Castor Oil Plant, fruits

Castor beans

Ricin ( /ˈraɪsɪn/), 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 human. 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.^[1] Oral exposure to ricin is far less toxic and a lethal dose can be up to 20–30 milligrams per kilogram.

Toxicity[link]

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.^[2] 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,^[3][4] 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.^[6] 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).^[7] The pulp from eight beans is considered toxic for an adult.^[8] A solution of saline and glucose has been used to treat ricin overdose.^[9] 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."^[10]

Overdosage[link]

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, diarrhea, tachycardia, hypotension and seizures persisting for up to a week. Blood, plasma or urine ricin concentrations may be measured to confirm diagnosis.^[11]

Biochemistry[link]

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.^[12]

Structure[link]

Ribosome inactivating protein (Ricin A chain)

Ricin structure. The A chain is shown in blue and the B chain in orange.
Identifiers
Symbol	RIP
Pfam	PF00161
InterPro	IPR001574
PROSITE	PDOC00248
SCOP	1paf
SUPERFAMILY	1paf
Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary

The tertiary structure of ricin was shown to be a globular, glycosylated heterodimer of approximately 60-65 kDA.^[7] 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.^[13] It has three structural domains with approximately 50% of the polypeptide arranged into alpha-helices and beta-sheets.^[14] 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.^[15] 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[link]

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.^[16] Experimentally, RTB has been shown to bind to the cell surface on the order of 10⁶-10⁸ ricin molecules per cell surface.^[17]

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.^[18][19] 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.^[20] 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).^[21]

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.^[22] 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.^[23] Roles for the ER chaperones GRP94 ^[24] and EDEM ^[25] 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,^[26] 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.^[27] 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 ^[24] that de-purinates ribosomes, thus halting protein synthesis.

Ribosome inactivation[link]

Study of the N-glycosidase activity of ricin was pioneered by Endo and Tsurugi^[28] who showed that RTA cleaves a glycosidic bond within the large rRNA of the 60S subunit of eukaryotic ribosomes. They subsequently showed RTA specifically and irreversibly hydrolyses the N-glycosidic bond of the adenine residue at position 4324 (A4324) within the 28S rRNA, but leaves the phosphodiester backbone of the RNA intact.^[29] The ricin targets A4324 that is contained in a highly conserved sequence of 12 nucleotides universally found in eukaryotic ribosomes. The sequence, 5’-AGUACGAGAGGA-3’, termed the sarcin-ricin loop, is important in binding elongation factors during protein synthesis.^[30] The depurination event rapidly and completely inactivates the ribosome, resulting in toxicity from inhibited protein synthesis. A single RTA molecule in the cytosol is capable of depurinating approximately 1500 ribosomes per minute.

Depurination reaction[link]

Within the active site of RTA, there exist several invariant amino acid residues involved in the depurination of ribosomal RNA.^[20] Although the exact mechanism of the event is unknown, key amino acid residues identified include tyrosine at positions 80 and 123, glutamic acid at position 177, and arginine at position 180. In particular, Arg180 and Glu177 have been shown to be involved in the catalytic mechanism, and not substrate binding, with enzyme kinetic studies involving RTA mutants. The model proposed by Mozingo and Robertus,^[31] based x-ray structures, is as follows:

1. Sarcin-ricin loop substrate binds RTA active site with target adenine stacking against tyr80 and tyr123.
2. Arg180 is positioned such that it can protonate N-3 of adenine and break the bond between N-9 of the adenine ring and C-1’ of the ribose.
3. Bond cleavage results in an oxycarbonium ion on the ribose, stabilized by Glu177.
4. N-3 protonation of adenine by Arg180 allows deprotonation of a nearby water molecule.
5. Resulting hydroxyl attacks ribose carbonium ion.
6. Depurination of adenine results in a neutral ribose on an intact phosphodiester RNA backbone.

Manufacture[link]

Ricin is easily purified from castor oil manufacturing waste. The aqueous phase left over from the oil extraction process is called waste mash. It would contain about 5–10% ricin by weight, but heating during the oil extraction process denatures the protein, making the resultant seed cake safe for use as animal feed. From fresh seed, separation requires chromatographic techniques similar to other plant proteins.^{[citation needed]}

Patented extraction process[link]

A process for extracting ricin has been described in a patent.^[32] The described extraction method is very similar to that used for the preparation of soy protein isolates.

