24 May 2012
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Natural Remedies
"Bacterial/Viral Coinfections";
TLR2 (fungi)Signaling Depletes IRAK1 and Inhibits Induction of Type 1 by TLR7/9 (viruses)-- -CV Harding, 2012 (More in the chart at the bottom of this homepage)
"Multiple Mechanisms of Immune Suppression by B Lymphocytes" (New and Trashes Yale and IDSA)
NIH's Treatment Recommendations for Chronic Active Epstein-Borreliosis, the chronic illness also induced by OspA vaccination or exposure to molds.
ELISA = arbitrary cutoff.
Disclaimer
1998, CIA Oilmen & Israelis plan to overthrow Saddam for the oil.
Bush/Gore Oil/War-(Oct,2000)
Bush's own explainer (Oct
2000) re:
Iraq Oil
rOSPA WAS NOT A VACCINE
1) Yale did not demonstrate that there were not spirochetes in the ticks:
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=1608951&dopt=Abstract
A) Elimination of Borrelia burgdorferi from vector ticks
feeding on OspA-immunized mice.
Fikrig E, Telford SR 3rd, Barthold SW, Kantor FS, Spielman A, Flavell RA.
Proc Natl Acad Sci U S A. 1992 Jun 15;89(12):5418-21.
B) Barbour, 1986, "The Biology of Borrelia Species"-- Borrelia pinch off, or bleb-off the antibody-bound Osp.
C) Barbour, Patent # 6,296,849 "
The morphologic changes observed with class A mAbs were similar to what was
observed when bactericidal antiborelial antibodies were used (Coleman et al.,
1992; Sadziene et al., 1994). Class A mAbs were associated with a homogeneous
patchy pattern of binding to whole cells and little fluorescent staining of the
background.
In contrast class B mAbs in the wet IFA did not produce staining of single whole
cells. Instead it was associated with numerous fluorescent spots in the
background. By GIA class A antibodies were inhibitory at dilutions of
hybridoma supernatant of 1:256-2048; class B mAbs inhibited growth only at
dilutions of supernatants of 1;16 or lower. Both class A and B mAbs inhibited
the growth of B311 at a dilutions of 1:16 or 1:32, but not at higher dilutions.
None of the antibodies inhibited the growth of B. hermsii. When 1 HU of guinea
pig complement was added, it did not increase the inhibitory effect of either
class of mAb against B313 cells."
http://aac.asm.org/cgi/reprint/39/5/1127.pdf
D) Effects of penicillin, ceftriaxone, and doxycycline on
morphology of Borrelia burgdorferi.
Kersten A, Poitschek C, Rauch S, Aberer E.
Antimicrob Agents Chemother. 1995 May;39(5):1127-33.
E) The Scientist, Vol:10, #14, pg.13, July 8,
1996)
(Copyright, The Scientist, Inc.)
Many researchers believe that the secret to B. burgdorferi's infectivity and
inflammatory capacity lies in the
interaction of its surface proteins with the host's immunological system. **Yale
researcher Stephen Barthold, a
veterinarian and professor of comparative medicine who developed the first mouse
model of Lyme disease, studies the
expression of B. burgdorferi surface proteins throughout various stages of the
spirochete's life cycle. He finds that
during the early stages of infection, B. burgdorferi avoids immune detection by
decreasing its expression of surface
proteins or cloaking its expressed surface proteins under a layer of slime.
"It's using some sort of stealth-bomber-type
mechanism," he says. Or, using another diversionary tactic called blebbing, the
spirochete can pinch off bits of its
membrane in order to release its surface proteins. Explains Barbour:
"It's like s bscterial Star Wars defense program,"
in which released surface proteins might intercept incoming host antibodies,
keeping the spirochete safe from
immunological attack.**
================
2) To assess outcomes, use chromosomally and not plasmid-coded DNA:
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8234271&dopt=Abstract
Borrelia burgdorferi is clonal: implications for taxonomy
and vaccine development.
Dykhuizen DE, Polin DS, Dunn JJ, Wilske B, Preac-Mursic V, Dattwyler RJ, Luft
BJ.
Proc Natl Acad Sci U S A. 1993 Nov 1;90(21):10163-7.
===============
3) rOspA vaccination results in escape mutants or variants spirochetes which INCREASE at a greater rate than normal.
Selection of variant Borrelia burgdorferi isolates from
mice immunized with outer surface protein A or B.
