Why Homeopathy needs prolonged treatment to eradicate deep rooted chronic diseases?

In chronic diseases, Homeopathy needs prolonged treatment to completely cure the disease. During the process of treatment, we observe the appearance of various symptoms of detoxification through various routes, which disturb the patients. These processes of elimination of toxins are generally irritating to the patients. But without these disturbing symptoms, the complete cure cannot be achieved.

But the homeopathic physicians face hurdles to convince the patients not to use any alternative treatment to suppress those discharges. The scientists of conventional medicine never accepted this hypothetical concept of homeopathy and helped the patients to use all possible measures to suppress the discharges. Only recently, in case of diarrheal diseases, they are advising the patients to help the process of discharge by oral rehydration therapy and prevented the use of anti-diarrheal drugs.  Otherwise, they never found any harm in using steroids which suppressed the immune system by giving relief to the sufferings caused by painful symptoms of detoxification.

A recent invention presented below will show that the bacteria or virus remain well protected against any possible attack from the members of immune system, the T-cell and the B-cell and remain unharmed and cause disease by producing toxins.

Up till now, we are told by the scientists that, the micro-organisms are responsible for acute diseases only. But the above invention will show that they are responsible for chronic diseases also. This concept was postulated by Hahneman by the concept of miasm as the cause of chronic diseases, which could not be explained by any scientific evidence.

 This invention will help us to make our patients convinced that such mighty viruses need persistent repeated and prolonged assault by the immune system to penetrate the barrier around the micro-organism. That type of vigorous repeated attack can only be applied by the repeated use of homeopathy drugs for a long period of time and by the method of selecting the drugs by symptom analogy, called similimum of homeopathy.

This will help the followers of homeopathy to explain many hypothetical concepts to establish homeopathy on a scientific ground.

How Bacteria Build Homes Inside Healthy Cells

ScienceDaily (Dec. 20, 2011) — Bacteria are able to build camouflaged homes for themselves inside healthy cells — and cause disease — by manipulating a natural cellular process.

 

Purdue University biologists led a team that revealed how a pair of proteins from the bacteria Legionella pneumophila, which causes Legionnaires disease, alters a host protein in order to divert raw materials within the cell for use in building and disguising a large structure that houses the bacteria as it replicates.

Zhao-Qing Luo, the associate professor of biological sciences who headed the study, said the modification of the host protein creates a dam, blocking proteins that would be used as bricks in cellular construction from reaching their destination. The protein “bricks” are then diverted and incorporated into a bacterial structure called a vacuole that houses bacteria as it replicates within the cell. Because the vacuole contains materials natural to the cell, it goes unrecognized as a foreign structure.

“The bacterial proteins use the cellular membrane proteins to build their house, which is sort of like a balloon,” Luo said. “It needs to stretch and grow bigger as more bacterial replication occurs. The membrane material helps the vacuole be more rubbery and stretchy, and it also camouflages the structure. The bacteria is stealing material from the cell to build their own house and then disguising it so it blends in with the neighborhood.”

The method by which the bacteria achieve this theft is what was most surprising to Luo.

The bacterial proteins, named AnkX and Lem3, modify the host protein through a biochemical process called phosphorylcholination that is used by healthy cells to regulate immune response. Phosphorylcholination is known to happen in many organisms and involves adding a small chemical group, called the phosphorylcholine moiety, to a target molecule, he said.

The team discovered that AnkX adds the phosphorylcholine moiety to a host protein involved in moving proteins from the cell’s endoplasmic reticulum to their cellular destinations. The modification effectively shuts down this process and creates a dam that blocks the proteins from reaching their destination.

The bacterial protein Lem3 is positioned outside the vacuole and reverses the modification of the host protein to ensure that the protein “bricks” are free to be used in creation of the bacterial structure.

This study was the first to identify proteins that directly add and remove the phosphorylcholine moiety, Luo said.

“We were surprised to find that the bacterial proteins use the phosphorylcholination process and to discover that this process is reversible,” he said. “This is evidence of a new way signals are relayed within cells, and we are eager to investigate it.”

The team also found that the phosphorylcholination reaction is carried out at a specific site on the protein called the Fic domain. Previous studies had shown this site induced a different reaction called AMPylation.

It is rare for a domain to catalyze more than one reaction, and it was thought this site’s only responsibility was to transfer the chemical group necessary for AMPylation, Luo said.

“Revealing that this domain has dual roles is very important to identify or screen for compounds to inhibit its activity and fight disease,” he said. “This domain has a much broader involvement in biochemical reactions than we thought and may be a promising target for effective treatments.”

During infection bacteria deliver hundreds of proteins into healthy cells that alter cellular processes to turn the hostile environment into one hospitable to bacterial replication, but the specific roles of only about 20 proteins are known, Luo said.

“In order to pinpoint proteins that would be good targets for new antibiotics, we need to determine their roles and importance to the success of infection,” he said. “We need to understand at the biochemical level exactly what these proteins do and how they take over natural cellular processes. Then we can work on finding ways to block these activities, stop the infection and save lives.”

A paper detailing their National Institutes of Health-funded work is published in the current issue of the Proceedings of National Academy of Sciences. In addition to Luo, Purdue graduate student Yunhao Tan and Randy Ronald of Indiana University co-authored the paper.

Luo next plans to use the bacterial proteins as a tool to learn more about the complex cellular processes controlled by phosphorylcholination and to determine the biochemical processes role in cell signaling.

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