The patent was removed from the United States Patent and Trademark Office (USPTO) database sometime in 2004.^[33][34] Modern theories of protein chemistry cast doubt on the effectiveness of the methods disclosed in the patent.^[35]

Potential medicinal use[link]

Some researchers have speculated about using ricins in the treatment of cancer, as a so-called "magic bullet" to destroy targeted cells.^[36] Because ricin is a protein, it can be genetically linked to a monoclonal antibody to target malignant cells recognized by the antibody. The major problem with ricin is that its native internalization sequences are distributed throughout the protein. If any of these native internalization sequences are present in a therapeutic, then the drug will be internalized by, and kill, untargeted epithelial cells as well as targeted cancer cells.

Some researchers hope that modifying ricin will sufficiently lessen the likelihood that the ricin component of these immunotoxins will cause the wrong cells to internalize it, while still retaining its cell-killing activity when it is internalized by the targeted cells. Generally, however, ricin has been superseded for medical purposes by more practical fragments of bacterial toxins, such as diphtheria toxin, which is used in denileukin diftitox, an FDA-approved treatment for leukemia and lymphoma. No approved therapeutics contain ricin.

A promising approach is also to use the non-toxic B subunit as a vehicle for delivering antigens into cells thus greatly increasing their immunogenicity. Use of ricin as an adjuvant has potential implications for developing mucosal vaccines.

This article is missing information about ricinine. This concern has been noted on the talk page where whether or not to include such information may be discussed. (March 2011)

Ricinine has some insecticidal effects on three insect pests as well as a hepatoprotective activity. Ricinine, when administered to mice at low doses has memory-improving effects. The signs of intoxication caused by ricinine can be used as chemical model of epilepsy in the screening of anticonvulsant drugs.^[37]

Incidents involving ricin[link]

Ricin has been involved in a number of incidents, including the high-profile assassination of Georgi Markov using a weapon disguised as an umbrella.

The ingestion of Ricinus communis cake is responsible for fatal ricin poisoning in animals.^[38]

Use as a chemical/biological warfare agent[link]

The United States investigated ricin for its military potential during World War I.^[39] At that time it was being considered for use either as a toxic dust or as a coating for bullets and shrapnel. The dust cloud concept could not be adequately developed, and the coated bullet/shrapnel concept would violate the Hague Convention of 1899 (adopted in U.S. law at 32 Stat. 1903), specifically Annex § 2, Ch.1, Article 23, stating "...it is especially prohibited...[t]o employ poison or poisoned arms".^[40] World War I ended before the U.S. weaponized ricin.

During World War II the US and Canada undertook studying ricin in cluster bombs.^[41] Though there were plans for mass production and several field trials with different bomblet concepts, the end conclusion was that it was no more economical than using phosgene. This conclusion was based on comparison of the final weapons rather than ricin's toxicity (LCt₅₀ ~40 mg·min/m³). Ricin was given the military symbol W or later WA. Interest in it continued for a short period after World War II, but soon subsided when the U.S. Army Chemical Corps began a program to weaponize sarin.

The Soviet Union also possessed weaponized ricin. There were speculations that the KGB even used it outside of the Soviet bloc; however, this was never proven. In 1978, the Bulgarian dissident Georgi Markov was assassinated by Bulgarian secret police who surreptitiously 'shot' him on a London street with a modified umbrella using compressed gas to fire a tiny pellet contaminated with ricin into his leg.^[2][42] He died in a hospital a few days later; his body was passed to a special poison branch of the British Ministry of Defence (MOD) that discovered the pellet during an autopsy. The prime suspects were the Bulgarian secret police: Georgi Markov had defected from Bulgaria some years previously and had subsequently written books and made radio broadcasts which were highly critical of the Bulgarian communist regime. However, it was believed at the time that Bulgaria would not have been able to produce the pellet, and it was also believed that the KGB had supplied it. The KGB denied any involvement although high-profile KGB defectors Oleg Kalugin and Oleg Gordievsky have since confirmed the KGB's involvement. Earlier, Soviet dissident Aleksandr Solzhenitsyn also suffered (but survived) ricin-like symptoms after a 1971 encounter with KGB agents.^[43]

