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Post by kammy on Jul 16, 2009 10:04:09 GMT -5
I believe this Serratia marcescens is also involved somehow... we'll have to wait to see what the other bacteria is in MM's report... How many of you have white pox marks on your skin - Jeany and I both have them on our arms?If we look at Serratia marcescens again... Serratia marcescens PathogenesisS. marcescens can cause infection in several sites, including the urinary tract, respiratory tract, wounds,[3] and the eye, where it may cause conjunctivitis, keratitis, endophthalmitis, and tear duct infections.[5] It is also a rare cause of endocarditis and osteomyelitis (particularly in people who use intravenous drugs recreationally), pneumonia, and meningitis.[2][3] Most S. marcescens strains are resistant to several antibiotics because of the presence of R-factors, which are a type of plasmid that carry one or more genes that encode resistance; all are considered intrinsically resistant to ampicillin, macrolides, and first-generation cephalosporins (such as cefalexin).[2] In elkhorn coral, S. marcescens is the cause of the disease known as white pox.[6] In silkworms, it sometimes occurs as a secondary pathogen in viral flacherie disease.[citation needed] In Drosophila (fly) research laboratories, infection with S. marcescens is common. It manifests itself as a pink discolouration or plaque in or on larvae, pupae, or the usually starch and sugar-based food (especially when improperly prepared)."
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Post by kammy on Jul 16, 2009 10:06:11 GMT -5
Doing a search on dogpile on "CBP21", I get this article, which shows the crystal nature of chitin: The Non-catalytic Chitin-binding Protein CBP21 from Serratia marcescens Is Essential for Chitin Degradation -- Vaaje-Kolstad et al. 280 (31): 28492 -- Journal of Biological Chemistry"The Gram-negative soil bacterium Serratia marcescens uses three different family 18 chitinases to degrade chitin, an abundant insoluble carbohydrate polymer composed of {beta}(1,4)-linked units of N-acetylglucosamine. We show that efficient chitin degradation additionally depends on the action of a small non-catalytic protein, CBP21, which binds to the insoluble crystalline substrate, leading to structural changes in the substrate and increased substrate accessibility. CBP21 strongly promoted hydrolysis of crystalline {beta}-chitin by chitinases A and C, while it was essential for full degradation by chitinase B. CBP21 variants with single mutations on the largely polar binding surface lost their ability to promote chitin degradation, while retaining considerable affinity for the polymer. Thus, binding alone is not sufficient for CBP21 functionality, which seems to depend on specific, mostly polar interactions between the protein and crystalline chitin. This is the first time a secreted binding protein is shown to assist in the enzymatic degradation of an insoluble carbohydrate via non-hydrolytic disruption of the substrate. Interestingly, homologues of CBP21 occur in most chitin-degrading microorganisms, suggesting a general mechanism by which chitin-binding proteins enhance chitinolytic activity. Homologues also occur in chitinase-containing insect viruses, whose infectiousness is known to depend on chitinase efficiency."
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Post by kammy on Jul 16, 2009 10:08:23 GMT -5
www.jbc.org/cgi/reprint/M504468200v1.pdf"Gram-negative soil-bacterium Serratia marcescens, known as one of the most effective microbial chitin degraders (4), produces three family 18 chitinases, ChiA, ChiB and ChiC (5-8). Like cellulases (9,10), chitinases, including ChiA, ChiB and ChiC, often contain one or more noncatalytic domains that are known to help in binding and degrading the insoluble substrate (11-14). Such domains are often referred to as carbohydrate-binding modules (CBMs1) and have been classified in the CAZY database ( afmb.cnrs-mrs.fr/CAZY/). In addition to being important for biomass turnover, chitin degradation is essential in a variety of biological processes. For example, plants are known to produce chitinases in response to attack by chitin-containing fungi (15), whereas some non-pathogenic fungi such as Trichoderma species are considered as “biocontrol” agents because of their ability to inhibit other, chitin-containing, fungi (16)." Jeany - didn't you mention the Trichoderma species of fungi? Derma - as in skin?
