. doi: 10.7554/eLife.01489.

Structural basis for the prion-like MAVS filaments in antiviral innate immunity.

Xu H1, He X, Zheng H, Huang LJ, Hou F, Yu Z, de la Cruz MJ, Borkowski B, Zhang X, Chen ZJ, Jiang QX.
Author information

1Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, United States.

Abstract

Mitochondrial antiviral signaling (MAVS) protein is required for innate immune responses against RNA viruses.

In virus-infected cells MAVS forms prion-like aggregates to activate antiviral signaling cascades,

but the underlying structural mechanism is unknown.

Here we report cryo-electron microscopic structures of the helical filaments

formed by both the N-terminal caspase activation and recruitment domain (CARD) of MAVS

and a truncated MAVS lacking part of the proline-rich region and the C-terminal transmembrane domain.

Both structures are left-handed three-stranded helical filaments,

revealing specific interfaces between individual CARD subunits that are dictated by electrostatic interactions

between neighboring strands and hydrophobic interactions within each strand.

Point mutations at multiple locations of these two interfaces impaired filament formation and antiviral signaling.

Super-resolution imaging of virus-infected cells

revealed rod-shaped MAVS clusters on mitochondria.

These results elucidate the structural mechanism of MAVS polymerization,

and explain how an α-helical domain uses distinct chemical interactions to form self-perpetuating filaments.

DOI: http://dx.doi.org/10.7554/eLife.01489.001.

Pandora
Posts: 252
Joined: Tue 20 Mar 2012 14:58

Re: Doxycycline stops Prion Protein Infections

Post by Pandora » Mon 17 Mar 2014 21:24

Interesting "New" concept from Germany and France on Tick Born Disease.....

Viruses 2014, 6(3), 1149-1187; doi:10.3390/v6031149
Review
Incorporation of Hepatitis C Virus E1 and E2 Glycoproteins: The Keystones on a Peculiar Virion
Gabrielle Vieyres 1,* email, Jean Dubuisson 2,3,4,5email and Thomas Pietschmann 1email
http://www.mdpi.com/1999-4915/6/3/1149

Surprisingly however, both E1 and E2 models have been calculated based on their homology with the same protein,

namely the TBEV envelope protein E [63,64].

In both cases, the authors found a homology resulting in the description of either E1 [64] or E2 [63] as a class II fusion protein. Also, the small size of E1 and E2 ectodomains as compared to their flavivirus parent (E ectodomain) is startling.

This suggested that HCV might have a truncated class II fusion protein [64,65]

or that both glycoproteins might participate in the fusion process,

as also suggested by E1E2 mutagenesis and functional fusion assays [29,66–70]. Interestingly, similar analyses successfully predicted the bunyavirus class II fold and fusion loop [71,72].
------------------
http://www.sciencedirect.com/.../pii/S1046592885710030
Expression of Truncated and Full-Length Forms of the Lyme Disease Borrelia Outer Surface Protein...
--
I am beginning to think we got HepC because they used synthetic peptides in vaccines. ------------

TBEV as well as several mosquito-borne flaviviruses, like dengue, yellow fever, Japanese encephalitis, and West Nile viruses, are important human pathogenic viruses. The flavivirus E polypeptide chain contains about 500 amino acids.

The structure of the TBEV E ectodomain (termed sE and containing about 400 residues)

has shown that the E subunits are elongated rods

that associate in an antiparallel fashion,

leading to a brick-shaped dimer with the C-termini at either end (Rey et al, 1995).

Infectious virions contain 90 dimers at their surface,

forming a smooth protein shell completely covering the viral membrane (Kuhn et al, 2002).

The sE ectodomain is responsible for the lateral contacts between dimers at the viral surface.

The viral membrane-interacting segment of the protein contains roughly the 100 C-terminal amino acids that immediately follow sE in the amino-acid sequence.