Fikrig E, Tao H, Barthold SW, Flavell RA.
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=7729870&dopt=Abstract
================
4) Experiments in vitro in which complement is added demonstrate the antibodies to rOspA alone do not kill the spirochetes:
Borrelia burgdorferi escape mutants that survive in the
presence of antiserum to the OspA vaccine are killed when complement is also
present.
Sole M, Bantar C, Indest K, Gu Y, Ramamoorthy R, Coughlin R, Philipp MT.
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=9596714&dopt=Abstract
===================
5) OspA vaccination was not demonstrated to protect monkeys from infection:
The outer surface protein A (OspA) vaccine against Lyme
disease: efficacy in the rhesus monkey.
Philipp MT, Lobet Y, Bohm RP Jr, Roberts ED, Dennis VA, Gu Y, Lowrie RC Jr,
Desmons P, Duray PH, England JD, Hauser P, Piesman J, Xu K.
Vaccine. 1997 Dec;15(17-18):1872-87.
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=9413097&dopt=Abstract
====================
6) rOspA vaccination did not protect rabbits:
Comparison of protection in rabbits against host-adapted
and cultivated Borrelia burgdorferi following infection-derived immunity or
immunization with outer membrane vesicles or outer surface protein A.
Shang ES, Champion CI, Wu XY, Skare JT, Blanco DR, Miller JN, Lovett MA.
Department of Microbiology and Immunology, Department of Medicine, School of
Medicine, University of California, Los Angeles, California 90095, USA.
"Analysis of the antibody responses to outer membrane proteins, including DbpA, OspA, and OspC, suggests that the remarkable protection exhibited by the infection-immune rabbits is due to antibodies directed at antigens unique to or markedly up-regulated in host-adapted B. burgdorferi."
Natural infection was better in infection-immune rabbits, because of adaptation to antigenic variation.
===========================
7) OspA was not shown to protect mice, and why, by Russell Johnson:
Resistance to tick-borne spirochete challenge induced by
Borrelia burgdorferi strains that differ in expression of outer surface
proteins.
Kurtti TJ, Munderloh UG, Hughes CA, Engstrom SM, Johnson RC.
Infect Immun. 1996 Oct;64(10):4148-53
There was no reduction of strain 297 spirochetes in ticks that fed on four hamsters immunized with M297, but the hamsters were protected.
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8926082&dopt=Abstract
The journal publications of Russell Johnson--> MEDLINE: "Johnson RC [au] and spirochete"
=========================
8) Other lipoprotein vaccine failures and activation of latent infection:
The 19-kD antigen and protective immunity in a murine
model of tuberculosis.
Yeremeev VV, Lyadova IV, Nikonenko BV, Apt AS, Abou-Zeid C, Inwald J, Young
DB.
"These results are consistent with a model in which the presence of the 19-kD protein has a detrimental effect on the efficacy of vaccination with live mycobacteria."
Mycobacterium tuberculosis 19-kilodalton lipoprotein inhibits
Mycobacterium smegmatis-induced cytokine production by human macrophages in
vitro.
Post FA, Manca C, Neyrolles O, Ryffel B, Young DB, Kaplan G.
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11179309&dopt=Abstract
The 19-kDa lipoprotein of M. tuberculosis,
expressed in M. vaccae or M. smegmatis (M. smeg19kDa), abrogates this protective
immunity....Thus, the immunosuppressive effect is dependent on glycosylated and
acylated 19-kDa lipoprotein present in the phagosome containing the
mycobacterium. These results suggest that the diminished protection against
challenge with M. tuberculosis seen in mice vaccinated with M. smegmatis
expressing the 19-kDa lipoprotein is the result of reduced TNF-alpha and IL-12
production, possibly leading to reduced induction of T-cell activation.
============
Benach and Radolf → Extremely high titers of OspA- antibody are necessary to be protective
==================
POST LYMErix SYNDROME
Vaccination with lipoprotein vaccines exacerbate infection and make the disease undetectable.
The evidence from the vaccine trial and adverse events reported afterwards, suggests rOspA activates latent infections.
OspA is biologically active in the free form (1). OspA binds Plasminogen, an enzyme which degrades membranes
OspA induces the expression of the anti-inflammatory cytokine IL-10 (2)
Borreliosis, itself, is associated with activation of Epstein-Barr virus (3).
