Hemp (Cannabis sativa L.) as a Resource for Green Cosmetics: Yield of Seeds and Fatty Acids Composition of 20 Varieties under the Growing Conditions of Organic Farming in Austria

The interest in hemp (non-drug Cannabis sativa L.) for skin care and cosmetic use is due to the high content of oil, especially unsaturated fatty acids in seed with technological and therapeutic effects. In a field trial on an organic farm, seed weight and content of fatty acids of 20 hemp varieties were surveyed on three different harvest dates. The dry matter seed yields ranged from 27-149 g m2. The varieties Ferimon-12, Fedora-19, and Bialobreszie produced high seed yields on all three harvest dates but yields were not significantly different from a large group of other varieties. Contents of palmitic acid range from 3.1 to 4.1%, of stearic acid from 0.1 to 1.9%, of oleic acid from 3.7 to 9.2%, of linoleic acid from 44.8 to 60.2%, of α-linolenic acid from 18.2 to 27.4%, and of γ-linolenic acid from 1.6 to 4.7%. The genotype has no significant influence on fatty acid content. All 20 varieties tested show high quantities of fatty acid depending on the harvest date, so that no variety can be favored. Results confirm that hemp is a very good source of fatty acids for skin care and cosmetic use

Detection of novel biomarkers of liver cirrhosis by high performance proteomics

Comunicaciones a congreso

The Chlamydia psittaci Genome: A Comparative Analysis of Intracellular Pathogens

Chlamydiaceae are a family of obligate intracellular pathogens causing a wide range of diseases in animals and humans, and facing unique evolutionary constraints not encountered by free-living prokaryotes. To investigate genomic aspects of infection, virulence and host preference we have sequenced Chlamydia psittaci, the pathogenic agent of ornithosis.A comparison of the genome of the avian Chlamydia psittaci isolate 6BC with the genomes of other chlamydial species, C. trachomatis, C. muridarum, C. pneumoniae, C. abortus, C. felis and C. caviae, revealed a high level of sequence conservation and synteny across taxa, with the major exception of the human pathogen C. trachomatis. Important differences manifest in the polymorphic membrane protein family specific for the Chlamydiae and in the highly variable chlamydial plasticity zone. We identified a number of psittaci-specific polymorphic membrane proteins of the G family that may be related to differences in host-range and/or virulence as compared to closely related Chlamydiaceae. We calculated non-synonymous to synonymous substitution rate ratios for pairs of orthologous genes to identify putative targets of adaptive evolution and predicted type III secreted effector proteins.This study is the first detailed analysis of the Chlamydia psittaci genome sequence. It provides insights in the genome architecture of C. psittaci and proposes a number of novel candidate genes mostly of yet unknown function that may be important for pathogen-host interactions

Identification and Characterization of a Novel Porin Family Highlights a Major Difference in the Outer Membrane of Chlamydial Symbionts and Pathogens

The Chlamydiae constitute an evolutionary well separated group of intracellular bacteria comprising important pathogens of humans as well as symbionts of protozoa. The amoeba symbiont Protochlamydia amoebophila lacks a homologue of the most abundant outer membrane protein of the Chlamydiaceae, the major outer membrane protein MOMP, highlighting a major difference between environmental chlamydiae and their pathogenic counterparts. We recently identified a novel family of putative porins encoded in the genome of P. amoebophila by in silico analysis. Two of these Protochlamydia outer membrane proteins, PomS (pc1489) and PomT (pc1077), are highly abundant in outer membrane preparations of this organism. Here we show that all four members of this putative porin family are toxic when expressed in the heterologous host Escherichia coli. Immunofluorescence analysis using antibodies against heterologously expressed PomT and PomS purified directly from elementary bodies, respectively, demonstrated the location of both proteins in the outer membrane of P. amoebophila. The location of the most abundant protein PomS was further confirmed by immuno-transmission electron microscopy. We could show that pomS is transcribed, and the corresponding protein is present in the outer membrane throughout the complete developmental cycle, suggesting an essential role for P. amoebophila. Lipid bilayer measurements demonstrated that PomS functions as a porin with anion-selectivity and a pore size similar to the Chlamydiaceae MOMP. Taken together, our results suggest that PomS, possibly in concert with PomT and other members of this porin family, is the functional equivalent of MOMP in P. amoebophila. This work contributes to our understanding of the adaptations of symbiotic and pathogenic chlamydiae to their different eukaryotic hosts