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Influenza is one of the most common human respiratory diseases, and represents a serious public health concern. However, the high mutability of influenza viruses has hampered vaccine development, and resistant strains to existing anti-viral drugs have also emerged. Novel anti-influenza therapies are urgently needed, and in this study, we describe the anti-viral properties of a Spirulina (Arthrospira platensis) cold water extract. Anti-viral effects have previously been reported for extracts and specific substances derived from Spirulina, and here we show that this Spirulina cold water extract has low cellular toxicity, and is well-tolerated in animal models at one dose as high as 5,000 mg/kg, or 3,000 mg/ kg/day for 14 successive days. Anti-flu efficacy studies revealed that the Spirulina extract inhibited viral plaque formation in a broad range of influenza viruses, including oseltamivir-resistant strains. Spirulina extract was found to act at an early stage of infection to reduce virus yields in cells and improve survival in influenza-infected mice, with inhibition of influenza hemagglutination identified as one of the mechanisms involved. Together, these results suggest that the cold water extract of Spirulina might serve as a safe and effective therapeutic agent to manage influenza outbreaks, and further clinical investigation may be warranted.

Allophycocyanin (APC) is one of the phycobiliproteins expressed in cyanobacteria. Phycobiliproteins contain a covalently bound chromophore, and thus, they are valuable as fluorescent probes. Biosynthesis of a functional phycobiliprotein is achieved by a bilin attachment process between the chromophore and apoprotein. Chromophore lyases are necessary to catalyze the chromophorylation of cyanobacterial phycobiliproteins, such as C-phycocyanin, and phycoerythrocyanin. To identify the lyase that catalyzes the chromophorylation of the APC alpha-subunit (ApcA), we searched the entire genomes of two cyanobacteria, Synechocystis sp. PCC6803 and Anabaena sp. PCC 7120; however, these genomes do not appear to encode an APC-specific chromophore lyase. In this study, chromophorylated ApcA (chromo-ApcA) was obtained via a spontaneous bilin attachment reaction. The absorption and fluorescence characteristics of chromo-ApcA were similar to those of the native APC alpha-subunit. The extent of chromophore attachment to apo-ApcA was comparable to that of the lyase-catalyzed reactions for other phycobiliproteins. These results indicate that ApcA has autocatalytic bilin:biliprotein lyase activity.

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A novel design for vortex modulation of a passive micromixer, named as the circulation–disturbance micromixer (CDM), has been achieved and analyzed experimentally and numerically. The micromixer consists of slanted grooves on the bottom and a zigzag barrier on the top. In this micromixer, the fluid produces a transverse motion perpendicular to the main field, and two modulated and hyperbolic vortices of disparate size are induced. The active-like agitation produced by the constructive interference of these two vortices induces increased flow through the grooves and the mixing efficiency is hence improved significantly. The 3D flow structure in CDM has been analyzed through both numerical simulation (CFD-ACE+) and two methods of visualization—using dyes and using micro laser-induced fluorescence (μ-LIF, B-phycoerythrin (BPE) and Allophycocyanin alpha subunit (ApcA)) with a confocal microscope. Our results contribute to an understanding of the resulting enhanced hyperbolic flow mixing and provide also a superior microfluidic element for a ‘lab on a chip’. Compared with a slanted groove micromixer, the mixing index of the designed CDM-2T increases 132%, whereas CDM-4T and CDM-8T respectively increase 183% and 280% at Reynolds number 10.

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Highlights d Circular permutation was introduced to untie the topological knot of YbeA d The unknotted circular permutant forms a domain-swapped dimer with reduced stability d Untying the conserved protein knot abrogates cofactor binding essential for function

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