GAINESVILLE, Ga. (AP) — Four men in Georgia intended to use an online novel as a script for a real-life wave of terror and assassination using explosives and the lethal toxin ricin, according to court documents.
Federal agents raided their north Georgia homes Tuesday and arrested them on charges of conspiring to plan the attacks.
Frederick Thomas, 73; Dan Roberts, 67; Ray Adams, 65; and Samuel Crump, 68, are scheduled to appear in court Wednesday. Relatives of two of the men said the charges were baseless.
Court documents accused the men of trying to obtain an explosive device and a silencer to carry out targeted attacks on government buildings and employees. Two of the men are also accused of trying to seek out a formula to produce ricin, a biological toxin that can be lethal in small doses.
Thomas' wife, Charlotte, told The Associated Press that the charges were "baloney."
"He spent 30 years in the U.S. Navy. He would not do anything against his country," she said. "He loves his country."
Thomas, who is portrayed as the ringleader, talked of modeling the actions on the online novel "Absolved," which involves small groups of citizens attacking U.S. officials, according to court documents. It was written by former Alabama militia leader Mike Vanderboegh, who wrote on his blog Wednesday that his book was fiction and said he was skeptical a "pretty geriatric" militia could carry out the attacks the men were accused of planning.
Vanderboegh told AP his novel was a "useful dire warning" about what could happen if the federal government encroaches too far on the rights of armed citizens. Vanderboegh said he is trying to warn the federal government to back off before violence occurs, yet he also believes a civil war is possible.
"My reason for everything I write is that there are a number of people in this country who have been pushed back and will not be pushed anymore," he said.
Investigators said the four men took several concrete steps to carry out their plans. Thomas is accused of driving to Atlanta with a confidential informant to scope out federal buildings that house the IRS and other agencies.
During the trip, Thomas at one point said to the informant: "There's two schools of thought on this: go for the feds or go for the locals. And I'm inclined to consider both. We'd have to blow the whole building like Timothy McVeigh," according to court documents.
He and Adams also arranged to buy what they thought was an explosive device and a silencer from an undercover agent. The men were arrested days after a lab test confirmed they had trace amounts of ricin in their possession, authorities said.
"While many are focused on the threat posed by international violent extremists, this case demonstrates that we must also remain vigilant in protecting our country from citizens within our own borders who threaten our safety and security," said U.S. Attorney Sally Quillian Yates.
Federal investigators have monitored the group since at least March 17, when a confidential source recorded a meeting of the fringe group at Thomas' two-story house in Cleveland, a small town in the mountains of north Georgia. Thomas boasted of making a "bucket list" of government employees, politicians, businessman and media members that he felt needed to be "taken out."
At the meeting, Thomas said: "There is no way for us, as militiamen, to save this country, to save Georgia, without doing something that's highly, highly illegal: Murder," according to the court records.
Roberts, who attended several meetings, mentioned in May that he knew a former U.S. Army soldier who was a "loose cannon" who may be able to help them make ricin that the group could disperse in major U.S. cities. Crump and Adams were assigned to try to obtain or make the lethal toxin, and Crump was recorded in September saying he would like to make 10 pounds of the substance.
It's not clear from the court documents exactly how the men obtained the trace amounts of ricin.
An informant who met Adams' at his home in October saw lab equipment and a glass beaker, and a bean obtained by the informant was later tested by state officials as positive for ricin.
Court documents also accused Crump of suggesting the ricin could be blown out of a car speeding down an interstate highway to attack people in Washington; Newark, N.J.; Jacksonville, Fla.; Atlanta and New Orleans.
The group also had a “bucket list” of politicians and members of the media that they planned to kill, which seems to be a misreading of the “bucket list” concept. Two of the men bought “what they believed was a silencer and and unregistered explosive” from an FBI informant, as well. They also — with the informant — drove to Atlanta to “scope out” IRS and ATF buildings.
The “good news,” I guess, is that now the Justice Department is carrying out the same ridiculous stings on old Christian guys that it regularly carries out on young Muslim guys. Because let’s be honest, we have no way of knowing whether these four guys would’ve actually acted on their anti-government beliefs if they hadn’t been led to action by the “informants.” They met at a Waffle House and called themselves “the covert group.” They range in age from 65 to 73. How much of a real threat could they possibly have been? How much of a role did the “informant” play in pushing the men toward formulating an actual terror plot instead of just grumbling fantasies of revolution over omelets?
They may have been able to manufacture ricin — one of the men “used to work as a lab technician for a U.S. Department of Agriculture agency known as the Agricultural Research Service,” according to ABC News — but it’s unclear how practical ricin is as a chemical weapon. A terrorist needs tons of ricin to kill people through mass dispersal. Ricin is what terrorists turn to when they fail to make anthrax.
This looks like the same “entrapment in all but name” approach to fighting terror that the Justice Department has been pursuing against American Muslims for years. What will be interesting to see is whether the entrapment defense works any better for a gang of four elderly white guys than it does for teenagers with names like “Hosam Maher Husein Smadi.”
Ricin , from the castor oil plant Ricinus communis, is a highly toxic, naturally occurring protein. A dose as small as a few grains of salt can kill an adult. The LD50 of ricin is around 22 micrograms per kilogram (1.76 mg for an average adult, around 1/228 of a standard aspirin tablet (0.4 g gross)) in humans if exposure is from injection or inhalation. Oral exposure to ricin is far less toxic and lethal dose can be up to 20–30 milligrams per kilogram.
