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ABSTRACT:
Carolyn Larabell, Steven Huber and Heike Winter have synthesized
a peptide that is capable, in a very specific manner, of changing
the organization ('bundling') of filamentous actin (F-actin)
in vitro and, importantly, also in situ. The synthetic peptide
(SS2), derived from the sequence of a plant-specific enzyme,
may prevent cell division by causing irreversible actin bundling
in situ. The synthetic peptide has also been demonstrated
to prevent the formation of "actin comet tails"
in vitro — the process that produces the motile actin
tail utilized by certain pathogenic bacteria (e.g. Listeria
monocytogenes) and viruses (Vaccinia) to travel from cell
to cell in their host without encountering the immune system.
These in vitro and in situ effects of the peptide suggest
potential approaches as a pharmaceutical drug to block cell
division of rapidly growing cells (i.e., cancer cells); to
block the rapid spread of certain highly pathogenic bacteria
that infect humans through contaminated foods; and to block
the spread of certain viral infections. This peptide may,
furthermore, be extremely useful in prevention of metastasis.
Finally, the synthetic peptide can also be useful as a tool
for basic research to study the role of the actin cytoskeleton
in various processes in vivo and in vitro.
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