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| Morgellons Disease (Fiber Disease) General discussion on Morgellons Disease |
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| SS had posted this: Our Strange World Excerpt: c) My research also shows that the cure might already be available, but not yet released to the public in order not to implicate Monsanto in a lawsuit and cause a panic among the human population. Monsanto greatly funds the campaigns of many politicians, in which many have been corrupted and bought to shut up about this life threatening health hazard. end Ok- that caught my eye- and is of interest because I have read that before- That Monsanto has the antidote- cure- years ago. If it is out there- it can be found. Monstanto and the many subsidiaries patent everything that they can. They attempted to patent pigs not long ago. Given that fact, it would seem to me that if you would follow their patents- maybe in the same time frame that this was introduced to the world, you may have a bingo- that is- find the cure. My logic is that if something was unleashed-on purpose either via GMO in food or other sources then there will be an antidote out there that would be in the same time frame as the GMO that caused the damage. So you would follow the GM/Agro research and development and may find the 'countermeasure' or cure. If this 'something' was unleashed by accident then the time frame would be a later date and more difficult to locate but still doable. I truly believe that Lyme disease is at the heart of this condition and that other symptoms (fibers) may be caused by toxins and/or GMO- specifically Agrobacterium Ti (C 5 . IMO, the condition is multilayered.With the new information coming to light on Agrobacterium/GMO's and the potential health effects there can be no denial that with or without Lyme or any other disease, this needs to be addressed. That is why I started to 'Hunt' for the Monsanto Antidote/cure. Venetia Last edited by Venetia; May 24th, 2009 at 07:24 AM. |
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| Find the Antidote- the Monsanto "Cure" First stop out on the search for the Monsanto Antidote- Can't recall the researcher that stated that the unknown component is a protein. Found this: X-rays reveal the structure of proteins Cells reveal communication secrets Excerpt: In 2002, Argonne’s Rong-guang Zhang and SBC collaborators, including Joachimiak, revealed a method cells may use to communicate. Bacteria communicate by releasing and sensing chemical signals known as pheromones—a phenomenon called quorum sensing. Biologists may one day manipulate this communication to thwart harmful bacteria or aid helpful bacteria. Biologists determined the structure of TraR protein of the well-known Agrobacterium tumefaciens—an agricultural pathogen that causes tumors in plants. “The structure,” Zhang said, “is the most asymmetrical we have seen for protein-DNA complex. It is shaped liked a butterfly with its wings bent back.” Pheromones lie fully embedded within the protein. To activate the pheromones, several amino acid residues critical to RNA polymerase activation, or gene copying, make contact with the “butterfly body” of TraR. Argonne researchers collaborated with Cornell University and Monsanto Company. This research was published in Nature. End **** TraR protein of Agrobacterium ti with Pheromones fully embedded within the protein- activated by amino acid residues or gene copying making contact with "butterfly body" of TraR. What comes to mind when reading this is Tam Tams' work. ![]() The Chaperone GroESL Enhances the Accumulation of Soluble, Active TraR Protein, a Quorum-Sensing Transcription Factor from Agrobacterium tumefaciens -- Chai and Winans, 10.1128/JB.01434-08 -- The Journal of Bacteriology JB Accepts, published online ahead of print on 27 March 2009 Previous Article | Next Article J. Bacteriol. doi:10.1128/JB.01434-08 Copyright (c) 2009, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved. The Chaperone GroESL Enhances the Accumulation of Soluble, Active TraR Protein, a Quorum-Sensing Transcription Factor from Agrobacterium tumefaciens Yunrong Chai and Stephen C. Winans* Department of Microbiology, Cornell University, Ithaca, New York 14853 * To whom correspondence should be addressed. Email: scw2@cornell.edu. Fair use Abstract TraR of Agrobacterium tumefaciens is a LuxR-type quorum-sensing transcription factor that regulates genes required for replication and conjugation of the tumor-inducing (Ti) plasmid. TraR requires its cognate autoinducer N-3-oxooctanoyl-homoserine lactone (OOHL) for resistance of proteolysis in wild type bacteria and for correct protein folding and solubility when overexpressed in E. coli. In this study, we ask whether GroESL might also play a role in TraR folding, as this molecular chaperone assists many proteins in attaining their native tertiary structure. Expression of E. coli GroESL in a strain expressing TraR increases the solubility of TraR and increases transcriptional activity of a TraR-dependent promoter. Both solubility and activity still require OOHL. We also studied the folding of TraR in the closely related bacterium Sinorhizobium meliloti. A mutation in one groEL gene slightly decreased the expression of a TraR-dependent promoter, strongly decreased the accumulation of TraR in western immunoblot assays, and also strongly influenced the fate of pulse-labeled TraR. Last edited by Venetia; October 9th, 2009 at 07:53 AM. |
