Science: Biology:

 

Two Notes on Progress in BSE-Crisis

by Professor Dr. Dr. hc Randolph Riemschneider

Berlin, Germany

 

 

Background: Bovine spongiform encephalopathy (BSE) and some other diseases like scrapie (sheep), Creutzfeldt-Jakob disease (human) and kuru (human) have one thing in common:

both are transmissible chronic degenerative diseases of the brain with characteristic changes of the brain structures.

 

It is estimated that between 1977 and 1995 over 900,000 British cattle were infected with the BSE agent, of which some 165,000 head in the United Kingdom developed BSE by the end of 1996, while the other animals were slaughtered before the outbreak of the clinical symptoms (commonly known as mad cow disease). Feeding infected bone meal is now considered the most important way of transmitting the pathogen. The question of whether the BSE derives from the scrapie of sheep and goats, or whether it has always occurred in cattle, is to date unresolved.

 

The pathogens are currently believed to be Prions. Prion according to Prosinger (1982), derived from Proteinaceous infectious particle: Prions are membrane-bound protein molecules which can self-replicate and lead to the formation of vacuoles of so-called amyloid plaques.

 

Evidences:

Chemical and physical processes which modify or degrade nucleic acids, do not destroy the agent’s infectivity. On the other hand, chemical and physical processes which modify or degrade proteins do destroy the agent’s infectivity; however, the thermic inactivation of, for example, BSE prions requires approx 18 minutes at 134-138°  C, with differences by breed in cattle. BSE prions are resistant to formalin; the usual heat sterilization with 70% alcohol does not achieve the aim. BSE agents resist ultraviolet or ionizing radiation which in viruses results in the complete destruction of their infectivity by damaging their genomes.

 

By reason of these characteristics, the American microbiologist Griffith in 1967 surmised that these pathogens could be pure proteins. Prusinger took this idea up at the end of the 70's and formulated the basis of the prion theory in 1982. It assumes that a pathologically reconfigured protein, the prion protein, is the infective agent, which postulates a fundamentally new class of pathogens (in addition to having a protein sheath, viruses also contain a core of DNA or RNA). There is as yet no conclusive proof of this theory.

 

There is also discussion about whether a virus, which only uses the prion protein as a receptor for entering the cell, could be responsible for these diseases. On the other hand, supporters of the virion theory postulate that a small viral nucleic acid is not surrounded by the virus’s own proteins but by prion protein. However, to date, it has not been possible to demonstrate such a pathogen-specific nucleic acid.

 

The function of the prions – now known as prion proteins (PrP) - is to date just as unclear as the mechanism of their infectivity. Their existence is no longer disputed. It is now recognized, even if not undisputed, that not bacteria or viruses - but rather these prions, a completely new type of pathogen – are responsible for causing these prion diseases, e.g. new variant Creutzfeldt-Jakob disease (nvCJD) in humans, bovine spongiform encephalopathy (BSE) in cattle, scrapie in sheep, and others.

 

Prions are the body’s own quite normal, non-vital proteins (PrP^c - c for cellular), whose function is still unclear. They occur in all tissues but are mainly located on the outer wall of nerve cells in the brain. They are harmless in their original physiological form and trigger no disease. They can only cause diseases when infective prions reconfigure them into harmful prions (so-called PrP^Sc - sc for scrapie-specific). The two isoforms PrP^c and PrP^Sc  differ only in their spatial structure, i.e. the way in which the prion amino acid chain is folded: a- helix structure or a-helix and b-folding structure.

 

It is assumed that a single PrP^Sc molecule, functioning as a template, docks onto a PrP^c and thus reconfigures it into the pathological form. These newly created PrP^Sc in their turn can supposedly affect the reconfiguration of normal PrP^c into PrP^Sc. Subsequently a sort of chain reaction commences which leads to an accumulation of PrP^c building blocks and finally results in the destruction of the nerve cells. This manifests itself as perforated, spongy brain tissue.

 

The body’s own healthy proteins, i.e. PrP^c, can be degraded and destroyed by proteases (not, however, the PrP^Sc pathogens) – an important prerequisite in the assumed infection via food, e.g. through BSE-infected meat.

 

The central event is the reconfiguration of a host-encoded amyloidogenic protein (PrP^c) into an abnormal isoform (PrP^Sc) which accumulates as amyloid in BSE brain.

 

 

 

Two Notes on Progress in BSE-Crisis:

 

I      Substitution of organ extracts prepared from fresh glands by BSE-free cell lines extracts

 

II   A new probiotic animal food additive based on plant material useful in BSE-crisis

 

 

I.   The BSE problem, which arose in Great Britain in 1985/86, has reached in the meantime most other European countries. Since December 2000, overseas countries have stopped the import of European animal material, medical and cosmetic preparations of bovine origin, including Asia, for instance, on December 12, 2000.

