A review of techniques used by microbes to evade the immune system.

Prion diseases, also known as transmissible spongiform encephalopathies, are infectious progressive fatal neurodegenerative diseases which affect humans as well as wild and domestic animals. Distribution of prion infectivity in organs and tissues is important in understanding prion disease pathogenesis and designing strategies to prevent prion infection in animals and humans. We show for the first time the presence of prion infectivity in white fat and brown fat tissues of mice with prion disease. Our results suggest that fat tissues of domestic or wild animals infected with prions may pose an unappreciated hazard for spread of infection to humans or domestic animals. The presence of prion infectivity in fat suggests that additional consideration may be required to eliminate from the food chain any fat from ruminants suspected of exposure to or infection with prions. Thus, this finding has implications for public health, food safety, and prion disease prevention strategies.

Researchers from the National Institutes of Health and the Scripps Research Institute have found novel prion infectivity in white and brown fat tissues of mice. The study appears December 5 in the open-access journal PLoS Pathogens. Prion diseases, also known as transmissible spongiform encephalopathies, are infectious progressive fatal neurodegenerative diseases which affect humans as well as wild and domestic animals. Distribution of prion infectivity in organs and tissues is important in understanding prion disease pathogenesis and designing strategies to prevent prion infection in animals and humans. Previous studies in animals including sheep, goats, cattle, deer, mink, hamsters and mice, have found prion infectivity mostly in nervous system tissues such as the brain and spinal cord. The tissues studied here in a mouse model demonstrate a proof of principle that white and brown fat tissues are sites of prion agent deposition and therefore may play a previously unrecognized role in prion infectivity and transmission of prion disease. The authors state clearly that it will be important to extend their studies to prion-infected large animals, such as cattle, sheep, deer, and elk where they may be potential sources of contamination of human and domestic animal food chains. Results of the current and future studies may merit additional consideration of steps to eliminate from the food chain any fat from ruminants suspected of exposure to or infection with prions.

Following several decades of research, there is not yet a convincing vaccine against shigellosis. It is still difficult, in spite of the breadth of strategies (i.e. live attenuated oral, killed oral, subunit parenteral) to select an optimal option. Two approaches are clearly emerging: (i) live attenuated deletion mutants based on rational selection of genes that are key in the pathogenic process, and (ii) conjugated detoxified polysaccharide parenteral vaccines, or more recently conjugated synthetic carbohydrates. Some of these approaches have already undergone phase I and II clinical trials with promising results, but important issues have also emerged, particularly the discrepancy between colonization and immunogenic potential of live attenuated vaccine candidates depending upon the population concerned (i.e. non endemic vs. endemic areas). Efforts are needed to definitely establish the proof of concept of these approaches, and thus the need for clinical trials which should also soon explore the possibility to associate different serotypes, in response to serotype specific protection against shigellosis. More basic research is also required to improve what we can still consider as first-generation vaccines, and to explore possible new paradigms including the search for cross-protective antigens.