This segment is folded

as four α-helices that have been visualized by electron cryomicroscopy (cryo EM) and image reconstruction of mature dengue virus particles (Zhang et al, 2003a). The first two helices are amphipathic and lie flat on the viral membrane, interacting with the lipid heads of the outer leaflet of the lipid bilayer.

This region of the protein is called the ‘stem' (Allison et al, 1999). The third and fourth α-helices traverse the membrane as an antiparallel coiled-coil.

Exposure of the soluble sE fragment to low pH leads to a reversible dissociation of the dimer, resulting in exposure of the fusion peptide loops but not to trimerization as on the virion envelope (Stiasny et al, 1996).

However, as initially shown for the soluble ectodomain of SFV E1 (Klimjack et al, 1994), when the low-pH treatment is carried out in the presence of liposomes,

the interaction of the fusion peptide loops with lipids

triggers an irreversible trimerization of sE,

which remains stably membrane associated (Stiasny et al, 2002).

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC380989/

These data suggest that the ‘open' and ‘closed' conformations of the fusion proteins

may interact differently with the lipid bilayer.
---------------------------
Because we already know where HepB came from when they found 88% of HIV pos. for HepB....Spirochetal infected cell lines used for decades.
http://vimeo.com/9581140
http://vimeo.com/9581140

TicksSuck
Posts: 100
Joined: Thu 31 May 2012 20:25

Re: Doxycycline stops Prion Protein Infections

Post by TicksSuck » Tue 18 Mar 2014 1:29

For some reason, these posts reminded me of the automatic computer science paper generator: http://pdos.csail.mit.edu/scigen/.

Is it possible that someone built a similar generator for LymeNet Europe postings? :geek:

TicksSuck

Pandora
Posts: 252
Joined: Tue 20 Mar 2012 14:58

Re: Doxycycline stops Prion Protein Infections

Post by Pandora » Tue 18 Mar 2014 6:41

Pandora just pulls her's out of a Box when it is opened in front of her. I don't know how they do it since the "peer review" experts never read this stuff anyway! LOL Seeds.....They all have been stuck in the matrix of 1956 when they offered us all immune suppression sold for lies of protection.
http://www.lymeneteurope.org/forum/view ... 246#p36246

Pandora
Posts: 252
Joined: Tue 20 Mar 2012 14:58

Re: Doxycycline stops Prion Protein Infections

Post by Pandora » Fri 21 Mar 2014 14:39

Good Spirochetal Morphology of Morgellin pics.

We demonstrate that all identified β-sheets feature an in-register parallel stacking for both polymorphs.

The two forms show a different molecular arrangement in the unit cell and distinct dynamic features, while sharing a highly flexible C-terminal domain.
http://www.ncbi.nlm.nih.gov/.../figure/ ... 0659-g001/
http://www.ncbi.nlm.nih.gov/pubmed/24599158
---------
Doctor MacDonalds pics way back in the day.....And to think....He could have won a Nobel Prize too!
http://molecularalzheimer.org/files/Cel ... tic_Bb.pdf

Prion-like Polymerization Underlies Signal Transduction in Antiviral Immune Defense and Inflammasome Activation.
http://www.ncbi.nlm.nih.gov/pubmed/24630723
Cell. 2014 Mar 13;156(6):1207-22. doi: 10.1016/j.cell.2014.01.063.

Cai X1, Chen J1, Xu H2, Liu S1, Jiang QX3, Halfmann R4, Chen ZJ5.
Author information
Abstract

Pathogens and cellular danger signals activate sensors such as RIG-I and NLRP3 to produce robust immune and inflammatory responses through respective adaptor proteins MAVS and ASC,

which harbor essential N-terminal CARD and PYRIN domains, respectively.

Here, we show that CARD and PYRIN function as bona fide prions in yeast and that their prion forms are inducible by their respective upstream activators.

Likewise, a yeast prion domain can functionally replace CARD and PYRIN in mammalian cell signaling.