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Post by kammy on Jul 16, 2009 10:09:46 GMT -5
www.jbc.org/cgi/reprint/M504468200v1.pdf"Despite its resilience, insolubility and abundant production, chitin does not accumulate in most ecosystems, suggesting that nature has developed efficient processes for chitin degradation. Chitin is degraded by chitinases (EC 3.2.1.14) that belong to families 18 and 19 of the glycoside hydrolases ((2,3) afmb.cnrsmrs.fr/CAZY/ (*this link is not good - figures...) Chitinolytic enzymes have been detected in many microorganisms in both terrestrial and aquatic ecosystems."
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Post by kammy on Jul 16, 2009 10:12:27 GMT -5
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Post by kammy on Jul 16, 2009 10:14:56 GMT -5
QUOTE=Jeany Neem Products - Trichoderma Viride
Trichoderma Viride 1 % (2 X 106 cfu/gm. minimum) (Mother culture:- Tamil Nadu Agricultural University, Coimbatore) Talcum based formulation. Trichoderma viride is an antagonistic fungal organism present in the soil and is highly effective for the control of seed and soil borne diseases of majority of economically important crops, especially pulses and oilseeds. This biocontrol agent when applied along with seed, colonizes the seed and multiplies on the surface of the seed and kills not only the pathogens present on the surface of the seed but also gives protection against soil-borne pathogens until life time of crop by action of mycoparasitism and antibiosis. Seed treatment with Trichoderma viride has registered higher germination in a number of studies and was at par Captan. Its effective control of soil-borne diseases caused by Rhizoctonia solani, macrophomina phaseolina and Fusarium spp. makes it a very important weapon against diseases such as root rot, seedling diseases, charcoal rot, wilt, damping off, collar rot, etc.. The potential of Trichoderma viride in managing soil-borne pathogens has been demonstrated in many crop diseases like seedling disease of cotton (Ramakrishna and Jeyarajan, 1986; Aagarsamy et al., 1987a and b), root rot of soybean (Jharia and Khare – 1986), Root rot of Cowpea (Alagarasami Shivaprakasam. 1988), charcoal rot of sorghum (Sekhar and Analosur, 1986) and root rot of mung bean caused by Macrophomina phaseolina (Samiyyapan et al., 1987). Kam** haven't we seen a green mold in the dishes?Cotton??...soy beans?? Jeany
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Post by kammy on Jul 16, 2009 10:17:41 GMT -5
HOW TO KILL THIS? WE'VE GOT TO TERMINATE IT! Glycoside hydrolase Glycoside hydrolase - Wikipedia, the free encyclopedia"Glycoside hydrolases (also called glycosidases) catalyze the hydrolysis of the glycosidic linkage to generate two smaller sugars. They are extremely common enzymes with roles in nature including degradation of biomass such as cellulose and hemicellulose, in anti-bacterial defense strategies (eg lysozyme), in pathogenesis mechanisms (eg viral neuraminidases) and in normal cellular function (eg trimming mannosidases involved in N-linked glycoprotein biosynthesis). Together with glycosyltransferases, glycosidases form the major catalytic machinery for the synthesis and breakage of glycosidic bonds. Occurrence and importanceGlycoside hydrolases are found in essentially all domains of life. In bacteria and prokaryotes, they are found both as intracellular and extracellular enzymes that are largely involved in nutrient acquisition. One of the important occurrences of glycoside hydrolases in bacteria is the enzyme beta-galactosidase (LacZ), which is involved in regulation of expression of the lac operon in E. coli. In higher organisms glycoside hydrolases are found within the endoplasmic reticulum and Golgi apparatus where they are involved in processing of N-linked glycoproteins, and in the lysozome as enzymes involved in the degradation of carbohydrate structures. Deficiency in specific lysozomal glycoside hydrolases can lead to a range of lysosomal storage disorders that result in developmental problems or death. Glycoside hydrolases are found in the intestinal tract and in saliva where they degrade complex carbohydrates such as lactose, starch, sucrose and trehalose. In the gut they are found as glycosylphosphatidyl anchored enzymes on endothelial cells. The enzyme lactase is required for degradation of the milk sugar lactose and is present at high levels in infants, but in most populations will decrease after weaning or during infancy, potentially leading to lactose intolerance in adulthood. The enzyme O-GlcNAcase is involved in removal of N-acetylglucoamine groups from serine residues in the cytoplasm and nucleus of the cell. The glycoside hydrolases are involved in the biosynthesis and degradation of glycogen in the body."
