Spidersmilk

Spidersmilk
Spidersmilk
Born	Error: Invalid birth date for calculating age; Montreal, Quebec, Canada

The name Spidersmilk is taken from a combination of spidersilk and goatsmilk: Spidersmilk. My inspiration for the name came from a group of scientists at bioSteel who have engineered goats that have a gene from spiders that produces the spider silk protein in their milk that, when concintrated, forms silk.^[1] Goats that produce spider silk have been dubbed Spidergoats on google. Spidergoats give Spidersmilk or Goatsilk This silk can be woven into bulletproof vests, dresses, rugs, and ultra strong cables (which are stronger than an equally thick peace of steel) used to operate strong robotic arms to lift very heavy objects, among other uses. This user is a Time Traveler who has masterd manipulation of the 4th dimention through bending of light. This user is more than 4,000 years old. SPOOOOOOOOOOOOOOKY!!!!!!!!!!!^[2]

I am also a fan of the X files and interested in UFOs and free energy. The truth is out there.

Well known hoax articles that were deleted

here are some of the links that I have collected:

Bicholim conflict

Upper Peninsula War

microbiology

I am interested in microbiology, especially prions, Transmissible spongiform encephalopathies (TSEs) and Alzheimer's links to infections. I have more of an open mind about it then most people and question weather prions really cause the TSEs or are merly the result of the infection with an as yet unidentified "Scrapie pathogen". I used to think that prions were the cause of the TSEs, as well as Alzheimer's. My reasons were that if Prion plaques in the brains of CJD cause CJD, then Amyloid plaques must cause Alzheimer's, which is what most of the articles I read also said. Then I saw a PBS documentary about Lyme disease, linking it and related bacteria to Alzheimer's by finding Lyme and other Spirochete DNA in 90% of Alzheimer's brains but not in healthy individuals. It confused me at first because I thought it couldn't be caused by bacteria because Alzheimer's is associated with misfolded proteins in the brain (Beta-amyloid and Tau neurofibrillary tangles) and therefore has to be caused by misfolded proteins (After all, Mad cow disease is caused by a misfolded protein called a prion, I thought). But it also interested me so I looked into it, and I found many articles about how Borrelia (Lyme bacteria) and other Spirotchees had the ability to cause Alyloid Beta (Aβ) and neurofibrillary tangles (NFT) in neuronal cell cultures. After that I was less skeptical and found other articles on the subject, I was convinced.

After that I began to wonder "if misfolded prions don't cause Alzheimer's, they must not cause Mad cow disease either" and I looked for alternative theories and found the Spiroplasma hypothesis and the Viral hypothesis. I found that the Spiroplasma and Viral hypothesis (especially the Spiroplasma one) made just as much, if not more, sense than the prion theory. It explains just about all of what we observe with the TSEs, as I will discuss later.

If one looks back at the history of the Prion theory, it is obvious that it has changed a lot over the years. When the Prion was first discovered, it was thought to be a foreign protein that is the product of a normally silenced gene, and that introducing the protein woke the gene up, creating more of the protein, spreading to other cells which then wake up their silenced gene. The new, supposedly infectious protein was named a Prion for the words protein and infection. It was subsequently found that the protein was also present in healthy individuals, but in a different form (it was folded differently and clumped together), thus it was an altered but previously undiscovered host protein. The host protein was then named PrP for Prion Protein, and the gene that encoded it was named PRNP for PrioN Protein. The normal form of the protein was named PrP^C for C for Cellular prion protein while the abnormal or prion form was named PrP^Sc for Sc from Scrapie. It was then thought that the prion, PrP^Sc, replicated by causing normally the normally folded PrP^C to misfold into the PrP^Sc shape by acting as a template. The newly formed PrP^Sc would then go on with the original PrP^Sc to misfold more of the PrP^C, thus leading to a chain reaction. With the creation of synthetic prions aka PrP^Sc, it was found that they were not infectious in a reproducible manner, leading to the theory that not all prions are infectious. Then, in 2005, PMCA (Protein misfolding cyclic amplification), a technology designed to amplify prions if they are capable of replication, came out. It was found that PrP^Sc was capable of replicating, supporting the idea that PrP^Sc acts as a template for more PrP^Sc formation and thus strongly supporting the Prion theory. Such prions were also found to reproducibly cause disease, further supporting the theory that prions caused the diseases. However, when only purified PrP was used in place of the brain homogenate used in the original experiment, natural prions that replicated in PMCA had no reproducible ability to cause disease, just like synthetic prions.

