Fw: Fwd: [ISSInstitute] MAD COW, AIDS (and ALZHEIMERS): Caused by the same protein: MYCOPLASMAS

[Guest guest]

-

Boyd Graves

editor

Monday, January 19, 2004 1:42 PM

Re: Fwd: [iSSInstitute] MAD COW, AIDS (and ALZHEIMERS): Caused by the

same protein: MYCOPLASMAS

 

 

 

 

Boyd Graves <boyded2003 wrote:

 

 

 

 

> ATTACHMENT part 2 message/rfc822

" Dr. Pierluigi Gambatti " ,

lederman.michael,

" Dr. Robert Gallo " , bhahn,

duesberg, hgoldste,

 

Boyd Graves

Sun, 18 Jan 2004 09:49:40 -0800 (PST)

[iSSInstitute] MAD COW, AIDS (and ALZHEIMERS): Caused by the same

protein: MYCOPLASMAS

 

 

Dr. Pierluigi Gambetti, Director

National Prion Disease Pathology Surveillance Center

Case Western University

 

re: HIV and MAD COW

 

Dear Dr. Gambatti:

 

Today an article about your center appeared ont he fromt page of the Clevenad

Plain Dealer, " On the Trail of Brain Killers " by Plain Dealer reporter Regina

McEnery.

 

Are you aware of the association of mycoplasmas as the causative agent that

allows for the " colonization " (build up of particles) on the brain? It is odd

that we are still not able to talk about the building block of dementia as it

correlates through all of the brain killer diseases. The very fact that the

United States studied " kuru " in the 1940's (The research of Carlton Gajdusek) is

indicative of the extent of the medical conspiracy being perpetrated by the

United States and the pharmaceutical industry.

 

The protein linked to MAd COW is a mycoplasma. The protein linked to AIDS is a

mycoplasma. As we go further you will find the mycoplasma (protein) at the heart

of many chronic diseases including multiple sclerosis.

 

I offer the following science abstract as our opening salvo regarding the

connection between MAD COW and HIV. It is our summation that if we concentrate

on wiping out the mycoplasma we can solve, possible cure many of the chronic man

made diseases that plague human society today. Our best science evidence of the

man made nature of HIV is the " research logic " flowchart of the mostly secret,

U.S. Special Virus program. See, www.boydgraves.com/flowchart/ . The blueprint

for making AIDS is page 61 of progress report #8 (1971) of the secret, federal

virus development program. The preceding sixty pages answer every question as to

how the United States sought to make a 'candidate' " special " virus. Several of

the progress reports of t he secret program are located in the government

documents section of our main library.

 

The " full disclosure " of the U.S. Special Virus program would save millions of

lives and billions of research dollars. We trust your interests in this research

area will require you to respond to this email or via phone. I am in Cleveland

Heights 216-382-9252. Our colleagues have posted their reviews here:

www.boydgraves.com/comments/ .

 

I look forward to speaking and collaborating with you. Sincerely, Boyd Ed

Graves, J.D., DIRECTOR-AIDS CONCERNS, the Common Cause International Medical

Research Foundation, Don Scott, President 705-670-0180 Sudbury, Ontario, Canada.

 

Identification of a common sphingolipid-binding domain in Alzheimer, prion,

and HIV-1 proteins.

 

Mahfoud R, Garmy N, Maresca M, Yahi N, Puigserver A, Fantini J.

 

Institut Mediterraneen de Recherche en Nutrition, Unite Mixte de

Recherche-Institut National de la recherche Agronomique 1111, Faculte des

Sciences St-Jerome, 13397 Marseille Cedex 20, France.

 

The V3 loop of the human immunodeficiency virus (HIV)-1 surface envelope

glycoprotein gp120 is a sphingolipid-binding domain mediating the attachment of

HIV-1 to plasma membrane microdomains (rafts). Sphingolipid-induced

conformational changes in gp120 are required for HIV-1 fusion.

Galactosylceramide and sphingomyelin have been detected in highly purified

preparations of prion rods, suggesting that the prion protein (PrP) may interact

with selected sphingolipids. Moreover, a major conformational transition of the

Alzheimer beta-amyloid peptide has been observed upon interaction with

sphingolipid-containing membranes. Structure similarity searches with the

combinatorial extension method revealed the presence of a V3-like domain in the

human prion protein PrP and in the Alzheimer beta-amyloid peptide. In each case,

synthetic peptides derived from the predicted V3-like domain were found to

interact with monomolecular films of galactosylceramide and sphingomyelin at the

air-water interface. The V3-like domain of PrP is a disulfide-linked loop

(Cys(179)-Cys(214)) that includes the E200K mutation site associated with

familial Creutzfeldt-Jakob disease. This mutation abrogated sphingomyelin

recognition. The identification of a common sphingolipid-binding motif in gp120,

PrP, and beta-amyloid peptide underscores the role of lipid rafts in the

pathogenesis of HIV-1, Alzheimer, and prion diseases and may provide new

therapeutic strategies.

 

PMID: 11792705 [PubMed - indexed for MEDLINE]