 

A way out has been offered by the author, who has developed a new manufacturing method for BSE-free organ extracts derived from BSE-free cell lines. In some publications (1,2) the author compared the analytical data of classic organ extracts derived from fresh glands with the new ones from cell lines. Practical experience with cell line based organ extracts has been collected in Asia for more than 10 years, e.g. medical remedies similar to Cellryl or cosmetic additives like Placenta or Thymus extracts. The new manufacturing method is secured by the author’s patents in Europe and overseas countries (2).

 

II.  To handle the animal feeding problem related to BSE the animal nutrition was changed as much as possible to vegetarian fodder and the use of antibiotics was limited. Useful can be the new plant based food additive H 2000 which was developed in the 80s and has been tried since. H 2000 is an environment friendly natural agent based on Actinomycetae cell preparations (3).

 

Extensive field experiments with more than 500,000 chickens, more than 300,000 piglets and cattle proved that H 2000 is useful in concentrations of 0.1%-0.2% concerning food saving and the health of the animals. These experiments were done at first in Brazil, then in the USSR, Poland, Hungary and Switzerland. Toxicological laboratory tests in the 80s and the positive results of the above mentioned field experiments prove the non-toxicity of H 2000.

 

How does it work? H 2000 is activating, in principle, energy producing reactions like cell-respiration and glycolysis so delivering more energy for all metabolic reactions consuming energy.

The patented manufacturing process does neither imply any chemistry nor does it use organic solvents.

 

References:

(1)   R. Riemschneider, Relata Technica Web Site http://www.very.com/relata, Issues, Articles 2001

(2)   For instance: DE 19624476 A I from Dec. 12, 1997 (69 pages)

(3)   R. Riemschneider: “The animal food additive H 2000” (1990); see APPENDIX

 

 

 

Appendix:

 

The animal food additive

H 2000

 

H 2000 is a new biological plant-based <<animal food additive>>, tested during the last ten years in large scale on chicken, pigs, sheep, calves, rabbits, dogs, etc. in many countries like Brazil, Japan, Poland, USSR, Hungary, Switzerland and Germany under the names:

-         Proval (Pro from probiotic, val from value) (Proval sometimes Socoproval)

-         H 2000 (H from Hefe)

-         Y (Y from yeast)

-         S 2000 (S from Saccaromyces cerevisiae).

The decisive viewpoint for the development of H 2000 was to use vegetal starting material.

Starting from yeast like Saccaromyces – applying several combined physical influences in the manufacturing process, we came to new << yeast cell-preparations >>, not anymore reproductive and not anymore fermentating, but activating the yeast-fermentation of glucose and activating the cell-respiration in a high degree: more scientifically spoken: activating anaerobic and aerobic reactions of the cell-metabolisms in general. H 2000 is really something new: H 2000 is not to be confused with the normal food-yeast which is used since long time as donator for proteins and B-vitamins.

 

H 2000 is added to animal food in very low concentration of 0,1%-0,2%. Such low concentrations are sufficient to activate the cell metabolism in different ways – so increasing the effectivness of foodstuff. The patented manufacturing process does not imply any chemistry, no organic solvents are necessary. H 2000 shows no toxicity. One not can observe any mortality determination DL50 mouse, using 15gr H 2000 pro kg mouse.

 

In the mentioned filed-experiments with thousands and thousands of chicken, hundreds of pigs and other animals – never was the observed mortality higher than in the control experiments, if any.

 

Activation of cell-metabolism by H 2000:

The cell-metabolism activation of H 2000 can be demonstrated: anaerobic by increased fermentation (I), aerobic by increased cell-respiration (II), for instance by WARBURG-method.

I:       Manometric measurement of increased CO2-production of fermenting yeast under H 2000 influence or

II:       Manometric measurements of increased O2 – consumption of liver homogenate under H 2000 influence.

 

      The activation of the anaerobic and aerobic cell-metabolism in cytoplasma and in mitochondriae means increasing the ATP-production of the cells. So more energy is available for all energy depending reactions. For instance more energy for synthetic reactions (protein biosynthesis), for catabolic reactions, energy for maintaining concentration-differences between the cell compartments etc.

 

The cell-metabolism-activation by H 2000 can also be demonstrated by growth experiments in laboratory-tests with guppy-fish or with tadpoles (Xenopus), or in practical animal nutrition experiments.

 

 

BWW Society Member Dr. Randolph G.A. Riemschneider is a graduate of the University of Berlin and has a carer of more a than half-century of scientific research. His areas of study include Polyacyl Chemistry, specifically o-Diacetylbenzene; his other research areas include work with natural, synthetic and cell-cultured BSE-free organ extracts. Metabolism activation, stereochemistry and other specialized work.