Increasing world population worsens the serious problem of food security in developing countries. On the other hand in industrialized countries, where the problem of food security is of minor concern, health problems related to food refer to 2 main factors: food safety and environmental sustainability of food production. For these reasons, new ways must be found to increase yields while preserving food quality, natural habitats, and biodiversity. Insects could be of great interest as a possible solution due to their capability to satisfy 2 different requirements: (i) they are an important source of protein and other nutrients; (ii) their use as food has ecological advantages over conventional meat and, in the long run, economic benefits. However, little is known on the food safety side and this can be of critical importance to meet society's approval, especially if people are not accustomed to eating insects. This paper aims to collect information in order to evaluate how insects could be safely used as food and to discuss nutritional data to justify why insect food sources can no longer be neglected. Legislative issues will also be discussed.

Dystroglycan is a receptor responsible for crucial interactions between extracellular matrix and cytoplasmic space. We provide the first evidence that dystroglycan is truncated. In HC11 normal murine and the 184B5 non-tumorigenic mammary human cell lines, the expected L L-dystroglycan 43 kDa band was found but human breast T47D, BT549, MCF7, colon HT29, HCT116, SW620, prostate DU145 and cervical HeLa cancer cells expressed an anomalous W W31 kDa L L-dystroglycan band. K K-Dystroglycan was udetectable in most of the cell lines in which L L-dystroglycan was found as a W W31 kDa species. An anomalous W W31 kDa L L-dystroglycan band was also observed in N-methyl-N-nitrosurea-induced primary rat mammary tumours. Reverse transcriptase polymerase chain reaction experiments confirmed the absence of alternative splicing events and/or expression of eventual dystroglycan isoforms. Using protein extraction procedures at low-and high-ionic strength, we demonstrated that both the 43 kDa and W W31 kDa L L-dystroglycan bands harbour their transmembrane segment. ß

Diet and lifestyle have a strong influence on gut microbiota, which in turn has important implications on a variety of health-related aspects. Despite great advances in the field, it remains unclear to which extent the composition of the gut microbiota is modulated by the intake of animal derived products, compared to a vegetable based diet. Here the specific impact of vegan, vegetarian, and omnivore feeding type on the composition of gut microbiota of 101 adults was investigated among groups homogeneous for variables known to have a role in modulating gut microbial composition such as age, anthropometric variables, ethnicity, and geographic area. The results displayed a picture where the three different dietetic profiles could be well distinguished on the basis of participant’s dietetic regimen. Regarding the gut microbiota; vegetarians had a significantly greater richness compared to omnivorous. Moreover, counts of Bacteroidetes related operational taxonomic units (OTUs) were greater in vegans and vegetarians compared to omnivores. Interestingly considering the whole bacterial community composition the three cohorts were unexpectedly similar, which is probably due to their common intake in terms of nutrients rather than food, e.g., high fat content and reduced protein and carbohydrate intake. This finding suggests that fundamental nutritional choices such as vegan, vegetarian, or omnivore do influence the microbiota but do not allow to infer conclusions on gut microbial composition, and suggested the possibility for a preferential impact of other variables, probably related to the general life style on shaping human gut microbial community in spite of dietary influence. Consequently, research were individuals are categorized on the basis of their claimed feeding types is of limited use for scientific studies, since it appears to be oversimplified.

Salmonella spp. is one of the main causes of foodborne illnesses in humans worldwide. Consequently, great interest exists in reducing its impact on human health by lowering its prevalence in the food chain. Antimicrobial formulations in the form of nanoparticles exert bactericidal action due to their enhanced reactivity resultant from their high surface/volume ratio. Silver nanoparticles (AgNPs) are known to be highly toxic to Gram-negative and Gram-positive microorganisms, including multidrug resistant bacteria. However, few data concerning their success against different Salmonella serovars are available. Aims of the present study were to test the antimicrobial effectiveness of AgNPs, against Salmonella Enteritidis, Hadar, and Senftenberg, and to investigate the causes of their different survival abilities from a molecular point of view. Results showed an immediate, time-limited and serovar-dependent reduction of bacterial viability. In the case of S. Senftenberg, the reduction in numbers was observed for up to 4 h of incubation in the presence of 200 mg/l of AgNPs; on the contrary, S. Enteritidis and S. Hadar resulted to be inhibited for up to 48 h. Reverse transcription and polymerase chain reaction experiments demonstrated the constitutive expression of the plasmidic silver resistance determinant (SilB) by S. Senftenberg, thus suggesting the importance of a cautious use of AgNPs.

Eukaryotic DNA topoisomerase I (Top1) is a monomeric protein clamp that functions in DNA replication, transcription, and recombination. Opposable ''lip'' domains form a salt bridge to complete Top1 protein clamping of duplex DNA. Changes in DNA topology are catalyzed by the formation of a transient phosphotyrosyl linkage between the active-site Tyr-723 and a single DNA strand. Substantial protein domain movements are required for DNA binding, whereas the tight packing of DNA within the covalent Top1-DNA complex necessitates some DNA distortion to allow rotation. To investigate the effects of Top1-clamp closure on enzyme catalysis, molecular modeling was used to design a disulfide bond between residues Gly-365 and Ser-534, to crosslink protein loops more proximal to the active-site tyrosine than the protein loops held by the Lys-369 -Glu-497 salt bridge. In reducing environments, Top1-Clamp was catalytically active. However, contrary to crosslinking the salt-bridge loops [Carey, J. D NA topoisomerases alter DNA topology by the concerted cleavage and religation of DNA strand(s) (reviewed in refs. 1-3). The nucleophilic attack of an active-site tyrosine on a phosphodiester DNA bond generates a phosphotyrosyl linkage, providing a transient protein-linked gate through which another DNA strand or duplex may pass. A second transesterification resolves the tyrosyl-DNA linkage to restore DNA integrity. DNA topoisomerases play critical roles in most DNA transactions, including DNA replication, transcription, and recombination, as well as chromosome segregation. These enzymes also constitute the targets of clinically important anticancer and antibacterial agents (4-6). With human DNA topoisomerase I (Top1), camptothecin (CPT) analogues (topotecan and CPT-11) have shown remarkable antitumor activity against pediatric and adult malignancies (7). These agents poison Top1 by reversibly stabilizing the covalent enzyme-DNA complex, inducing S-phase-dependent cell lethality.Type IB enzymes, including eukaryotic and vaccinia virus Top1, are distinct from other enzymes in that the active-site tyrosine becomes linked to a 3Ј-phosphoryl end, versus the 5Ј-phosphotyrosine bond formed by types IA and II enzymes (1-3). Crystallographic data indicate that the monomeric enzymes (types IA and IB) or the protein subunits that constitute the symmetrical halves of type II enzymes [DNA gyrase and DNA topoisomerase II (Top2)] form a protein clamp (1-3). Yet, type IB enzymes are again unique in that biochemical and structural data support a mechanism of DNA rotation, as opposed to the coordinated domain movements in types IA and II enzymes that are necessary for an enzyme-bridging mechanism (1, 3, 8).The conserved central domain of eukaryotic Top1 forms the protein clamp (Fig. 1). Subdomains I and II constitute the upper cap, which is connected by a flexible hinge to the bottom part of the clamp, subdomain III. Two extended ␣-helices connect the clamp core with the conserved C-terminal domain, containing the activesite tyrosine. Human Top1 struc...