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| Amino-Terminal Protein Fusions to the TraR Quorum-Sensing Transcription Factor Enhance Protein Stability and Autoinducer-Independent Activity J Bacteriol. 2005 February; 187(4): 1219–1226. doi: 10.1128/JB.187.4.1219-1226.2005. PMCID: PMC545634 Copyright © 2005, American Society for Microbiology Amino-Terminal Protein Fusions to the TraR Quorum-Sensing Transcription Factor Enhance Protein Stability and Autoinducer-Independent Activity Yunrong Chai and Stephen C. Winans* Department of Microbiology, Cornell University, Ithaca, New York *Corresponding author. Mailing address: Department of Microbiology, Cornell University, Ithaca, NY 14853. Phone: (607) 255-2413. Fax: (607) 255-3904. E-mail: scw2@cornell.edu. Received September 13, 2004; Accepted November 8, 2004. *** Turns out that there is an INHIBITOR for the TraR Protein: Activity of the quorum-sensing regulator TraR of A...[Mol Microbiol. 1998] - PubMed Result 1: Mol Microbiol. 1998 Jan;27(2):289-97.Click here to read Links Activity of the quorum-sensing regulator TraR of Agrobacterium tumefaciens is inhibited by a truncated, dominant defective TraR-like protein. Zhu J, Winans SC. Section of Microbiology, Cornell University, Ithaca, NY 14853, USA. Fair use Horizontal transfer of Agrobacterium tumefaciens tumour-inducing plasmids requires opines, which are released from plant tumours as nutrients for the bacteria. The opine octopine causes synthesis of the quorum-sensing TraR protein, which activates several tra promoters in the presence of a pheromone called Agrobacterium autoinducer (AAI). A gene, traS, was previously found on the same Ti plasmid in an operon that directs the uptake of mannopine, another opine. TraS strongly resembles TraR but lacks a DNA-binding module. TraS did not activate a TraR-dependent promoter and blocked TraR function, probably by forming inactive heteromultimers. Expression of traS was induced by mannopine, although this induction was strongly inhibited by the favoured catabolites succinate, glutamine and tryptone. Mannopine inhibited conjugation in a TraS-dependent fashion, and artificial overexpression of TraS also inhibited conjugation. Favoured catabolites restored tra gene expression in wild-type strains but not in strains that overexpress TraS. Downstream of traS is a gene encoding a truncated, defective chemoreceptor whose expression abolished chemotaxis. ** If this is the protein that is causing Morgellons via Agro- then TraS Inhibits TraR Last edited by Venetia; May 16th, 2009 at 01:03 PM. |
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| Per above: Horizontal transfer of Agrobacterium tumefaciens tumour-inducing plasmids requires opines, which are released from plant tumours as nutrients for the bacteria. Opines: Wapedia - Wiki: Opines Opines are low molecular weight compounds found in plant crown gall tumors produced by the parasitic bacterium Agrobacterium. Opine biosynthesis is catalyzed by specific enzymes encoded by genes contained in a small segment of DNA (known as the T-DNA, for 'transfer DNA'), which is part of the Ti plasmid, inserted by the bacterium into the plant genome. The opines are used by the bacterium as an important source of nitrogen and energy. Each strain of Agrobacterium induces and catabolizes a specific set of opines. There are at least 30 different opines described so far. Contents: 1. Chemical structure 2. Nomenclature 3. Other sources of opines 4. List of opines 1. Chemical structure Chemically, opines fall into two major structural classes: 1. The vast majority are secondary amine derivatives formed by condensation of an amino acid, either with a keto acid or a sugar. The first subcategory includes the nopaline and octopine families. The nopaline family (nopaline, nopalinic acid, leucinopine, glutaminopine, succinamopine) is formed when alpha-ketoglutarate serves as the keto substrate in the condensation reaction. The octopine family (octopine, octopinic acid, lysopine, histopine) is formed when pyruvate is involved in the condensation reaction. The second subcategory includes the mannityl family (mannopine, mannopinic acid, agropine, agropinic acid) formed by the condensation of an amino-acid with mannose. general overview of opine-synthesis 2. Agrocinopines form a small, separate class of opines. Chemically they are sugar-phosphodiesters. For example, agrocinopine A is a phosphodiester of sucrose and L-arabinose. 