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Post by kammy on Jul 16, 2009 10:19:12 GMT -5
Glycoside hydrolase - Wikipedia, the free encyclopedia" ClassificationGlycoside hydrolases are classified into EC 3.2.1 as enzymes catalyzing the hydrolysis of O- or S-glycosides. Glycoside hydrolases can also be classified according to the stereochemical outcome of the hydrolysis reaction: thus they can be classified as either retaining or inverting enzymes.[1] Glycoside hydrolases can also be classified as exo or endo acting, dependent upon whether they act at the (usually non-reducing) end or in the middle, respectively, of an oligo/polysaccharide chain. Glycoside hydrolases may also be classified by sequence based methods. Sequence-based classificationSequence-based classifications are among the most powerful predictive method for suggesting function for newly sequenced enzymes for which function has not been biochemically demonstrated. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of more than 100 different families[2][3][4]. This classification is available on the CAZy(CArbohydrate-Active EnZymes) web site[5]. The database provides a series of regularly updated sequence based classification that allow reliable prediction of mechanism (retaining/inverting), active site residues and possible substrates. Based on three dimensional structural similarities, the sequence-based families have been classified into 'clans' of related structure. Recent progress in glycosidase sequence analysis and 3D structure comparison has allowed the proposal of an extended hierarchical classification of the glycoside hydrolases.[6]" **The bad link above was to the CAZY data base. UsesGlycoside hydrolases have a variety of uses including degradation of plant materials (eg cellulases for degrading cellulose to glucose, which can be used for ethanol production), in the food industry (invertase for manufacture of invert sugar, amylase for production of maltodextrins), and in the paper and pulp industry (xylanases for removing hemicelluloses from paper pulp). Cellulases are added to detergents for the washing of cotton fabrics and assist in the maintenance of colours through removing microfibres that are raised from the surface of threads during wear. In organic chemistry, glycoside hydrolases can be used as synthetic catalysts to form glycosidic bonds through either reverse hydrolysis (kinetic approach) where the equilibrium position is reversed; or by transglycosylation (kinetic approach) whereby retaining glycoside hydrolases can catalyze the transfer of a glycosyl moiety from an activated glycoside to an acceptor alcohol to afford a new glycoside. InhibitorsMany compounds are known that can act to inhibit the action of a glycoside hydrolase. Nitrogen-containing, 'sugar-shaped' heterocycles have been found in nature, including deoxynojirimycin, swainsonine, australine and castanospermine. From these natural templates many other inhibitors have been developed, including isofagomine and deoxygalactonojirimycin, and various unsaturated compounds such as PUGNAc. Inhibitors that are in clinical use include the anti-diabetic drugs acarbose and miglitol, and the antiviral drugs oseltamivir and zanamivir. Some proteins have been found to act as glycoside hydrolase inhibitors." See also * Mucopolysaccharidoses * Glucosidase * Lysozyme * Glycosyltransferase * Glycoside hydrolase family 1
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Post by kammy on Jul 16, 2009 10:21:44 GMT -5
QUOTE=Jeany
[/url]"][/video]
Kam was asked to play the main actor in Terminator Part 24!! lolcool She'll be back!!
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Post by kammy on Jul 16, 2009 10:24:07 GMT -5
quote=Jeany
Kam was asked to play the main actor in Terminator Part 24!!lolcool She'll be back!!
Kammy: HA HA! Yeah, this stuff isn't killing you, anymore... I've got to keep plugging along!...
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Post by kammy on Jul 16, 2009 10:25:20 GMT -5
I just spoke with Ms. McGyver on the phone. I initially told her that I was being treated for Pseudomonas aeruginosa. She took this information to her doctor.
From what she understood with her phone conversation with the nurse was that this is a combination of Pseudomonas aeruginosa AND Enterobacter cloacae.
!!!!!!!!!!!!!!!!! :eek:
(She has not spoken with her doctor yet, nor seen the paperwork, her doctor has prescribed Ciproflaxin and Bactrim.)