Despite ricin's extreme toxicity and utility as an agent of chemical/biological warfare, it is extremely difficult to limit the production of the toxin. The castor bean plant from which ricin is derived is a common ornamental and can be grown at home without any special care, and the major reason ricin is a public health threat is that it is easy to obtain.^{[citation needed]}

Under both the 1972 Biological Weapons Convention and the 1997 Chemical Weapons Convention, ricin is listed as a schedule 1 controlled substance. Despite this, more than 1 million tonnes of castor beans are processed each year, and approximately 5% of the total is rendered into a waste containing negligible concentrations of undenatured ricin toxin.^[44]

Ricin is several orders of magnitude less toxic than botulinum or tetanus toxin, but the latter are harder to come by. Compared to botulinum or anthrax as biological weapons or chemical weapons, the quantity of ricin required to achieve LD₅₀ over a large geographic area is significantly more than an agent such as anthrax (tons of ricin vs. only kilogram quantities of anthrax).^[45] Ricin is easy to produce, but is not as practical nor likely to cause as many casualties as other agents.^[2] Ricin is inactivated (the protein changes structure and becomes less dangerous) much more readily than anthrax spores, which may remain lethal for decades. Jan van Aken, a Dutch expert on biological weapons, explained in a report for The Sunshine Project that Al Qaeda's experiments with ricin suggest their inability to produce botulinum or anthrax.^[46]

Ian Davison, a British white supremacist and neo-Nazi, was arrested in 2009 for planning terrorist attacks involving ricin.

In 2011 the United States government discovered information that terrorist groups were attempting to obtain large amounts of castor beans for weaponized ricin use.^[47]

On November 1, 2011 the FBI arrested 4 North Georgia men and charged them in plots to purchase explosives, a silencer and to manufacture the biological toxin ricin from castor beans.^[48]

References[link]

External links[link]

Wikimedia Commons has media related to: Ricin

• Canola oil: Does it contain toxins? from Mayo Clinic
• Castor bean information at Purdue University
• ricin information at Department of Health (United Kingdom)
• ricin information at Cornell University
• Medical research on ricin at BBC
• Chemical Review at United States Army
• Ricin - Emergency Preparations at CDC
• BioHealthBase Bioinformatics Resource Center Ricin bioinformatics resource

John McAfee (born September 18, 1945) is a computer programmer and founder of McAfee. He was one of the first people to design anti-virus software and to develop a virus scanner. He was born in England and raised in Salem, Virginia.^[1] He received his bachelor's degree in mathematics from Roanoke College in 1967, and he received an honorary doctorate from Roanoke College in 2008.

John was employed as a programmer by NASA's Institute for Space Studies in New York City from 1968 to 1970. From there he went to Univac as a software designer and later to Xerox as an Operating System architect. In 1978 he joined Computer Sciences Corporation as a software consultant. Later, while employed by Lockheed in the 1980s, McAfee received a copy of the Pakistani Brain computer virus and began developing software to combat viruses. He was the first to distribute anti-virus software using the shareware business model. In 1989, he quit Lockheed and began working full time at his anti-virus company McAfee Associates, which he initially operated from his home in Santa Clara, California.

This company later became Network Associates, a name it retained for seven years until it was renamed McAfee, which remains today as one of the largest anti-virus companies in the world. John McAfee teaches yoga^[2] and has written several books about yoga.^[3]

Other business ventures that he founded included Tribal Voice, which developed one of the first instant messaging programs,^[4] PowWow.

In August 2009, The New York Times reported that McAfee's personal fortune had declined to $4 million from a peak of $100 million, the effect of the global financial crisis and recession on his investments.^[5]

Beginning in February 2010, John started a new venture in the field of bacterial quorum sensing. His new company QuorumEx is headquartered in Belize and is working towards producing commercial all natural antibiotics based on anti-quorum sensing technology.^[6]

In a 2012 article in Mensa Bulletin, the magazine of American Mensa, he stated that being the developer of the first commercial anti-virus program has made him "the most popular hacking target", adding "Hackers see hacking me as a badge of honor." He added that for his own security he has other people buy his computer equipment for him, uses pseudonyms for setting up computers and logging in, and changes his IP address several times a day.^[7]

