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Rare 'Gene-for-gene' Interaction Helps Bacteria Kill Their Host

Date: 7.5.2007 

Scientists have discovered that a cousin of the plague bacterium uses a single gene to out-fox insect immune defences and kill its host. In new research, scientists have found that Photorhabdus bacteria produce an antibiotic which inhibits the work of an enzyme that insects’ immune systems use to defend themselves from attack. Although such so-called gene-for-gene interactions are thought to be common in diseases, very few examples of a single gene in a pathogen targeting a single gene in an animal or human host have been identified so far. Photorhabdus is a family of bacteria that in relatively small concentrations can kill insects - between 10-100 cells of it are typically enough – but most are harmless to humans and can be used as a biological control mechanism to replace pesticide use.... Whole article "ScienceDaily":[ www.sciencedaily.com]

Researchers Uncover Protection Mechanism Of Radiation-resistant Bacterium - Results of a recent study titled “Protein Oxidation Implicated as the Primary Determinant of Bacterial Radioresistance,” will be published in the March 20 edition of PLoS Biology The field of radiobiology is built on the premise that radiation is dangerous because of its damaging effects on DNA This new model of radiation toxicity shifts the emphasis away from DNA damage toward protein damage, where DNA repair-related proteins in sensitive cells are devastated by radiation long before DNA is significantly damaged Whole article: http://www (23.3.2007)

Secret Of Worm's Poison Pill Box Protein Could Produce New Natural Insecticide - Researchers at the University of Warwick have discovered how a protein from a bacterium acts like a cunningly designed poison pill box that could now be used as a basis of a new range of natural insecticides The bacterium uses a protein (XptA1) a toxin which helps the nematode to kill and feed on the dead body of the insect The research team, based at the University of Warwick’s horticultural research arm Warwick HRI, have now been able to reveal the shape of the protein XptA1 and discovered a number of properties that make it a particularly efficient natural insecticide and possible alternative to Whole article: http://www (20.3.2007)

Researchers Discover Cell-wall Carbohydrate That Is Crucial To Anthrax Bacterium - A week after the 9/11 attacks in 2001, the letters began to arrive Since that time, governmental authorities have been engaged in a race to find ways to keep citizens safe if terrorists attack again with Bacillus anthracis, the bacterium that causes anthrax The unique nature of the carbohydrate makes the molecule an important target for evaluating its role in virulence and survival of the anthrax bacterium, the development of new diagnostic tests and perhaps even as a new vaccine additive Russell Carlson of the department of biochemistry and molecular biology at the University of Georgia and faculty member at UGA’s Complex Carbohydrate Research Center (CCRC), was corresponding author on a paper reporting the research, which was just published in the online version of the Journal of Biological Chemistry Anthrax is a naturally occurring animal disease The problems facing researchers as they unravel all the molecular riddles of anthrax are enormous Effective vaccines and antibiotics against anthrax do exist As a first step in understanding the structure and function of cell wall carbohydrates, the research team examined four Bacillus anthracis strains – Ames, Pasteur, Sterne and UT60 – and compared them to two related strains of Bacillus cereus, a soil-dwelling bacterium that causes food-borne illnesses One important discovery in the just-reported research is that the newly discovered carbohydrate in the cell wall of B The research was supported by grants from the National Institutes of Health (to Carlson) and the U Source (11.10.2006)

Structure of key enzyme in plague bacterium found - Researchers at the National Institute of Standards and Technology (NIST) have solved the structure of a key enzyme from the bacterium responsible for plague, finding that it has a highly unusual configuration The NIST team determined the three-dimensional shape of class IV adenylyl cyclase (AC), an enzyme found in plague bacteria -- Yersinia pestis -- by purifying and crystallizing the protein and using X-ray crystallography at the Center for Advanced Research in Biotechnology to resolve its configuration Shape plays an essential role in determining the biological function of a protein, but it's very difficult to determine for such large molecules The purpose of AC-IV in plague is not well understood, but it may play a role in disrupting cell processes in the infected host Source (24.8.2006)
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