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Post by kammy on Jul 16, 2009 10:35:13 GMT -5
If we look at my last photos of what is believed to be PA... it looks like the white fuzzy cotton-like one lives inside of it. And if EC is involved... that possibly PA is birthing EC? That we're seeing a bacteria birth another bacteria and not a fungus...?
From the Photo Comparions thread:
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Post by kammy on Jul 16, 2009 10:37:02 GMT -5
Pseudomonas aeruginosa AND Enterobacter cloacae How did one of these get inside the other one, did this happen in nature inside our bodies? hmmm... let me look on a search of "Pseudomonas aeruginosa AND Enterobacter cloacae" and see what comes up? Pseudomonas aeruginosa AND Enterobacter cloacae - Dogpile Web SearchMy first stop is a pdf abstract that is very damning to someone... (put it on 100% to read it better). www.insinet.net/jasr/2007/848-852.pdfit shows where they 'married' PA and EC for the purpose of "used for controlling plant diseases and, also used to suppressing herbivorous insect pets." **INSECT PETS?... Yeah, that's what we have now! Enhancement of Enterobacter Cloacae Antagonistic Effects Against the Plant Pathogen Fusarium Oxysporium "Abstract: The present investigation aimed to enhance and producing high efficient antagonistic mycoparasites to control the soilborne plant pathogens F. oxysporum f. sp. sesame and F. oxysporum f. sp. vicia which cause root wilt disease. Hybrids of E. cloacae and P. aeruginosa were produced by fusion of the bacterial protoplasts." **We have a hybrid form of these bacteria.THERE THEY ARE!! THERE'S THE SPHERES IN our cultures we've been looking at all this time, they show a diagram of both of them on the second page (849)... THERE ARE TWO Different SPHERES that we've been looking at, as I suspected. Look how similiar they look to each other and to my photos. Look at Figure 1 on the second page of the above pdf abstract! Alright, so one is not 'birthing' the other - they co-exist side by side. It looks like from this diagram that EC is the one with the brown spot in it - then, PA is 'birthing' something that we have been calling a white, cotton 'fungus', as seen in my photos above. And this 'fungus' is what later goes to produce the fiber and 'carbon balls' networks as seen from previous photos. "Results presented in Table (1) and Fig. (2) show that no antagonistic effect was detected to any of the two strains when glucose was used as the source of carbon. This may reflects glucose repression to antagonistic gene(s) expression. Repression by glucose suggests that catabolite repression or the so-called glucose effect may be involved in the regulation of chitinase synthesis[26]."
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Post by ruth on Jul 16, 2009 11:42:36 GMT -5
i did the ciproflaxacin for a year and a half. i was pulsing with other abx. along the way with no effect on the M. complex.
i also did smz/tmp for a year and a half. i think it is the same as bactrim.
so i should have done them both at the same time!!!!!!!
kammy, none of the photos open for me. i've got to pick up a pc cleaner. it could be my pc. if others are able to open them.
so many recombinants released without thought of the future!
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Post by violet on Jul 16, 2009 11:57:39 GMT -5
i did the ciproflaxacin for a year and a half. i was pulsing with other abx. along the way with no effect on the M. complex. i also did smz/tmp for a year and a half. i think it is the same as bactrim. so i should have done them both at the same time!!!!!!! kammy, none of the photos open for me. i've got to pick up a pc cleaner. it could be my pc. if others are able to open them. so many recombinants released without thought of the future! Hi, Ruth and Kammy. I couldn't open them either. I got a message that the page didn't exist.