On May 2, 2012, McAfee's property in Orange Walk Town, Belize was raided by the Gang Suppression Unit. A GSU press release stated that he was arrested for unlicensed drug manufacturing and possession of an unlicensed weapon. McAfee was allegedly in the presence of his 17 year old Belizean girlfriend. All charges were dropped and Mr. McAfee is suing the Belizean Government for false arrest.^{[8][9][10][11]}

References[link]

External links[link]

• McAfee Quotes
• QuorumEx.com
• NNDB bio
• InformationWeek article: "Zone Labs To Get Funding, New Board Member"
• PCWorld article: "It's Official: Network Associates Becomes McAfee"
• radsoft.net: 'Business strategy, move to Colorado'
• radsoft.net: 'Nothing to Sell

Roger Wicker
United States Senator from Mississippi
Incumbent
Assumed office December 31, 2007 Serving with Thad Cochran
Preceded by	Trent Lott
Member of the U.S. House of Representatives from Mississippi's 1st district
In office January 3, 1995 – December 31, 2007
Preceded by	Jamie Whitten
Succeeded by	Travis Childers
Mississippi State Senator
In office 1987–1994
Personal details
Born	Roger Frederick Wicker (1951-07-05) July 5, 1951 (age 60) Pontotoc, Mississippi
Political party	Republican
Spouse(s)	Gayle Wicker
Children	Margaret Wicker Caroline Wicker McDaniel Wicker
Residence	Tupelo, Mississippi
Alma mater	University of Mississippi (B.A., J.D.)
Occupation	Attorney
Religion	Southern Baptist
Website	wicker.senate.gov
Military service
Service/branch	United States Air Force
Years of service	1976-2004
Rank	Lieutenant Colonel

Roger Frederick Wicker (born July 5, 1951) is the junior United States Senator from Mississippi and a member of the Republican Party. In December 2007 he was appointed by Governor Haley Barbour to fill the seat vacated by Trent Lott. He subsequently won the 2008 special election for the remainder of the term. Wicker served in the U.S. House of Representatives, representing Mississippi's 1st congressional district from 1995 to 2007.

Early life[link]

Wicker was born in Pontotoc, Mississippi on July 5, 1951, the son of Wordna Glen (née Threadgill) and Frederick T. "Fred" Wicker.^[1] He served as a page in the U.S. House of Representatives when he was 16.^{[citation needed]} He earned a bachelor's degree in journalism and political science and a law degree from the University of Mississippi where he was a member of the Sigma Nu fraternity.^{[citation needed]}

After graduation, Wicker served as an officer in the United States Air Force from 1976 to 1980.^[2][3] Starting in 1980, he was a member of the Air Force Reserve; he retired from the Reserve in 2003 as a lieutenant colonel.^[2] Wicker served as a judge advocate.^[4]

Early political career[link]

Wicker began his political career as a member of Trent Lott's political counsel. He then served in the Mississippi State Senate from 1987 to 1994, representing a district that included Tupelo. He was the first Republican elected to the legislature from Northern Mississippi since Reconstruction.^{[citation needed]}

U.S. House of Representatives[link]

Elections[link]

In 1994, Democrat Jamie Whitten declined to seek re-election; he had represented the 1st District for 54 years, a historical record at the time. Wicker finished first in a crowded six-way Republican primary; the other big name in the primary, former U.S. Attorney Bob Whitwell, finished 600 votes short of the other runoff spot. In the runoff, Wicker defeated attorney Grant Fox with 53 percent of the vote.

In the general election, Wicker defeated Fulton attorney Bill Wheeler, capturing 63 percent of the vote,^[5] making him the first Republican to represent the 1st District in over a century. However, this was not considered an upset, as the 1st has always been a rather conservative district (especially in the Memphis suburbs). The last time it supported a Democrat for president was in 1976, when Jimmy Carter carried the district. Before then, Mississippi had not supported the official Democratic candidate since 1956 (it voted for George Wallace in 1968). Although Whitten had a nearly unbreakable hold on the district, it had been considered very likely that he would be succeeded by a Republican once he retired.

Then-Rep. and Mrs. Wicker visit with Afghan leader Hamid Karzai

Wicker was reelected six more times without much difficulty, never dropping below 60 percent of the vote.

Tenure[link]

He was formerly a member of the House Appropriations Committee. He was also Deputy Republican Whip.

