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Anti-Microbial Peptide Hypothesis Published in 2006

Posted by Eli-Kammerman on 02 Apr 2010 at 16:51 GMT

My 2006 publication (excerpt below) explicitly described Aβ as an antimicrobial peptide based on its multiple similarities to melittin.

In addition, the described antimicrobial action was explicitly cited as a basis for Aβ to be considered a component of the innate immune system, likely as a rapid response to infections by enveloped viruses such as HSV.

Excerpt from Kammerman et al., 2006:

"Numerous groups have reported that Aβ42 can disrupt lipid membranes by creating pore-like holes (ion channels) within the membranes. This property of Aβ42 appears to be related to an antimicrobial function; nature is replete with examples of peptide antimicrobials that effect their function through membrane disruption. In fact, some of these peptides show strong activity against HSV-1. For example, melittin, which has an α-helical amphipathic structure similar to Aβ42, has anti-HSV activity. We assert that β amyloid, by virtue of its similar molecular shape and size, is a peptide antimicrobial component of the innate immune system which [...continued] can neutralize enveloped viruses such as HSV-1. We contend accordingly that ion-channel pore formation in the HSV-1 envelope generated by Aβ42 is virucidal."

References:
Kammerman EM, Neumann DM, Ball MJ, Lukiw W, Hill JM. Senile plaques in Alzheimer's diseased brains: possible association of beta-amyloid with herpes simplex virus type 1 (HSV-1) L-particles. Med Hypotheses. 2006;66(2):294-9.

No competing interests declared.
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