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Post by kammy on Jul 16, 2009 12:03:13 GMT -5
Pseudomonas aeruginosa AND Enterobacter cloacae Looking at the same pdf abstract, I see where their attempted fusion of these two bacteria did not obtain the best results. www.insinet.net/jasr/2007/848-852.pdf"P. aeruginosa and E. Cloacae Protoplast Fusion: In this work, in order to combine different mechanisms for fungal biocontrol, the protoplast fusion technique was performed between P. aeruginosa and E. cloacae. Protoplasts were induced from P. aeruginosa or E. cloacae cultures[23]. Results showed that 24 % of P. aeruginosa cells were converted to protoplasts comparing with 42 % of E. cloacae cells. The difference in protoplast induction efficiencies of both strains may reflect differences in their cell walls structure as mentioned by Hopwood,[13]. A mixture of 85 x 103 P. aeruginosa protoplasts and 19 x 103 of E. cloacae protoplasts was mixed with 25% PEG 6000. One hundred microliters of protoplast suspension were tested for hybrid fusants at 10 min interval. Fusants selection was done by inoculation on Pseudomonas medium supplemented with L-arabinose, and incubation at 41ºC for four days. Table 2 presented the best protoplast fusion efficiency which was in the first 10 min of the treatment, where about 94 fusants were found per sample tested. In 20 min incubation, the protoplast fusion efficiency reduced about 20 % where about 76 fusants were found per sample. Increasing the incubation to 30 min gave the least fusants efficiency where only about 39 fusants were obtained in 100μl sample, i.e. less than 60 % of the 10 min protoplast efficiency. These results may be due to that increasing incubation time increases the probability of more than two cells to fuse. This situation resulted in less viability and more instability of the fusants produced In four days several hybrid colonies were grown. They have been subcultured at the same incubation conditions for more than a week. No fusant was able to re-grow on the selective condition. These results could be an indication for unstable fusants. This could be the result of the huge genetic difference between the two parental genera, i.e., Pseudomonas and Enterobacter. These results are in agreement with what Dale has found, [6] that viable progeny will not be obtained unless the two parents are from closely related species and disagree with what Abdel-Salam et al.[1] had found where they could obtained stable intergeneric fusants between Bradyrhizobium japonicum and Rhizobium leguminosarum." **What's a 'protoplast'?
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Post by kammy on Jul 16, 2009 12:18:09 GMT -5
Something went 'whacky' with LB's system of posting URL's... I noticed this a couple of weeks ago... So, instead of me manually altering each photo link here is my photo progression study that shows in Example 1 - how - what is believed to be 'PA' is the mother and births a white, cotton-like 'fungus' - that later becomes the fiber / carbon ball network. This was a mini study I did to show the progression by isolating the particular parts of my (and what is being seen in others) Morgellons. Look at Example 1: This study is found in completion on page 25, post #'s 245, 246 & 247 at: www.morgellons-disease-research.com/Morgellons-Message-Board/morgellons-pictures/5024-kammys-photo-comparions-25.html(These are the same links cut and pasted from over there - but, will not work here. )
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Post by kammy on Jul 16, 2009 12:20:24 GMT -5
i did the ciproflaxacin for a year and a half. i was pulsing with other abx. along the way with no effect on the M. complex. i also did smz/tmp for a year and a half. i think it is the same as bactrim. so i should have done them both at the same time!!!!!!! kammy, none of the photos open for me. i've got to pick up a pc cleaner. it could be my pc. if others are able to open them. so many recombinants released without thought of the future! Yes, Ruth... I just finished 14 days of Ciproflaxin 750 mg. with also a topical to put on my ear... (QUORUM SENSING ANTIBIOTIC!) CIPROFLAXIN DID NOT PHASE THIS !!!!!!!!!
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Post by kammy on Jul 16, 2009 12:33:04 GMT -5
I have the samples of 3 other people out here that I have kept sealed in their mailing envelopes. I will culture these samples in the next day or so and see if we all have either EC or PA in common.
Now, that I can tell the difference in the two spheres I can now go back and look at the photos and see if one is present and the other is not.
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Post by kammy on Jul 16, 2009 12:41:24 GMT -5
Meg has recommended that I put silver soaked on gauze pads on my ear and this has helped, I believe, here's an abstract that supports this - wtg, Meg! Antimicrobial activities of silver dressings: an in vitro comparison jmm.sgmjournals.org/cgi/content/full/55/1/59"All five silver-impregnated dressings investigated exerted bactericidal activity, particularly against Gram-negative bacteria, including Enterobacter species, Proteus species and E. coli. The spectrum and rapidity of action, however, ranged widely for different dressings. Acticoat and Contreet had a broad spectrum of bactericidal activities against both Gram-positive and -negative bacteria. Urgotul silver showed variable antibacterial effects. It achieved a reduction of >100 000 c.f.u. ml–1 with Proteus vulgaris, E. coli, Enterobacter cloacae and P. aeruginosa at 24 h, but regrowth occurred for the two acinetobacters." **Urgotul silver ?
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