In Congress, Wicker worked on issues related to medical research and on economic development for his home state. He advocated private-public partnerships to bring investment to rural areas. Wicker also worked for veterans' issues while serving as a member of the Military Construction and Veterans Affairs Subcommittee.^[6] In his final year as Representative, Wicker topped the list in earmarks.^[7]

U.S. Senate[link]

Committee Assignments, 112th Congress[link]

• Senate Committee on Armed Services
  • United States Senate Armed Services Subcommittee on Airland
  • United States Senate Armed Services Subcommittee on Strategic Forces
  • United States Senate Armed Services Subcommittee on Seapower (Ranking Member)
• Senate Committee on Banking, Housing, and Urban Affairs
  • Subcommittee on Economic Policy
  • Subcommittee on Housing, Transportation, and Community Development
  • Subcommittee Securities, Insurance, and Investment
• Senate Committee on Commerce, Science and Transportation
  • Subcommittee on Aviation Operations, Safety, and Security
  • Subcommittee on Communications, Technology, and the Internet
  • Subcommittee on Consumer Protection, Product Safety, and Insurance
  • Subcommittee on Oceans, Atmosphere, Fisheries, and Coast Guard
  • Subcommittee on Science and Space
  • Subcommittee on Surface Transportation and Merchant Marine Infrastructure, Safety and Security (Ranking Member)

• Senate Committee on Veterans' Affairs

• Commission on Security and Cooperation in Europe

Caucus memberships[link]

• Congressional Human Rights Caucus
• Congressional Immigration Reform Caucus
• International Conservation Caucus
• Interstate 69 Caucus (Co-Chair)
• Sportsmen's Caucus
• Tennessee Valley Authority Congressional Caucus

Tenure[link]

At a press conference on December 31, 2007, Mississippi Governor Haley Barbour appointed Wicker to fill the Senate seat vacated by Trent Lott on December 18, 2007.^[8] He was sworn in by the clerk of the U.S. Senate just prior to that news conference.^[9]

Wicker ran for the remainder of Lott's term in the November 2008 special election against Ronnie Musgrove, Barbour's predecessor as governor. He won the seat with 55% of the vote. Wicker's resignation from the House also triggered a May 13, 2008 special election to fill the vacancy in the House, which was won by Democrat Travis Childers.

On September 16, 2010, President Barack Obama announced his intent to nominate Wicker as representative of the United States to the Sixty-fifth Session of the General Assembly of the United Nations.^[10]

Electoral history[link]

Official photo as U.S. Representative.

This section requires expansion.

The following is a partial summary of Wicker's election results.^{[citation needed]}

Personal life[link]

Wicker is married to the former Gayle Long of Tupelo. They have three children: Margaret and son-in-law Manning McPhillips; Caroline and son-in-law Kirk Sims; and McDaniel; and one granddaughter, Caroline McPhillips. The Wickers reside in Tupelo, where he is a deacon at First Baptist Church.

References[link]

External links[link]

United States Air Force portal

Wikimedia Commons has media related to: Roger Wicker

• Official Senate website
• Official campaign website
• Biography at WhoRunsGov.com at The Washington Post
• Biography at the Biographical Directory of the United States Congress
• Voting record maintained by The Washington Post
• Biography, voting record, and interest group ratings at Project Vote Smart
• Congressional profile at GovTrack
• Congressional profile at OpenCongress
• Issue positions and quotes at On the Issues
• Financial information at OpenSecrets.org
• Staff salaries, trips and personal finance at LegiStorm.com
• Campaign finance reports and data at the Federal Election Commission
• Appearances on C-SPAN programs
• Collected news and commentary at The New York Times
• Profile at SourceWatch

v t e United States Senators from Mississippi Class 1 Leake Holmes Ellis Reed Ellis Black Trotter T. Hickman Williams Henderson Speight Davis McRae S. Adams Davis Ames Pease Bruce George Money J. Williams Stephens Bilbo Stennis Lott Wicker Class 2 T. Hill Williams Reed R. Adams Poindexter Walker Chalmers Foote Brooke Brown Revels Alcorn Lamar Walthall McLaurin Walthall Sullivan McLaurin Gordon Percy Vardaman Harrison Eastland Doxey Eastland Cochran