2. Nomenclature The name opine comes from octopine, the first opine discovered in 1927, not in crown galls, but in octopus muscle. According to Oxford English Dictionary, the word opine was first used in print in 1977. Usually, the name of newly discovered opines has the ending "-opine". Exceptions are nopaline and strombine. On the other hand, not all molecule names ending in "-opine" are opines. For example, atropine, stylopine, europine, and lycopine belong to different classes of molecules. 3. Other sources of opines Opines and opine-like substances are not restricted to crown galls tumors. The very first opine discovered, octopine, was initially isolated from octopus muscle. Similar derivatives have been isolated from muscle tissue of certain marine invertebrates: alanopine, strombine, and tauropine. Opines like acetopine and nopaline can also be formed in normal callus and plant tissue as a result of arginine metabolism. Saccharopine is an intermediate in the metabolism of amino acid lysine and occurs in fungi, higher plants and mammals, including man. The poisonous mushroom ****ocybe acromelalga is a source of four opine type amino acids: valinopine, epileucinopine, isoleucinopine and phenylalaninopine. On the list of Opines: Agropinic acid Agropinic acid (N-1-(D-mannityl)-L-glutamic acid lactam) is produced by crown gall tumors. Belongs to the mannityl family. It is formed by lactamization of agropine. |
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| This protein TraR ties to PM 1 which is a MTBE remediation product: *The product- PM 1 CONTAINS Agrobacterium Ti LymeBusters - MTBE-Filamentous fungus/polymers/bacteria PM 1, which is used in the remediation of the United States' most common pollutant: MTBE/TBA Scroll down to: PM 1 - PFD- see PDF: http://jb.asm.org/cgi/reprint/JB.01259-06v1.pdf mentions Type IV pilus Conjugal transfer- and the supplement indicates an area (outside perimeter) where this transfer would occur- in addition to a Mulitdrug transport 'tunnel'. The Type IV is a reference to the Agrobacterium T C58 found in the PM 1 Then: Genetic and Sequence Analysis of the pTiC58 trb Locus, Encoding a Mating-Pair Formation System Related to Members of the Type IV Secretion Family -- Li et al. 180 (23): 6164 -- The Journal of Bacteriology Journal of Bacteriology, December 1998, p. 6164-6172, Vol. 180, No. 23 Fair use Excerpt: Genetic and Sequence Analysis of the pTiC58 trb Locus, Encoding a Mating-Pair Formation System Related to Members of the Type IV Secretion Family Pei-Li Li,1 Dawn M. Everhart,2, and Stephen K. Farrand1,2,* Departments of Crop Sciences1 and Microbiology,2 University of Illinois at Urbana-Champaign, Urbana, Illinois 61801 Received 1 May 1998/Accepted 17 September 1998 Conjugal transfer of pTiC58 requires two regions, tra which contains the oriT and several genes involved in DNA processing and a region of undefined size and function that is located at the 2-o'clock position of the plasmid. Using transposon mutagenesis with Tn3HoHo1 and a binary transfer system, we delimited this second region, called trb, to an 11-kb interval between the loci for vegetative replication and nopaline catabolism. DNA sequence analysis of this region identified 13 significant open reading frames (ORFs) spanning 11,003 bp. The first, encoding traI, already has been described and is responsible for the synthesis of Agrobacterium autoinducer (AAI) (I. Hwang, P.-L. Li, L. Zhang, K. R. Piper, D. M. Cook, M. E. Tate, and S. K. Farrand, Proc. Natl. Acad. Sci. USA 91:4639-4643, 1994). Translation products of the next 11 ORFs showed similarities to those of trbB, -C, -D, -E, -J, -K, -L, -F, -G, -H, and -I of the trb region of the octopine-type Ti plasmid pTi15955 and of the tra2 core region of RP4. In RP4, these genes encode mating-pair formation functions and are essential for the conjugal transfer of the IncP plasmid. Each of the trb gene homologues is oriented counterclockwise on the Ti plasmid. Expression of these genes, as measured by using the lacZ fusions formed by Tn3HoHo1, required the traI promoter and the transcriptional activator TraR along with its coinducer, AAI. While related to that of RP4, the trb system of pTiC58 did not allow propagation of the trb-specific bacteriophages PRD1, PRR1, and Pf3. The products of several trb genes of the Ti plasmid are similar to those of other loci that encode DNA transfer or protein secretion systems, all of which are members of the type IV secretion family. end excerpt |
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| Additional searches for Monsanto- cure/antidote - US Patents- Monsanto and subsidiary companies *** As an aside: What we know- is that Monsanto has the ability to 'Silence' genes as relates to the horizontal transfer -Agrobacterium: Here is a link where a Professor, an expert in the area of GM, is talking about just that. The Bt silenced the gene for Golden Nematode Resistance. How interesting! An Interview with Plant Scientist Dr. E. Anne Clark on Genetic Engineering in Agriculture (Part I) Excerpt: For example, when Bt was inserted into one of the clones that Monsanto has marketed as their Bt potato, it silenced the gene for golden nematode resistance. Now golden nematode resistance has nothing to do with Bt, it was a completely different gene. But the gene for golden nematode resistance was turned off by the forced insertion of the Bt gene packet. end Last edited by Venetia; May 19th, 2009 at 07:11 AM. |
