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Book
Plant lectins
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ISBN: 0511895372 Year: 1991 Publisher: Cambridge : Cambridge University Press,

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Abstract

This volume surveys the chemistry, biochemistry, biosynthesis, metabolism and pharmacological properties of lectins. Lectins, which are most commonly found in plants, are widespread natural products with striking biological activities. Their specific ability to recognise and bind to simple or complex saccharides facilitates their role as effective information protein molecules. As agents of cell-to-cell recognition, lectins promote symbiosis between plants and specific nitrogen-fixing soil bacteria. As natural defensive molecules, they can protect plants against predators such as bacteria, fungi and insects. As part of our diet, lectins are powerful exogenous growth factors in the small intestine and influence our health, the digestive function and the bacterial ecology of the alimentary tract. Lectins are also important research tools in preparative biochemistry and cell science.

Plant lectins
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ISBN: 0521328241 Year: 1991 Publisher: Cambridge Cambridge University Press

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Book
The lectins : properties, functions and applications in biology and medicine
Author:
ISBN: 0124499457 0323144446 1299365418 Year: 1986 Publisher: New York (N.Y.): Academic press

Handbook of plant lectins : properties and biomedical applications.
Authors: --- --- ---
ISBN: 047196445X Year: 1997 Publisher: Chichester Wiley


Book
Ricin and shiga toxins : pathogenesis, immunity, vaccines and therapeutics
Author:
ISBN: 3642274692 3642428304 3642274706 9786613697240 128078685X Year: 2012 Publisher: Berlin : Springer-Verlag,

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The intent of this volume of Current Topics in Microbiology and Immunology was to bring together a collection of in-depth and cutting edge reviews that highlight our current understanding of the biology of ricin and Shiga toxin (Stx), with the long term goal of advancing the development of countermeasures against these toxic agents.  In May of 2011, Western Europe experienced a severe outbreak of Stx-producing E. coli (STEC) that culminated in more than 3200 cases and 39 deaths.  While Stx is not the only virulence factor associated with STEC, it is certainly the primary determinant associated with the onset of hemolytic uremic syndrome (HUS).  At the present time, there are no clinically approved measures to neutralize Stx in individuals suffering from STEC infection.  Nor are there any preventatives or therapeutics for ricin toxin.  Although incidents of ricin exposure are largely unheard of, federal agencies and public health officials consider it a significant threat.  It is well documented that domestic and international terrorist groups have stockpiled, and in some cases weaponized ricin with the intent of releasing it into the public sphere and causing panic, illness and/or death on a local, regional, or possibly national scale. As the title of this volume indicates, the chapters, written by leading experts in the field, are organized so as to cover all aspects of ricin and Stx, including pathogenesis, immunity, vaccines and therapeutics. This outstanding collection of reviews will serve as an important and readily accessible resource for the research community in the coming years.   .

Keywords

Antigens and antibodies. --- Chemical agents (Munitions) -- Toxicology. --- Ricin. --- Toxins. --- Verocytotoxins. --- Ricin --- Verocytotoxins --- Chemical agents (Munitions) --- Immunoglobulins --- Ribosome Inactivating Proteins, Type 2 --- Enterotoxins --- Plant Lectins --- Bacterial Toxins --- Albumins --- Ribosome Inactivating Proteins --- Proteins --- Toxins, Biological --- Lectins --- Biological Factors --- N-Glycosyl Hydrolases --- Amino Acids, Peptides, and Proteins --- Plant Proteins --- Glycoside Hydrolases --- Chemicals and Drugs --- Hydrolases --- Enzymes --- Enzymes and Coenzymes --- Shiga Toxins --- Biology --- Health & Biological Sciences --- Microbiology & Immunology --- Pharmacy, Therapeutics, & Pharmacology --- Toxicology --- Immunotherapy. --- Vaccines. --- Therapeutic immunology --- Natural toxicants --- Toxicants, Natural --- Toxins and antitoxins --- Castor bean lectin --- Ricinus lectin --- Medicine. --- Pharmacology. --- Biomedicine. --- Pharmacology/Toxicology. --- Drug effects --- Medical pharmacology --- Medical sciences --- Chemicals --- Chemotherapy --- Drugs --- Pharmacy --- Clinical sciences --- Medical profession --- Human biology --- Life sciences --- Pathology --- Physicians --- Physiological effect --- Biologicals --- Clinical immunology --- Therapeutics --- Antigens --- Metabolites --- Poisons --- Antitoxins --- Detoxification (Health) --- Plant lectins --- Plant toxins --- Toxalbumins --- Toxicology. --- Medicine --- Pharmacology --- Poisoning


Book
Toxic plant proteins
Authors: ---
ISBN: 3642263771 3642121756 1299335721 3642121764 Year: 2010 Publisher: Heidelberg ; New York : Springer,

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Many plants produce enzymes collectively known as ribosome-inactivating proteins (RIPs). RIPs catalyze the removal of an adenine residue from a conserved loop in the large ribosomal RNA. The adenine residue removed by this depurination is crucial for the binding of elongation factors. Ribosomes modified in this way are no longer able to carry out protein synthesis. Most RIPs exist as single polypeptides (Type 1 RIPs) which are largely non-toxic to mammalian cells because they are unable to enter them and thus cannot reach their ribosomal substrate. In some instances, however, the RIP forms part of a heterodimer where its partner polypeptide is a lectin (Type 2 RIPs). These heterodimeric RIPs are able to bind to and enter mammalian cells. Their ability to reach and modify ribosomes in target cells means these proteins are some of the most potently cytotoxic poisons found in nature, and are widely assumed to play a protective role as part of the host plant’s defenses. RIPs are able to further damage target cells by inducing apoptosis. In addition, certain plants produce lectins lacking an RIP component but which are also cytotoxic. This book focuses on the structure/function and some potential applications of these toxic plant proteins.

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