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Waves can drastically transform a sea ice cover by inducing break-up over vast distances in the course of a few hours. However, relatively few detailed studies have described this phenomenon in a quantitative manner, and the process of sea ice break-up by waves needs to be further parameterized and verified before it can be reliably included in forecasting models. In the present work, we discuss sea ice break-up parameterization and demonstrate the existence of an observational threshold separating breaking and non-breaking cases. This threshold is based on information from two recent field campaigns, supplemented with existing observations of sea ice break-up. The data used cover a wide range of scales, from laboratory-grown sea ice to polar field observations. Remarkably, we show that both field and laboratory observations tend to converge to a single quantitative threshold at which the wave-induced sea ice break-up takes place, which opens a promising avenue for robust parametrization in operational forecasting models.

Rapid development of spin noise spectroscopy of the last decade has led to a number of remarkable achievements in the fields of both magnetic resonance and optical spectroscopy. In this report, we demonstrate a new – magnetometric – potential of the spin noise spectroscopy and use it to study magnetic fields acting upon electron spin-system of an n -GaAs layer in a high-Q microcavity probed by elliptically polarized light. Along with the external magnetic field, applied to the sample, the spin noise spectrum revealed the Overhauser field created by optically oriented nuclei and an additional, previously unobserved, field arising in the presence of circularly polarized light. This “optical field” is directed along the light propagation axis, with its sign determined by sign of the light helicity. We show that this field results from the optical Stark effect in the field of the elliptically polarized light. This conclusion is supported by theoretical estimates.

Glycans of MVs are proposed to be candidates for mediating targeting specificity or at least promoting it. In contrast to exosomes, glycomic studies of MVs are largely absent. We studied the glycoprofile of endothelial cell-derived MVs using 21 plant lectins, and the results show the dominance of oligolactosamines and their α2-6-sialylated forms as N-glycans and low levels of α2-3-sialylated glycans. The low levels of α2-3-sialosides could not be explained by the action of extracellular glycosidases. Additionally, the level of some Man-containing glycans was also decreased in MVs. Spatial masking as the causative relationship between these low level glycans (as glycosphingolipids) by integral proteins or proteoglycans (thus, their lack of interaction with lectins) seems unlikely. The results suggest that integral proteins do not pass randomly into MVs, but instead only some types, differing in terms of their specific glycosylation, are integrated into MVs.

The methods of data collection, processing, and assessment of the quality of the results of a survey conducted at the Southern Ionian Sea off the Messinian Peninsula, Greece are presented. Data were collected by the GEBCO-Nippon Foundation Alumni Team, competing in the Shell Ocean Discovery XPRIZE, during the Final Round of the competition. Data acquisition was conducted by the means of unmanned vehicles only. The mapping system was composed of a single deep water AUV (Autonomous Underwater Vehicle), equipped with a high-resolution synthetic aperture sonar HISAS 1032 and multibeam echosounder EM 2040, partnered with a USV (Unmanned Surface Vessel). The USV provided positioning data as well as mapping the seafloor from the surface, using a hull-mounted multibeam echosounder EM 304. Bathymetry and imagery data were collected for 24 h and then processed for 48 h, with the extensive use of cloud technology and automatic data processing. Finally, all datasets were combined to generate a 5-m resolution bathymetric surface, as an example of the deep-water mapping capabilities of the unmanned vehicles’ cooperation and their sensors’ integration.

Many viruses, beside binding to their main cell target, interact with other molecules that promote virus adhesion to the cell; often, these additional targets are glycans. The main receptor for SARS-CoV-2 is a peptide motif in the ACE2 protein. We studied interaction of the recombinant SARS-CoV-2 spike (S) protein with an array of glycoconjugates, including various sialylated, sulfated, and other glycans, and found that the S protein binds some (but not all) glycans of the lactosamine family. We suggest that parallel influenza infection will promote SARS-CoV-2 adhesion to the respiratory epithelial cells due to the unmasking of lactosamine chains by the influenza virus neuraminidase.

