Originally published July 24 2005
Enzyme could help fight SARS
by Mike Adams, the Health Ranger, NaturalNews Editor
Researchers have found that the SARS virus binds to a blood pressure-regulating enzyme in the body, angiotensin-converting enzyme 2 (ACE2), and a study of rats suggested providing more of the enzyme could help fight the virus.
An enzyme that regulates blood pressure also is involved in infection by the SARS virus, a discovery that may lead to new ways of treating diseases that cause lung failure.
Learning how SARS (severe acute respiratory syndrome) became a deadly threat "possibly teaches us a lesson on how to actively fight so diverse and dreadful diseases as SARS, avian flu or the effects of such biotech weapons as anthrax," said Dr. Josef Penninger of the Institute of Molecular Biotechnology of the Austrian Academy of Sciences.
ADVERTISEMENT The research may have wider implications for a type of lung failure known as acute respiratory distress syndrome, Penninger reported in a communication to the journal Nature.
It can occur in cases such as sepsis, aspiration of gastric contents, pneumonia and both avian and human influenza.
Penninger and colleagues report in Monday's issue of Nature Medicine that, working in mice, they found that angiotensin-converting enzyme 2 (ACE2) is a crucial receptor for the SARS virus.
The result is disruption of the body's protective renin-angiotensin system, leading to respiratory distress syndrome as fluids seep into the air sacks.
SARS was first identified in 2003, originating in China and spreading rapidly to Asia, Canada and elsewhere.
The result was to protect mice from the lung failure effects of SARS.
A commentary by John Nicholls and Malik Peiris of the University of Hong Kong said the findings indicate that the potential therapeutic value of ACE2 and angiotensin 2 receptor inhibitors for acute lung injury will be a productive field for investigation.
But Peiris and Nicholls, who were not part of Penninger's team, said there are differences in the way SARS binds with human ACE2 and ACE2 in mice.
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