This lead to the theory that Prions need other host molecules like Lipids and RNA or DNA to take on an infectious form, called the Multi-component hypothesis. This hypothesis was supported by the fact that synthetic prions created by adding purified PrP to either normal mouse brain homogenate or a combination of DNA or RNA with and lipids and then amplified in PMCA caused disease in mice.

However, this too, while more likely to cause disease than synthetic prions created without other host compounds, was found to not be reproducible either.

This has lead to 2 theories. Either A: synthetic prions, even ones formed with other host compuonds such as brain homogenate, are only rarely infectious, or B: There is a foreign nucleic acid involved with the disease that links up with PrP^Sc to form the infectious prion. The latter hypothesis is a revival of the Virino hypothesis. The former hypothesis is currently supported by the majority of prion researchers, however some think that the the second hypothesis is supported by the fact that synthetic prions formed by taking purified PrP and synthetic lipids and synthetic RNA are less likely to be infectious to mice than synthetic prions formed by using mouse derived lipids and RNA or DNA, or brain homogenate.

So in short, the prion theory has gone from the infectious prion being basically a foreign self replicating protein, to a misfolded host protein PrP, to a subset of misfolded host PrP, to misfolded host host PrP that required host lipids and DNA or RNA to replicate, to a subset of misfolded host PrP that requires host lipids and nucleic acids to replicate or even to remain infectious. Some have even gone as far as suggesting that a foriegn, stain defining nucleic acid with misfolded PrP bound to and wrapped arround it is the real infectious prion. Basically, the role of the protein in the prion has become progressively less significant. It doesn't make any sense that if prions really do cause TSEs, then a prion that is capable of replicating in a test tube should not also be able to cause disease. On the flip side, the diseases appears to have been transmitted without prions, where the prion has been destroyed to undetectable levels by antibodies or proteinase enzymes, in which case special dye that stains protein yields a negative result.

There are also discrepancies with regard to distribution of the prion in TSEs with regard to infectivity, including the way the the prion sreads in the body and how the infection spreads. For example, the Prion seems to be absent 10% of CJD patients, and when CJD, VCJD/BSE or Scrapie are transmitted to mice, the Prion is undetectable in about 50% of cases, and doesn't become detectible in 100% of cases until the second, third or fourth transmission. It is thought that genetic susceptibility to TSE infection depends on the gut absorption of Prions. In an article however, liked below, notes that in studies where scientists infected sheep through the gut, sheep of all susceptiblility genotypes absorbed the prion in equal quantities, regardless of susceptibility. Using immunochemistry (a staining technique) they detected the injected prion villous lacteals (a type of lymph capillary in the Villi) and submucosal lymph nodes from 15 minutes to 3.5 hours after injection. The Prion was not taken up by the Peyer's patches, where early replication of the agent is known to occur. The prion could not be detected in the Peyer's patches until 30 days post injection. The authors, Martin Jeffrey, PhD et. al. said "These results indicate discrepancies between the routes of transportation of prion-protein from the inoculum and sites of de novo-generated disease-associated prion-protein subsequent to scrapie agent replication,".^[3] Further doubt was cast by the study when they took highly infectious Scrapie brain material and digested it similar to a sheep's stomach. After digestion, only faint traces of the Prion could be detected using Western blot dye. Dr Jeffry said of his study: "Think about it, a sheep grazing in a field is not naturally exposed to highly infected brain and could only pick up a tiny amount of prion protein from other tissues. This will then be exposed to 48 hours or more digestion before it arrives in the gut, and our experiments show that after this, the chance of there being more than an immeasurably small amount of prion protein left to absorb is very small."

