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Outer Surface Protein A (OspA) is a triacylated lipoprotein, or Pam3cys.


See the illustration at right (below, on mobile) which shows the chemical structure. It's easy to see the three acyl groups: the three zigzag lines that are labeled in red. These acyl groups are fatty acids and are what make OspA immunogenic, and a toxin. 

Triacylated lipoproteins are managed by Toll-like receptors 2 and 1, together (TLR2/1), in the human immune system, as are fungal-type antigens. Use your PubMed to verify this independently. This helps make spirochetes different from regular bacteria, which are managed by TLR4.

OspA is on the blebs (the bits of outer surface) that are shed by spirochetes when they undergo antigenic variation. Antigenic variation is the process by which the organisms are able to evade the immune system. Alan Barbour once likened the process to "stealth-bombing."

In the image at left (below, on mobile) you can see that there are far more blebs than spirochetes, and those blebs are covered in these toxic, fungal-type lipoproteins.

All of this means the two people (or groups of people) who filed for the intellectual property with US and foreign patent databases owning the recombinant Osps as vaccines (Fikrig & Flavell and Alan Barbour), knew they would never work.  That is research fraud and defrauding the government.



Yale’s Erol Fikrig and Richard Flavell published an article in 1995 that says OspA won't work as a vaccine due to antigenic variation or “antibody selection pressure.”  They own the patent for LYMErix (OspA):

Yale’s Erol Fikrig and Richard Flavell, who own the patent for LYMErix (OspA), also own the only VALID method for diagnosing "Lyme disease" (US Patent 5,618,533), but they did not use this method to evaluate the LYMErix trial victims. 

CDC officer, former head of the NIH’s Rocky Mountain Bioweapons Lab, Dearborn Cryme perpetrator, and ImmuLyme OspA patent owner Alan Barbour, wrote this  (below), in 1992, about how OspA won’t work as a vaccine due to antigenic variation.  (You can also farm these organisms to be specific tissue-tropic, as well as “select” “mutants.”)
Alan Barbour now is a scientific advisor to the Bay Area Lyme Foundation, an organization that has raised a lot of money but still has not cured Lyme disease.

“Notwithstanding infrequent application for bacterial studies presently, there were compelling reasons to use in vitro antibody selection with Borrelia burgdorferi, the agent of Lyme disease. First, we had shown for the related species,/t hermsii, that an antiserum specific for one serotype could select for new serotypes in an isogenic population undergoing in vitro growth (20). The ability of polyclonal antisera and mAbs to agglutinate (21) and inhibit the growth of/g burgdorferi (21a) indicated that this was also possible with the Lyme disease agent. 


"Second, previous studies had shown antigenic differences in outer membrane proteins, OspA and OspB, between strains (21-26) and also true antigenic variation of these proteins within a strain (25, 27-30). If borreliae did “escape” killing (31), growth inhibition (32), or agglutination (21) by antibodies, it was likely that this was the consequence of antigenic variation. 

Third, the success of passive immunization with either polyclonal antisera or mAbs in protecting animals indicated that an in vitro study of antibody effects was relevant for studies of pathogenesis and immunoprophylaxis of Lyme disease (33-38). In the present study we demonstrate in vitro selection of antibody-resistant mutants of B. burgdorferi. Among the several escape mutants evaluated, four major phenotypic classes were identified, and for two classes genotypes were determined….”

Barbour also quoted a report where it’s possible to get multiple variants from infection with a single spirochete.

1951: Relapse Phenomena in Rats with a Single Spirochete



Many research groups have confirmed that OspA gums up the immunity works, causes immunosuppression and inhibits the natural process of programmed cell death which is supposed to limit infection. In fact, a group of Lyme cabal members published in December 2016:

“This finding suggests that there is redundancy in the ability of the innate immune system to recognize B. burgdorferi and/or that these components can activate pathways that produce anti-inflammatory cytokines……the anti-inflammatory [immunosuppressive] effects might be the more important function of TLR signaling.”

Lyme borreliosis

Allen C. SteereFranc StrleGary P. WormserLinden T. HuJohn A. BrandaJoppe W. R. HoviusXin Li

Paul S. Mead

Nature Reviews Disease Primers 2, Article number: 16090 (2016) doi:10.1038/nrdp.2016.90

For more data on OspA being immunosuppressive, see the Occam's Razor charge sheet or this handy search that we've performed for you on PubMed.