Toxicity
Ricin is poisonous if inhaled, injected, or ingested, acting as a toxin by the inhibition of protein synthesis. It is resistant, but not impervious, to digestion by peptidases. By ingestion, the pathology of ricin is largely restricted to the gastrointestinal tract where it may cause mucosal injuries; with appropriate treatment, most patients will make a full recovery. Because the symptoms are caused by failure to make protein, they emerge only after a variable delay from a few hours to a full day after exposure. An antidote not yet tested on humans has been developed by the UK military, and a vaccine has been developed by the US military, and has had some human testing, and so far shown to be safe, and effective when lab mice were injected with ricin-antibody rich blood mixed with ricin.[5] Symptomatic and supportive treatment is available. Long term organ damage is likely in survivors. Ricin causes severe diarrhea and victims can die of shock. Death typically occurs within 3–5 days of the initial exposure. Abrin is a similar toxin, found in the highly ornamental rosary pea.
Deaths caused by ingestion of castor plant seeds are rare, partly because of the indigestible capsule, and partly because ricin can be digested (although it is resistant). The pulp from eight beans is considered toxic for an adult. A solution of saline and glucose has been used to treat ricin overdose. Rauber and Heard have written that close examination of early 20th century case reports indicates that public and professional perceptions of ricin toxicity "do not accurately reflect the capabilities of modern medical management."
Overdosage
Most acute poisoning episodes in humans are the result of oral ingestion of castor beans, 5-20 of which could prove fatal to an adult. Victims often manifest nausea, emesis, diarrhea, tachycardia, hypotension and seizures persisting for up to a week. Blood, plasma or urine ricin concentrations may be measured to confirm diagnosis.
Biochemistry
Ricin is classified as a type 2 ribosome inactivating protein (RIP). Whereas Type 1 RIPs consist of a single enzymatic protein chain, Type 2 RIPs, also known as holotoxins, are heterodimeric glycoproteins. Type 2 RIPs consist of an A chain that is functionally equivalent to a Type 1 RIP, covalently connected by a single disulfide bond to a B chain that is catalytically inactive, but serves to mediate entry of the A-B protein complex into the cytosol. Both Type 1 and Type 2 RIPs are functionally active against ribosomes in vitro, however only Type 2 RIPs display cytoxicity due to the lectin properties of the B chain. In order to display its ribosome inactivating function, the ricin disulfide bond must be reductively cleaved.
Structure
The tertiary structure of ricin was shown to be a globular, glycosylated heterodimer of approximately 60-65 kDA. Ricin toxin A chain and ricin toxin B chain are of similar molecular weight, approximately 32 kDA and 34 kDA respectively.
Ricin A Chain (RTA) is an N-glycoside hydrolase composed of 267 amino acids. It has three structural domains with approximately 50% of the polypeptide arranged into alpha-helices and beta-sheets. The three domains form a pronounced cleft that is the active site of RTA.
Ricin B Chain (RTB) is a lectin composed of 262 amino acids that is able to bind terminal galactose residues on cell surfaces. RTB form a bilobal, barbell-like structure lacking alpha-helices or beta-sheets where individual lobes contain three subdomains. At least one of these three subdomains in each homologous lobe possesses a sugar-binding pocket that gives RTB its functional character.
Many plants such as barley have the A chain but not the B chain. People do not get sick from eating large amounts of such products, as ricin A is of extremely low toxicity as long as the B chain is not present.
Entry into the cytosol
The ability of ricin to enter the cytosol depends on hydrogen bonding interactions between RTB amino acid residues and complex carbohydrates on the surface of eukaryotic cells containing either terminal N-acetyl galactosamine or beta-1,4-linked galactose residues. Additionally, the mannose-type glycans of ricin are able to bind cells that express mannose receptors.Experimentally, RTB has been shown to bind to the cell surface on the order of 106-108 ricin molecules per cell surface.
The profuse binding of ricin to surface membranes allows internalization with all types of membrane invaginations. Experimental evidence points to ricin uptake in both clathrin-coated pits, as well as clathrin-independent pathways including caveolae and macropinocytosis. Vesicles shuttle ricin to endosomes that are delivered to the Golgi apparatus. The active acidification of endosomes are thought to have little effect on the functional properties of ricin. Because ricin is stable over a wide pH range, degradation in endosomes or lysosomes offer little or no protection against ricin. Ricin molecules are thought to follow retrograde transport via early endosomes, the trans-Golgi network, and the Golgi to enter the lumen of the endoplasmic reticulum (ER).
For ricin to function cytotoxically, RTA must be reductively cleaved from RTB in order to release a steric block of the RTA active site. This process is catalysed by the protein PDI (protein disulphide isomerase) that resides in the lumen of the ER. Free RTA in the ER lumen then partially unfolds and partially buries into the ER membrane, where it is thought to mimic a misfolded membrane-associated protein. Roles for the ER chaperones GRP94 and EDEM have been proposed prior to the 'dislocation' of RTA from the ER lumen to the cytosol in a manner that utilizes components of the endoplasmic reticulum-associated protein degradation (ERAD) pathway. ERAD normally removes misfolded ER proteins to the cytosol for their destruction by cytosolic proteasomes. Dislocation of RTA requires ER membrane-integral E3 ubiquitin ligase complexes, but RTA avoids the ubiquitination that usually occurs with ERAD substrates because of its low content of lysine residues, which are the usual attachment sites for ubiquitin. Thus RTA avoids the usual fate of dislocated proteins (destruction that is mediated by targeting ubiquitinylated proteins to the cytosolic proteasomes). In the mammalian cell cytosol, RTA then undergoes triage by cytosolic molecular chaperones that results in its folding to a catalytic conformation that de-purinates ribosomes, thus halting protein synthesis.
