Red Algae Extract Fights Ebola ... and HIV, SARS and HCV
While researchers scramble to develop a vaccine or monoclonal antibody against the Ebola virus – ...
While researchers scramble to develop a vaccine or monoclonal antibody against the Ebola virus – and continue to develop chemo treatments to stem HIV and Hepatitis-C while fearing SARS – nature has already provided a natural treatment.
Research has shown that a healthy strong immune system can allow a person to not only avoid contracting the disease – but become resistant to it as well.
For those of us who need help or extract assurance, red algae proves to provide a key antiviral.
Hunting Natural Immunity For Ebola
After the two 1996 Ebola outbreaks in Gabon Africa, medical scientists determined that about Ebola causes death among about 70 percent of those who contracted the virus.
This question led researchers from Gabon’s Franceville International Center of Medical Research to investigate. The questions ensued: Why don’t the other 30 percent die? How do 30 percent of those infected recover?
Furthermore, medical researchers found many instances where there were close contacts of those who became infected who never were infected at all. Even though they were in contact with the infected patient while the patient was symptomatic.
Note: An infected patient with Ebola must be symptomatic in order to be contagious – with fever and other flu-like symptoms. A person must also have direct mucosal or blood contact in order to become infected with the virus. This means a transfer of saliva, urine, semen or blood from one person to another.
Thus, when the researchers investigated “close contact” individuals, they focused upon those who had this sort of exposure
The research found that nearly half of those who were asymptomatic and seemingly immune developed antibodies (IgM and IgG) to the Ebola virus.
This means these individuals certainly were intimately exposed to the virus, but simply naturally developed the immunity tools – including those discussed below – that prevented the infection from replicating out of control.
Furthermore, the asymptomatic group exhibited greater anti-inflammatory responses in general. They were found to have higher levels of circulating cytokines and chemokines – which speed up the body’s natural ability to break down the viral cells and stop their activity within the body.
“Asymptomatic individuals had a strong inflammatory response by high circulating concentrations of cytokines and chemokines.”
Mannose-Binding Lectins Attack Ebola Virus
The particular mechanism with which the body naturally breaks down and prevents infection from lethal infections including Ebola, HIV, HCV and SARS has gradually emerged.
The mechanism is called mannose-binding lectins. Mannose-binding lectins are apparently produced in the human body via a DNA sequence, called the MBL2.
When this part of our genes is in order, the body will produce and release these mannose-binding lectins into the bloodstream. Mannose-binding lectins will then recognize and glom onto certain carbohydrate molecules that cover and make up various microorganisms.
These include fungi, bacteria and even parasites, which utilize glycoprotein shells to protect themselves. But they also include viruses. Once the lectins attach to these shells, they will break apart the surface of the microbe and basically break them down, allowing the body’s other immune cells to kill off the microbe and prevent it from replicating.
In fact, a healthy body that produces good levels of these mannose-binding lectins will be able to easily fight off colds and flus, as well as other microbial infections. Several animal studies have shown mannose-binding lectins heartily beat down coronaviruses and infectious bronchitis.
Research over the past five years has found that low levels of mannose-binding lectins increases the risk of respiratory infections, including syncytial virus infections, pneumonia and others.
For example, in a study of 121 children, RSV-infections were associated with low levels of mannose-binding lectins. Nearly 70 percent of RSV-infected children had low levels of mannose-binding lectins. But other infections – especially those related to bacterial infections – are not necessarily connected with mannose-binding lectin levels.
When it comes to virulent infections such as Ebola, Hepatitis C and HIV, however, these are different. These viruses come with glycoprotein shells that protect the virus from being broken down.
Furthermore, the glycoprotein shell of the Ebola virus produces glycoproteins that damage cells, allowing the virus to penetrate and replicate within the cell.
Mannose-binding lectins actually break down this shell and the glycoprotein matrix through a mechanism called the lectin pathway.
Humans that don’t produce enough of these mannose-binding lectins are not only more susceptible because they don’t have enough lectins, but they are typically also immunosuppressed with regard to the rest of their immune system.
One of the reason some humans don’t produce enough mannose-binding lectins is because of a slight genetic mutation, where the MBL2 gene is switched off. The reason for this mutation/switch-off has yet to be fully understood. (Guess – something to do with our toxic environment and/or nutritional deficiency.)
Mannose-Binding Lectins From Red Algae
This brings us to the fun part. Yes, humans aren’t the only critters that produce mannose-binding lectins. Red algae also produce these profusely, which allow the algae to protect themselves from invasion by viruses.
The most promising form of mannose-binding lectins is a component of the Scytonema varium red algae called Scytovirin. The protein extract was isolated by researchers from the National Cancer Institute at Frederick, Maryland in 2003. The protein contains 95 amino acids, and was found to bind to HIV-1 viral shells.
A similar antiviral protein was found in Nostoc ellipsosporum – called Cyanovirin-N. Both of these antiviral proteins did similar things – they broke down the glycoprotein shells of HIV and HCV.
Yet another anti-viral extract was found from the New Zealand red alga species, Griffithsia sp. This protein is called Griffithsin, abbreviated with GRFT.