As the influenza virus life cycle critically depends on a balance between available receptor sitesand receptor binding, the new variant may have emerged by selection of a compensatory co-mutation in the hemagglutinin gene to acquire full virulence. Polysaccharides and in particular carrageenans were found to be potent antiviral agents against certain viruses. The antiviral effects of carrageenans were of limited practical importance so far, most likely because carrageenans are high-molecular weight components making it unlikely that they pass the different barriers of the body or even the cell membrane. However, these characteristics do not rule out local applications. A recent study with Carraguard, a carrageenan-based compound developed by the Population Council, did not show efficacy in prevention of vaginal transmission of HIV. The authors conclude that low acceptance of gel use could have compromised the potential to detect a significant protective effect of Carraguard. In contrast to influenza viruses, HIV causes a persistent systemic infection that is usually not cleared by the immune system of the organism. Therefore, an incomplete protective effect at the entry site of the virus might lead to full blown HIV infection that is inaccessible to treatment with an antiviral polymer. The results of our animal experiments allow the speculation that treatment with iota-carrageenan reduced the spreading of influenza virus in surface epithelia of infected animals and thereby provided sufficient benefit for animals to promote survival. In conclusion, our results suggest that iota-carrageenan is safe and effective in treating influenza infection in an animal model. Moreover, given that a iota-carrageenan-containing nasal spray is already marketed in Europe and has successfully been tested in an exploratory trial for treating common cold in humans, iotacarrageenan is also a promising antiviral candidate for the prophylaxis and treatment of influenza virus infections and should be tested for prevention and treatment of influenza A in clinical DAPT inquirer trials in humans. Besides their critical role in intra- and intercellular “waste management”, proteases are currently accepted as important signaling molecules involved in numerous biological and pathological functions. These include metabolism, tissue remodeling, apoptosis, cell proliferation and migration. Thus, protease signaling needs to be strictly regulated, and the deregulation of protease activity may contribute to various pathologies, including neoplastic diseases. The human Threonine Aspartase 1/Taspase1 gene encodes a protein of 420 amino acids, representing the proenzyme of the protease. In contrast to the other exclusively cis-active type 2 Asparaginases, only Taspase1 is also able to cleave other substrates in trans. Therefore, Taspase1 represents a distinct class of proteolytic enzymes. Taspase1 mediates LDK378 ALK inhibitor cleavage of proteins by recognizing a conserved peptide motif with an aspartate at the P1 position. The N-terminal threonineis generated by autoproteolysis of the Taspase1 proenzymeinto the two subunits a and b, which appear to assemble into an asymmetric 28 kDa/22 kDa a2/b2-heterotetramer, the active protease. The discovery of Taspase1 founded a new class of endopeptidases that utilize the N-terminal threonine of its mature b-subunit as the active site. Mutation of this catalytic nucleophile, Thr234, abolishes Taspase1��s proteolytic activity. Taspase1 was first identified as the 
protease responsible for cleavage of the Mixed Lineage Leukemiaprotein at conservedsites. Proteolytic cleavage of MLL is considered to stabilize the MLL proteinas a crucial event for proper Hox gene expression and normal cell cycle.