Epstein-Barr virus is associated with B cell changes. Borreliosis is associated with B cell changes. (Dorward, Spleens ) Giving asymptomatically infected Borreliosis patients the vaccine therefore appears to have created a disaster, not the least of which is new neoplasms, not reported in this abstract, and likely not reported to the World Health Organization, because Yale wrote that they scewed the results to fit into WHO's adverse events listing.
Mycoplasmal lipoprotein vaccine have failed to protect, in Tuberculosis. The lipoproteins seem to be related to fungi. Indeed, the mycoplasmal lipoproteins of 19 and 35 kD tried as vaccine in tuberculosis seem to have the same negative effects as OspA
"Thus, the immunosuppressive effect is dependent on glycosylated and acylated 19-kDa lipoprotein present in the phagosome containing the mycobacterium. These results suggest that the diminished protection against challenge with M. tuberculosis seen in mice vaccinated with M. smegmatis expressing the 19-kDa lipoprotein is the result of reduced TNF-alpha and IL-12 production, possibly leading to reduced induction of T-cell activation."
=========
OspA and IL-10: MEDLINE
ActionLyme, 2001, Vaccine Presentation of Empirical Results, and that OspA was not a vaccine. It was not qualified with a valid standard http://www.fda.gov/ohrms/dockets/ac/01/slides/3680s2_11.pdf
Pam Weintraub: http://www.whale.to/m/lymerix8.html
LYME FOUNDATION Re LymeRIX
LYME ASSOCIATION Re: LymeRIX
==============================
1) Binds a human degradive enzyme plasminogen and is active in the free form:
Infection 1996 Mar-Apr;24(2):190-4
The outer surface protein A (OspA) of Borrelia burgdorferi: a
vaccine candidate and bioactive mediator.
Kramer MD, Wallich R, Simon MM.
Institut fur Immunologie, Universitat Heidelberg, Germany.
In the search for a suitable vaccine candidate for Lyme borreliosis the
principles of protective immunity were studied in a murine model of Borrelia
burgdorferi infection. It was found that the spirochetal outer surface protein A
(lipOspA) in its native and recombinant lipidated form induces monospecific
immune sera, which in passive transfer experiments protect SCID mice against
experimental and tick-borne infection and disease. These and similar findings of
independent groups led to the development of a vaccine formulation containing
lipOspA. When tested in clinical phase I/II safety trials the recombinant
lipOspA vaccine was shown to be safe, immunogenic and able to elicit
borreliacidal antibodies. At present, clinical phase III efficacy trials are
being conducted. B. burgdorferi infection involves the dissemination of the
spirochetes from the site of the tick bite, infection of distant organs, and
induction of a chronic inflammatory process. Recent studies indicate that the
spirochetes may utilize host-derived enzyme systems to increase their
virulence/pathogenicity. It was found that lipOspA serves as a surface receptor
for the host-derived proteolytic enzyme plasmin(ogen), the central component of
the so-called plasminogen activator system. Moreover, it was found that
spirochetes are able to activate endothelial cells and blood-derived leukocytes,
such as monocytes/macrophages, B cells and T cells, to express functions and/or
secrete molecules, which are known to promote inflammatory responses. Part of these activities were exerted by
the isolated lipOspA. The studies indicate an important role of lipOspA, both for the
induction of a protective immune response by the host, as well as for the
pathogenic processes elicited during B. burgdorferi infection.
PMID: 8740121 [PubMed - indexed for MEDLINE]
Which means, who knows what's happening to people who receive this as vaccination if this mechanism is at work.
2) Induces the antiiflammatory cytokine IL-10 (suppresses the immune response).
People with Lyme borreliosis often test positive to Epstein-Barr. That is, IgM to Epstein-Barr apparently "cross-reacts"
with Borrelia burgdorferi OspC. That is, people who are infected with Borrelia, and who are "treated" to the CDC's
Dearborn serodiagnostic criteria, and therefore told they have Chronic Fatigue Syndrome (Chronic Epstein-Barr),
may have also activation of latent Epstein-Barr, as described here:
Interaction of Borrelia burgdorferi sensu lato with
Epstein-Barr virus in lymphoblastoid cells.
Hulinska D, Roubalova K, Schramlova J.
National Reference Laboratory on Borreliosis, Electron Microscopy, National
Institute of Public Health, Prague, Czech Republic.
