A medication that can protect people exposed to normally lethal doses
of radiation from a nuclear or a "dirty" bomb has been developed,
In tests involving 650 monkeys exposed to radiation equivalent to that
recorded during the Chernobyl nuclear reactor disaster in 1986, 70 per
cent died while the rest suffered serious maladies, the newspaper Yediot Achronot
Of the group given anti-radiation shots, almost all survived and had no
side effects. A test on humans not exposed to radiation showed none
suffered side effects from the medication.
The medication was developed by Andrei Gudkov, chief scientific officer
at Cleveland BioLabs in the US. Also involved was Israel's Elena
"We made a breakthrough that may save the lives of millions," Dr Gudkov
was quoted as saying.
The medication has important implications in the treatment of cancer,
the report said, since it permits use of more powerful radiation.
If the medication is given final approval by the Food and Drug
Administration, which Dr Gudkov said would happen within two years, it
could have a strategic impact, particularly for nations threatened with
nuclear attack. Among the major fears in the West is not nuclear attack
but "dirty bombs", which kill mostly by radiation.
Dr Gudkov conceived the idea in 2003 of using protein produced in
bacteria found in the intestine to protect cells from radiation. "The
medication works by suppressing the 'suicide mechanism' of cells hit by
radiation," the newspaper said, "while enabling them to recover from
the radiation-induced damages that prompted them to activate the
suicide mechanism in the first place."
The medication is a preventative drug administered by one or several
Flagellin is a protein that arranges itself in a hollow cylinder to
form the filament in bacterial flagellum. It has a mass of about 30,000
to 60,000 daltons. Flagellin is the principal substituent of bacterial
flagellum, and is present in large amounts on nearly all flagellated
The structure of flagellin is responsible for the helical shape of the
flagellar filament, which is important for its proper function.
The N- and C-termini of flagellin form the inner core of the flagellin
protein, and is responsible for flagellin's ability to polymerize into
a filament. The central portion of the protein makes up the outer
surface of the flagellar filament. While the termini of the protein is
quite similar between all bacterial flagellins, the central portion is
Mammals often have acquired immune responses (T-cell and antibody
responses) to flagellated bacterium occurs frequently to flagellar
antigens. Some bacteria are able to switch between multiple flagellin
genes in order to evade this response.
The propensity of the immune response to flagellin may be explained by
First, flagellin is an extremely abundant protein in flagellated
Secondly, there exists a specific innate immune receptor that
recognizes flagellin, Toll-like receptor 5 (TLR5).
In addition a 22 amino acid sequence (flg22) of the conserved
N-terminal part of flagellin is known to activate plant defence
mechanisms. Flagellin perception in Arabidopsis thaliana functions via
the receptor-like-kinase, FLS2 (flagellin-sensitive-2)).
Mitogen-activated-protein-kinases (MAPK) acts as signalling compounds
and more than 900 genes are affected upon flg22 treatment.
Pre-stimulation with a synthetic flg22-peptide led to enhanced
resistance against bacterial invaders.
MeSH Heading -- Flagellin
Tree Number -- D12.776.097.380
Annotation - a bact protein
Scope Note -- A protein with a molecular weight of 40,000
isolated from bacterial flagella. At appropriate pH and salt
concentration, three flagellin monomers can spontaneously reaggregate
to form structures which appear identical to intact flagella.
J Immunol. 2001 Aug 15;167(4):1882-5
flagellin activates basolaterally expressed TLR5 to induce epithelial
proinflammatory gene expression.
Gewirtz AT, Navas TA, Lyons S,
Godowski PJ, Madara JL.
Epithelial Pathobiology Division, Department of Pathology and
Laboratory Medicine, Emory University, Atlanta, GA 30322, USA
Flagellin, the structural component of bacterial flagella, is secreted
by pathogenic and commensal bacteria. Flagellin activates
proinflammatory gene expression in intestinal epithelia. However, only
flagellin that contacts basolateral epithelial surfaces is
proinflammatory; apical flagellin has no effect. Pathogenic Salmonella,
but not commensal Escherichia coli, translocate flagellin across
epithelia, thus activating epithelial proinflammatory gene expression.
Investigating how epithelia detect flagellin revealed that cell surface
expression of Toll-like receptor 5 (TLR5) conferred NF-kappaB gene
expression in response to flagellin. The response depended on both
extracellular leucine-rich repeats and intracellular Toll/IL-1R
homology region of TLR5 as well as the adaptor protein MyD88.
Furthermore, immunolocalization and cell surface-selective
biotinylation revealed that TLR5 is expressed exclusively on the
basolateral surface of intestinal epithelia, thus providing a molecular
basis for the polarity of this innate immune response. Thus, detection
of flagellin by basolateral TLR5 mediates epithelial-driven
inflammatory responses to Salmonella.
METHODS OF PROTECTING AGAINST
RADIATION USING FLAGELLIN
relates to a method of protecting a mammal against radiation comprising
administering said mammal a composition containing flagellin.
Also published as: WO2005056042 // WO2005056055 //
WO2005056055 // WO2005057218
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