Mutations in MAVS and ASC that disrupt their prion activities in yeast also abrogate their ability to signal in mammalian cells.

Furthermore, fibers of recombinant PYRIN can convert ASC into functional polymers capable of activating caspase-1.

Remarkably, a conserved fungal NOD-like receptor and prion pair can functionally reconstitute signaling of NLRP3 and ASC PYRINs in mammalian cells.

These results indicate that prion-like polymerization is a conserved signal transduction mechanism in innate immunity and inflammation.
--------------------------
One more time--
Likewise, a yeast prion domain can functionally replace CARD and PYRIN in mammalian cell signaling.

Mutations in MAVS and ASC that disrupt their prion activities in yeast also abrogate their ability to signal in mammalian cells.

Furthermore, fibers of recombinant PYRIN can convert ASC into functional polymers capable of activating caspase-1.

Remarkably, a conserved fungal NOD-like receptor and prion pair can functionally reconstitute signaling of NLRP3 and ASC PYRINs in mammalian cells.
==================
NO SIGNAL NOT SICK? NO!!! THEY CAN SIMPLY BE GROWING IN YOUR GUTS, BRAINS, AND SKIN SHARING THEIR GENES IN THE PRION SYNERGY OF SPIROCHETAL DISEASE IMMUNE SUPPRESSION AND YOUR LEFT TO SUFFER AND DIE OF INCREDIBLY CRIMINALLY STUPID!

Inflammasome: putting the pieces together.
http://www.ncbi.nlm.nih.gov/pubmed/24630715
Cell. 2014 Mar 13;156(6):1127-9. doi: 10.1016/j.cell.2014.02.038.

Ruland J.
Author information
Abstract

Microbial and danger signals result in inflammasome activation and release of inflammatory cytokines through mechanisms that remain elusive.

Cai et al. and Lu et al. show that triggering of inflammasome sensors induces prion-like polymerization of the adaptor ASC into filaments.

These structures function as platforms for inflammatory cytokine production

and represent a unified mechanism for inflammasome assembly.
--------------------
http://www.lymeneteurope.org/forum/view ... &start=110
PrP(Sc) was more efficiently transmitted from adherent spleen cells to neuronal cells than from floating spleen cells.

The adherent spleen cells were composed of
macrophages (80%),
dendritic cells (8%) and
follicular dendritic cells (3%),

indicating that macrophages play an important role in PrP(Sc) transmission from immune cells to neuronal cells.

Although PrP(Sc) in the immune cells used as donor cells was gradually degraded, the PrP(Sc) transmitted to neuronal cells was observed by Western blot analysis.

Investigation of the mechanism of PrP(Sc) transmission between cells represents an important step towards understanding the pathogenesis of prion diseases.
http://www.ncbi.nlm.nih.gov/pubmed/23246505
-----------------------------------------------------
You know all those macrophages that are supposed to get rid of infections.....sorry. Gotta kill all the bugs. And stop infecting them..
http://www.lymeneteurope.org/forum/view ... 246#p36246

Extracellular environment modulates the formation and propagation of particular amyloid structures.
Mol Microbiol. 2014 Mar 17. doi: 10.1111/mmi.12579. [Epub ahead of print]
http://www.ncbi.nlm.nih.gov/pubmed/24628771
Strikingly, exposure to specific stressful environments

dramatically altered the variants of [PSI+ ] that formed de novo.
-----------
WHAT IS THE TAKE AWAY FROM ALL THE RESEARCH?
Do we really want to deal with another SYNDROME or do we want to DO WHAT MUST BE DONE and treat the truth to stop the SYNDROMES?
http://vactruth.com/2014/03/19/tissue-s ... ild-abuse/

The exact same thing happens to Lupus pts. who get stem cells before treating the infections that cause it. Their FACES fall off from the induced immune response suddenly recognizing the infections are even there.

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