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| Could just be something like this V... Quote:
Bright-idea-could-doom-cancer-and-viruses--say-Purdue-scientists |
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| Good idea, Carla! You just don't know what could help. I've often thought about Keith Richards and his transfusions. Wondered if that method or one such as your post could be an answer. No doubt this 'stuff' is in our blood. Carla, because there are 2 threads (sorry...) on this topic, could you move this post and yours to the other thread? For some reason, I am not able to delete the first post (the duplicate). Thanks in advance, V |
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| Thank you Carla, for correcting the duplicate threads! ![]() Found some newer patents associated with Monsanto- having nothing to do with a cure or antidote for Morgellons more than likely- but interesting nevertheless: United States Patent: 7425622 -------------------------------------------------------------------------------- United States Patent 7,425,622 Rosen September 16, 2008 -------------------------------------------------------------------------------- Antibodies against C3a receptor Abstract The present invention relates to antibodies and related molecules that specifically bind to C3a Receptor. Such antibodies have uses, for example, in the prevention and treatment of asthma, allergy, and other related inflammatory and immune disorders. The invention also relates to nucleic acid molecules encoding anti-C3a Receptor antibodies, vectors and host cells containing these nucleic acids, and methods for producing the same. The present invention relates to methods and compositions for preventing, detecting, diagnosing, treating or ameliorating a disease or disorder, especially inflammatory and other related disorders, comprising administering to an animal, preferably a human, an effective amount of one or more antibodies or fragments or variants thereof, or related molecules, that specifically bind to C3a Receptor. ****** United States Patent: 7332596 United States Patent 7,332,596 Bunkers , et al. February 19, 2008 -------------------------------------------------------------------------------- Antifungal proteins and methods for their use Abstract A novel protein was isolated from Fusarium culmorum and characterized. The protein, termed FCWP1, demonstrated significant antifungal activity against several fungal species. Mutations in proteolytic consensus sequences contained within FCWP1 improved the stability of its antifungal activity. In addition, a class of proteins related to FCWP1 was identified and characterized. This class is made up of ribosomal proteins and displayed similar values for pI and molecular weight. A representative number of proteins from this class were tested and found to have significant antifungal activities.The antifungal proteins disclosed herein are useful in controlling fungal infections in plants. Transgenic plants may be produced that are more resistant to fungal infections relative to non-transgenic plants of the same species. Alternatively, the proteins may be applied to plants exogenously. ***** United States Patent: 7419667 United States Patent 7,419,667 Hatake , et al. September 2, 2008 -------------------------------------------------------------------------------- Drug for cancer therapy Abstract A lactoferrin hydrolysate mixture or lactoferrin partial peptide that can be obtained by hydrolyzing lactoferrin with a hydrolytic enzyme and has an action of enhancing cytotoxic activity of an antibody drug in an antibody therapy of cancer is used as an active ingredient of a drug for enhancing cytotoxic activity of an antibody drug in an antibody therapy of cancer. *********** The above patent is using Milk and Magnesium for a cancer therapy/cure. What is interesting as relates to Morgellons- is that many believe Morgellons to be Chronic Lyme-and with Lyme disease, Magnesium is depleted by the pathogen/s and therefore the sufferer needs to supplement the mineral. Given those variables- it seems it would be wise for those with Morgellons to drink lots of milk and supplement with magnesium. Couldn't hurt.... Venetia Last edited by Venetia; May 21st, 2009 at 02:43 PM. |
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| Unbelievable !!! Monsanto own us .WE are THEIR property. Monsatan have to be the most evil corporation ever . And they have reps in the White House. There are good men rotting in prison because they were curing cancer . ![]() |
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