Generalized Tu Formula and Hamilton Structures of Fractional Soliton Equation Hierarchy

With the modified Riemann-Liouville fractional derivative, a fractional Tu formula is presented to investigate generalized Hamilton structure of fractional soliton equations. The obtained results can be reduced to the classical Hamilton hierachy of ordinary calculus.Comment: 12 p

Lego-Microfluidics Generated Magnetically Responsive Bifunctional Microcapsules with Encapsulated Phase Change Material

We report an innovative Lego-microfluidic technology for room temperature synthesis of highly monodispersed bifunctional microcapsules enclosing phase change material (PCM), exhibiting magnetic and thermal energy storage properties. Iron(II, III) oxide (Fe$_3$O$_4$) nanoparticle-embedded microcapsules encapsulating hexadecane (HD) are synthesized without external heating or cooling in just ∼80 s. The process involves forming oil-in-oil-in-water (O/O/W) double emulsion droplets with Norland Optical Adhesive (NOA) photopolymeric shell and consolidating them through on-the-fly shell polymerization using thiol–ene “click” chemistry. PCM content and magnetic properties were accurately manipulated by adjusting inner phase (PCM) flow rate and mass fraction of Fe$_3$O$_4$ nanoparticles in the middle (polymer) phase. Microcapsules with a shell thickness of 17.1 μm achieved a maximum PCM content of 63.3%. Thermogravimetric analysis (TGA) revealed significantly enhanced thermal stability of Fe$_3$O$_4$ nanoparticle-embedded microcapsules compared to pure PCM. Vibrating sample magnetometry (VSM) verified an increase in saturation magnetization and residual magnetization of microcapsules, having higher Fe$_3$O$_4$ nanoparticle content. Notably, the sample containing 1% Fe$_3$O$_4$ nanoparticles exhibited excellent magnetic properties, showcasing a saturation magnetization of 0.194 emu/g. Concurrently, the PCM microcapsules demonstrated high magnetic responsiveness and maneuverability

Cyanobacteria and Chloroflexota cooperate to structure light-responsive biofilms

Microbial mats are stratified communities often dominated by unicellular and filamentous phototrophs within an exopolymer matrix. It is challenging to quantify the dynamic responses of community members in situ as they experience steep gradients and rapid fluctuations of light. To address this, we developed a binary consortium using two representative isolates from hot spring mats: the unicellular oxygenic phototrophic cyanobacterium Synechococcus OS-B′ (Syn OS-B′) and the filamentous anoxygenic phototroph Chloroflexus MS-CIW-1 (Chfl MS-1). We quantified the motility of individual cells and entire colonies and demonstrated that Chfl MS-1 formed bundles of filaments that moved in all directions with no directional bias to light. Syn OS-B′ was slightly less motile but exhibited positive phototaxis. This binary consortium displayed cooperative behavior by moving further than either species alone and formed ordered arrays where both species aligned with the light source. No cooperative motility was observed when a nonmotile pilB mutant of Syn OS-B′ was used instead of Syn OS-B′. The binary consortium also produced more adherent biofilm than individual species, consistent with the close interspecies association revealed by electron microscopy. We propose that cyanobacteria and Chloroflexota cooperate in forming natural microbial mats by colonizing new niches and building robust biofilms

Glycan shield of the ebolavirus envelope glycoprotein GP

The envelope glycoprotein GP of the ebolaviruses is essential for host cell entry and the primary target of the host antibody response. GP is heavily glycosylated with up to 17 N-linked sites, numerous O-linked glycans in its disordered mucin-like domain (MLD), and three predicted C-linked mannosylation sites. Glycosylation is important for host cell attachment, GP stability and fusion activity, and shielding from neutralization by serum antibodies. Here, we use glycoproteomics to profile the site-specific glycosylation patterns of ebolavirus GP. We detect up to 16 unique O-linked glycosylation sites in the MLD, and two O-linked sites in the receptor-binding GP1 subunit. Multiple O-linked glycans are observed within N-linked glycosylation sequons, suggesting crosstalk between the two types of modifications. We confirmed C-mannosylation of W288 in full-length trimeric GP. We find complex glycosylation at the majority of N-linked sites, while the conserved sites N257 and especially N563 are enriched in unprocessed glycans, suggesting a role in host-cell attachment via DC-SIGN/L-SIGN. Our findings illustrate how N-, O-, and C-linked glycans together build the heterogeneous glycan shield of GP, guiding future immunological studies and functional interpretation of ebolavirus GP-antibody interactions

Glycan shield of the ebolavirus envelope glycoprotein GP

The envelope glycoprotein GP of the ebolaviruses is essential for host cell entry and the primary target of the host antibody response. GP is heavily glycosylated with up to 17 N-linked sites, numerous O-linked glycans in its disordered mucin-like domain (MLD), and three predicted C-linked mannosylation sites. Glycosylation is important for host cell attachment, GP stability and fusion activity, and shielding from neutralization by serum antibodies. Here, we use glycoproteomics to profile the site-specific glycosylation patterns of ebolavirus GP. We detect up to 16 unique O-linked glycosylation sites in the MLD, and two O-linked sites in the receptor-binding GP1 subunit. Multiple O-linked glycans are observed within N-linked glycosylation sequons, suggesting crosstalk between the two types of modifications. We confirmed C-mannosylation of W288 in full-length trimeric GP. We find complex glycosylation at the majority of N-linked sites, while the conserved sites N257 and especially N563 are enriched in unprocessed glycans, suggesting a role in host-cell attachment via DC-SIGN/L-SIGN. Our findings illustrate how N-, O-, and C-linked glycans together build the heterogeneous glycan shield of GP, guiding future immunological studies and functional interpretation of ebolavirus GP-antibody interactions