In mice Scrapie on the other hand the Prion does accumulate in the Peyer's patches soon after infection through the gut, however, there are other discrepancies. For example, the Prion spreads through the body and crosses the blood brain barrier and enters the brain almost immediately after infection, and does so indiscriminately across all brain regions. The infection on the other hand doesn't cross the blood brain barrier until several months later, after a period of replication in the blood and lymphatic tissues. When it does enter, it doesn't enter the whole brain all at once like the Prion does but rather targets specific brain regions, and then progressively spreads outward along the brain's neuronal circuits. By the time the infection enters the brain, the Prion can no longer be detected in brain tissue, and doesn't reappear until the Scrapie pathogen has replicated 1000,000 fold.

In the hamster adapted Scrapie strain, when the infection is transmitted to mice, mice on initial transmission do not develop clinical disease but indefinitely retain and replicate the pathogen despite the absence of detectable Prions. Upon second transmission, the pathogen still doesn't cause clinical disease in mice but retains it's ability to cause disease in hamsters. Upon the third and fourth transmission however, the pathogen divides into a population that causes disease in mice but not hamsters, a population that causes disease in hamsters but not mice, and a population that causes disease in both. This is difficult to explain if Prions are the cause as the Prion was not detectable, and while it may be said that the Prion changing it's shape to become undetectable, if the Prion did mutate it would likely not retain it's strain properties (because it is thought that prion shape encodes strains). It did maintain it's strain properties, as when transmitted back to hamsters it induced the same disease.

There are other theories as to the cause of the TSEs, however, until recently even these usually theories assumed that the Prion, while not the cause, was the main toxin causing the damage. However recently even this is being called into question. In one article, scientists observed neurodegeneration in mice with CJD without detectable Prions. In Another article scientists have found that Beta amyloid can trap pathogens like HSV, slowing down their spread. Other studies in transgenic mice that over-produce Bera-amyloid for Alzheimer's mouse models develop only mild symptoms and no neuronal loss, no Tau NFT tangles and is not fatal. Human Alzheimer's on the other hand causes both neuronal loss and Tau NFT tangles, and is also fatal. Tau now appears the same way, as mice that overproduce tau develop tangles and memory impairment but no neuronal loss.

It now appears that Tau tangle deposits may have antioxidant effects, and appears to protect the neurons from oxidative stress, as things known to cause oxidative stress like concussions also cause Tau tangle formation. Some neuronal cells have been shown to carry tau tangles for decades without toxic effect or destabilization of cytoskeliton.

Also it is usually thought that once "misfolded" proteins appear, they will only progressively accumulate. However, imaging scans at least for Beta-Amyloid demonstrate that Amyloid forms rapidly in the brain following trauma, then is slowly cleared. This is also in line with AA amyloidosis that develops in people with TB, HIV and other chronic inflammation inducing diseases. Misfolded AA amyloid accumulates in the kidney and other organs. When the underlying disease is treated, the amyloid almost always regresses and shrinks. The same also appears to be true for PrP as it has been shown to have the ability to slow down the spread of HIV in the brain. It also appears to have antioxidant properties. Taken together it suggests that Prions may be just the result of infection with the Scrapie agent.

Here are some of the other theories.

Below are articles about Transmissible spongiform encephalopathies and Alzheimer's.