Since the possibility of interruption of latent EBV infection has been suggested
by the induction of the lytic virus cycle with chemical substances, other
viruses, and by immunosuppression, we hypothesized that the same effect might
happen in B. burgdorferi sensu lato infection as happens in Lyme disease
patients with positive serology for both agents. We have observed EBV
replication in lymphoblastoid cells after superinfection with B. garinii and B.
afzelii strains after 1 and 4 h of their interaction. We found that viral and
borrelial antigens persisted in the lymphoblasts for 3 and 4 days. Morphological
and functional transformation of both agents facilitate their transfer to
daughter cells. Association with lymphoblasts and internalization of B. garinii
by tube phagocytosis increased replication of viruses more successfully than B.
afzelii and chemical inductors. Demonstration of such findings must be
interpreted cautiously, but may prove a mixed borrelial and viral cause of
severe neurological disease.
PMID: 12630667 [PubMed - in process]
3) "Blot-smudging" The question that arises is, if OspA is "sticky" (according to an Alan Barbour patent), how can we be sure free OspA molecules are the actual immunogen a person is injected with, if the outcome, in antibodies, is as below? It appears that clumps of OspA of various sizes are being injected into people. And if OspA is the reactive molecule it is claimed to be, how do we know it is not causing Immune complex vasculitis?, as part of the Post-LYMErix Syndrome?
This same thing occurred in the Monkey trials of rOspA. It was not reported that this problem was addressed in the Human Trials..
http://www.journals.uchicago.edu/CID/journal/issues/v31n1/991200/991200.html
Figure 1. Results of
Western blotting (MarBlot for detection of IgG antibody
to Borrelia burgdorferi; MarDx, Carlsbad, CA) of
serum specimens from 14 recipients of the recombinant
outer surface protein A Lyme disease vaccine.
Representative molecular weights (in kDa) are identified
in the far left column. P, a positive
control subject with PCR analysis positive
Lyme arthritis; N, a negative control subject.
Study subjects 110:
A, baseline; B, 30 days after dose 3.
Study subjects 1114:
A, baseline; C, 30 days after dose 2;
D, 8 months after dose 3; E, 24 months
after dose 3.
|
Clinical Infectious Diseases 2000;31:42-47
© 2000 by the Infectious Diseases Society of America. All rights reserved.
1058-4838/2000/3101-0010$03.00
Detection of Multiple Reactive Protein Species by Immunoblotting after Recombinant Outer Surface Protein A Lyme Disease Vaccination
Philip J. Molloy,1,2 Victor P. Berardi,2 David H. Persing,2,3,a and Leonard H. Sigall4
1Rheumatology Associates of Southeastern Massachusetts, Plymouth, and 2IMUGEN, Norwood, Massachusetts; 3Department of Laboratory Medicine and Pathology, Mayo Clinic, Rochester, Minnesota; and 4Division of Rheumatology, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, New Brunswick
Received 31 August 1999; revised 3 December 1999; electronically published 17 July 2000.
| Laboratory confirmation of the diagnosis of Lyme disease
is based on the detection of an immune response
to Borrelia burgdorferi. The serodiagnosis of B.
burgdorferi infection is complex and may be
further confounded by the immune response to the
recombinant outer surface protein A (OspA) Lyme
disease vaccine. To describe how the serological response
to the recombinant OspA Lyme disease vaccine affects
testing for antibody to B. burgdorferi, 240
specimens from 80 study subjects were obtained at
defined intervals after recombinant OspA Lyme disease
vaccination. Samples were tested by indirect enzyme-linked
immunosorbent assay (ELISA), antibody capture enzyme
immunoassay (EIA), and Western blotting (WB). After
recombinant OspA Lyme disease vaccination, ELISA for
98% of the study subjects revealed reactivity. WB with
use of OspA-containing B. burgdorferi strains as sources
of antigens demonstrated multiple bands. Results of testing
with a US Food and Drug Administrationapproved
WB kit showed homogeneous reactivity in the molecular
weight region >30 kDa. Testing with OspA-free strains
completely eliminated all vaccine-associated reactivity
by both antibody capture EIA and WB.
|
For collection of serum samples, there
was separate institutional review board approval, and informed
consent was obtained from the study subjects.
Guidelines for human experimentation of the US
Department of Health and Human Services and/or those of
the authors' institutions were followed in the conduct of
the clinical research.
a Current affiliation:
Corixa Corporation Infectious Disease Research Institute,
Seattle Life Sciences Center, Seattle, WA.
Reprints or
correspondence: Victor Berardi, IMUGEN,
220 Norwood Park South,
Norwood, MA 02062 (vberardi@imugen.com).