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» LymeNet Flash » Questions and Discussion » Medical Questions » San Fran...WHOA...2014 heads up!

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Author Topic: San Fran...WHOA...2014 heads up!
Marnie
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http://naturalunseenhazards.wordpress.com/2014/02/21/california-study-finds-ticks-infected-with-lyme-disease-and-a-new-pathogen-widespread-in-san-francisco-bay-area-rabies-reports- from-ca-fl-nv-nj-ny-tx-va/


"“People who have difficulty getting diagnoses – maybe this is involved, ” Salkeld said.

https://woods.stanford.edu/news-events/news/ticks-may-cause-double-trouble

Posts: 9430 | From Sunshine State | Registered: Mar 2001  |  IP: Logged | Report this post to a Moderator
Robin123
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Thx for posting this - yep, a study funded by a new nonprofit in the area due to so many residents getting Lymed. It's great to be able to refer to the study! What was surprising for me was their finding B miyamotoi here, which has also been found in S CA.

Other tick infection stats for the area:
SF, a couple percent, since 10 known infections acquired in the city
Santa Cruz and Monterey - 15-20%
Marin and East Bay - 5-10%
Sonoma and Napa - 15-20%
Mendocino - hotspots show 40% infected nymph ticks, highest in the state

Sadly, people are reporting tick bites on trails leading out to the ocean so gotta stay from touching the long grasses.

More good research to come out of this effort!

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Marnie
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Need to start an effort to help mate (and release at night) the WFL's!

Or...give persons succinate dehydrogenase BEFORE Bb forms its biofilm.


SQR (succinate dehydrogenase) catalyzes the oxidation of succinate to fumarate with the

***reduction of ubiquinone to ubiquinol.***

MitoQ starts the process. And it is perfect. Made in New Zealand. They have taken ubiquinone and attached it to a phospholipid that FUNCTIONS like phosphatidylcholine (one of Bb's lipoproteins), but is NOT.

Ubiquinol is the antioxidant.

In high doses, MitoQ acts as a pro-oxidant. In low doses it acts as an anti-oxidant.

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Robin123
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Marnie - I think this was meant for a different post?

I do like the top line however - maybe Stanford could grow and release the blue belly lizards as a project!

Posts: 13117 | From San Francisco | Registered: May 2006  |  IP: Logged | Report this post to a Moderator
Marnie
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Borrelia miyamotoi AND Bb have been found together in the ticks.

Let's look at B. Miyamotoi:

"Borrelia miyamotoi, a spirochete that is genetically related to the species of borrelia that cause relapsing fever, has been detected in

all tick species that are vectors of Lyme disease.

It was detected in Ixodes scapularis ticks from Connecticut

in 2001

and subsequently has been detected in all areas of the United States where Lyme disease is endemic.


...*antibody* against B. miyamotoi ***GlpQ protein***

(an antigen that is nonreactive to B. burgdorferi antibody)"
http://www.nejm.org/doi/full/10.1056/NEJMc1215469

GlpQ = glycerol degradation - (happens in the gluconeogenesis pathway!!!)

The transfer of choline

from the host to the bacterial cell surface

requires **glpQ*** in Haemophilus influenza

Haemophilus influenzae incorporates choline obtained from environmental sources onto its lipopolysaccharide as phosphorylcholine (ChoP).

The decoration of the bacterial surface with ChoP contributes to pathogenesis by

allowing for mimicry of the host.

As the main reservoir for choline in the host is

phosphatidylcholine,

we tested whether other choline-containing molecules associated with eukaryotic membranes could provide an

alternative source of choline.

H. influenzae was able to use glycerophosphorylcholine (GPC),

an abundant degradation product of phospholipids,

as efficiently as free choline.

Utilization of GPC ***required glpQ***,

which expresses an enzyme with glycerophosphodiester phosphodiesterase activity.

In the absence of free choline,

this gene was required for adherent H. influenzae to

obtain choline directly from epithelial cells in culture.

GlpQ therefore allows choline to be transferred

from the host

to the bacterial cell surface.

http://onlinelibrary.wiley.com/doi/10.1046/j.1365-2958.2001.02571.x/full

Now we have TWO spirochetes that obtain/steal OUR choline? One of Bb's proteins is phosphatidylcholine.


Need help posting pictures.

Bob...would you once again help post a picture - the one on the right under "figures" in the link below:

First make it bigger and then find GlpQ in the upper right side and pay very close attention to L-Lactate -> pyruvate (which Bb uses for protection and/or likely Ubiquinol shuttled off as UQH2).

http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0098367

Pyruvate protects Bb:

http://www.researchgate.net/publication/259589595_Pyruvate_Protects_Pathogenic_Spirochetes_from_H2O2_Killing

Now find:

Now... in the following link, also see the picture

http://en.wikipedia.org/wiki/Succinate_dehydrogenase

See Q->QH2 = UQ -> UQH2.

Bb looks to *export* succinate dehydrogenase (an enzyme, a protein).

I think the WFL overwhelmed it's export function.

"Secretion proteins.

SecA is impressive, with the highest E(g) score relative to all PHX genes of MYXXA. The gene also qualifies as PHX in most of the other δ genomes.

PHX = predicted highly expressed

The SecA gene is also PHX (predicted highly expressed) in Vibrio cholerae, E. coli, Synechocystis, Mycoplasma pneumoniae, Treponema pallidum,

Borrelia burgdorferi,

Aquifex aeolicus, and other bacteria.

The secretion pathway is used by many protein substrates.

The cellular destination of all secretory polypeptides is governed by a 20- to 30-residue amino-terminal sequence, the leader peptide, which also helps guide SecA binding to the substrate.

SecA, SecB, and SecG are all involved in

protein export
and chaperone activity.

Gram-negative bacteria also secrete a variety of proteins into the extracellular and periplasmic milieu mediated by the secretion apparatus of types I to IV. These proteins can also influence bacterium–host interactions.


http://www.pnas.org/content/103/30/11352.full

Succinate dehydrogenase (spit out when not needed) is an enzyme that belongs to oxioreductases which oxidize a substrate by a reduction reaction that transfers one or more hydrides (H−) to an electron receptor…in this case to FAD.

SQR executes a series of internal electron transfer reactions that

couple succinate oxidation to the reduction of ubiquinone, also known as coenzyme Q (Q):

succinate + Q (ubiquinone) → fumarate + QH2 (ubiquinol)

Wiki.

When L-lactate -> pyruvate (pyruvate protects Bb from H2O2), UQ -> QH2 = dihydroquinone (ubiquinol).

Geeze, I wish there was ONE NAME for the same thing(s)!

Backing up a second:

There are three redox (= transfer of electrons – one thing loses electrons, another gains them) states of CoQ10:

***fully oxidized (ubiquinone)***,

semiquinone (ubisemiquinone),

and fully reduced (ubiquinol UQH2, the antioxidant).

The capacity of this molecule to exist in a completely oxidized form and a completely reduced form enables it to perform its functions in the electron transport chain, and as an antioxidant, respectively.

Very recent research indicates ***CoQ10 works WITH vitamin K2***…NOT vitamin K - K2 is a different FORM OF vitamin K which has entirely different functions (not blood clotting). Yes, vitamin K2 IS available as a supplement!

Wiki. What would I do without Wiki?!

Lyme = mitochondrial dysfunction (very common in MANY diseases!) Help out your cells powerhouses.

[ 07-21-2014, 06:36 PM: Message edited by: Marnie ]

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