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5845560/ HSV, Alzheimer's CJD and Spiroplasma link.

https://www.researchgate.net/publication/235220355_Prions_the_Protein_Hypothesis_and_Scientific_Revolutions History of the Prion theory.

https://www.biorxiv.org/content/biorxiv/early/2017/12/11/232074.full.pdf Primordial pathogen in CJD and Multiple Sclerosis.

http://www.pahousegop.com/News/Latest-News/Maloney-to-Join-Press-Conference-on-Chronic-Wasting-Disease CWD press conference, Spiroplasma hypothesis

https://books.google.com/books?id=P3H1BwAAQBAJ&pg=PA85&lpg=PA85&dq=Scrapie+in+mice:+ultrastructural+observations+in+the+cerebral+cortex&source=bl&ots=dyiI_LMIV9&sig=ACfU3U3iB8uJegACUqFfvaLabYmx6L3h_g&hl=en&sa=X&ved=2ahUKEwjZraXXm6jgAhUI7oMKHU8PD1Q4ChDoATAAegQICRAB#v=onepage&q=Scrapie%20in%20mice%3A%20ultrastructural%20observations%20in%20the%20cerebral%20cortex&f=false TVS in different TSE strains

https://www.alzforum.org/news/research-news/imaging-reveals-amyloid-year-after-traumatic-brain-injury Amyloid formation after concussion is gradually cleared

https://www.medpagetoday.org/infectiousdisease/publichealth/2958 Prion theory called full of holes

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5004172/ Prions cross the blood brain barrier early after infection

https://academic.oup.com/jid/article/186/Supplement_2/S166/2191257 Hamster scrapie adaptation to mice, infectivity persists despite absence of detectable prions

https://academic.oup.com/jnen/article/77/1/64/4633865

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2765711/ Tau tangles may protect the brain from oxidative stress

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3714129/ Agent induced neurodegeneration without detectable Prions

http://www.unifiedsportsmenpa.org/meetings.htm

https://www.ncbi.nlm.nih.gov/pubmed/19997557?log$=activity

https://www.dentistrytoday.com/news/todays-dental-news/item/3013-protect-your-patients-and-practice-from-prions-viruses-and-systemic-disease

https://www.alzforum.org/news/research-news/toxic-synuclein-corrupts-native-wild-type-mice Parkinson's

https://www.stressmarq.com/amyloid-hypothesis-vs-tau-hypothesis/?v=7516fd43adaa

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3745981/ Beta-amyloid may protect against oxidative stress in Alzheimer's

https://patents.google.com/patent/US20090258408A1/en

https://patents.google.com/patent/WO2010051055A2/en Spiroplasma culture

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4345559/ Mice with type F APOA2 are resistant to senile amyloidosis

http://www.jbc.org/content/287/36/30585.full.html Formation of amyoid fibrils is similar to crystal formation

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3975080/Gout crystal formation, once crystal growth is initiated, the concentration of urate needed to grow the crystals is lower

https://schaechter.asmblog.org/schaechter/2018/02/a-whiff-of-taxonomy-the-tenericutes.html Evolution of Mycoplasma

https://www.microbiologyresearch.org/docserver/fulltext/ijsem/63/7/2727_ijs048983.pdf?expires=1559322463&id=id&accname=guest&checksum=7EAD82CA6B11159E6B92BF4EEC3481D2 More Evolution of Mycoplasma

https://www.pnas.org/content/82/4/1160 Mycoplasma 16s RRNA, fermicutes

https://www.biorxiv.org/content/10.1101/185751v2.full

https://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1006491

https://www.tandfonline.com/doi/full/10.4161/pri.25809 Autophagy and prions

https://www.termedia.pl/Prion-diseases-a-riddle-wrapped-in-a-mystery-inside-an-enigma,20,10625,1,1.html Prion diseases: a riddle wrapped in a mystery inside an enigma

https://www.ncbi.nlm.nih.gov/pubmed/12179875

https://jcm.asm.org/content/47/11/3791 False negative PCR

https://www.researchgate.net/publication/232665674_Prions_Introducing_a_Complex_Scientific_Controversy_to_a_Biology_Classroom

https://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1004796 FFI transgenic mice that do not transmit disease