The recruitment of leukocytes from blood is one of the most important cellular processes in response to tissue damage and inflammation. This multi-step process includes rolling leukocytes and their adhesion to endothelial cells (EC), culminating in crossing the EC barrier to reach the inflamed tissue. Galectin-8 and galectin-9 expressed on the immune system cells are part of this process and can induce cell adhesion via binding to oligolactosamine glycans. Similarly, these galectins have an order of magnitude higher affinity towards glycans of the ABH blood group system, widely represented on ECs. However, the roles of gal-8 and gal-9 as mediators of adhesion to endothelial ABH antigens are practically unknown. In this work, we investigated whether H antigen–gal-9-mediated adhesion occurred between Jurkat cells (of lymphocytic origin and known to have gal-9) and EA.hy 926 cells (immortalized endothelial cells and known to have blood group H antigen). Baseline experiments showed that Jurkat cells adhered to EA.hy 926 cells; however when these EA.hy 926 cells were defucosylated (despite the unmasking of lactosamine chains), adherence was abolished. Restoration of fucosylation by insertion of synthetic glycolipids in the form of H (type 2) trisaccharide Fucα1-2Galβ1-4GlcNAc restored adhesion. The degree of lymphocyte adhesion to native and the “H-restored” (glycolipid-loaded) EA.hy 926 cells was comparable. If this gal-9/H (type 2) interaction is similar to processes that occur in vivo, this suggests that only the short (trisaccharide) H glycan on ECs is required.

Modification of vaccine carriers by decoration with glycans can enhance binding to and even targeting of dendritic cells (DCs), thus augmenting vaccine efficacy. To find a specific glycan-“vector” it is necessary to know glycan-binding profile of DCs. This task is not trivial; the small number of circulating blood DCs available for isolation hinders screening and therefore advancement of the profiling. It would be more convenient to employ long-term cell cultures or even primary DCs from murine blood. We therefore examined whether THP-1 (human monocyte cell line) and DC2.4 (immature murine DC-like cell line) could serve as a model for human DCs. These cells were probed with a set of glycans previously identified as binding to circulating human CD14low/-CD16+CD83+ DCs. In addition, we tested a subpopulation of murine CD14low/-CD80+СD11c+CD16+ cells reported as relating to the human CD14low/-CD16+CD83+ cells. Manα1–3(Manα1–6)Manβ1–4GlcNAcβ1–4GlcNAcβ bound to both the cell lines and the murine CD14low/-CD80+СD11c+CD16+ cells. Primary cells, but not the cell cultures, were capable of binding GalNAcα1–3Galβ (Adi), the most potent ligand for binding to human circulating DCs. In conclusion, not one of the studied cell lines proved an adequate model for DCs processes involving lectin binding. Although the glycan-binding profile of BYRB-Rb (8.17)1Iem mouse DCs could prove useful for assessing human DCs, important glycan interactions were missing, a situation which was aggravated when employing cells from the BALB/c strain. Accordingly, one must treat results from murine work with caution when seeking vaccine targeting of human DCs, and certainly should avoid cell lines such as THP-1 and DC2.4 cells.

Dendritic cells (DCs) play crucial roles in innate and adaptive immune response, for which reason targeting antigen to these cells is an important strategy for improvement of vaccine development. To this end, we explored recognition of DCs lectins by glycans. For selection of the glycan “vector”, a library of 229 fluorescent glycoprobes was employed to assess interaction with the CD14low/-CD16+CD83+ blood mononuclear cell population containing the DCs known for their importance in antigen presentation to T-lymphocytes. It was found that: 1) the glycan-binding profiles of this CD14low/-CD16+CD83+ subpopulation were similar but not identical to DCs of monocyte origin (moDCs); 2) the highest percentage of probe-positive cells in this CD14 low/-CD16+CD83+ subpopulation was observed for GalNAcα1-2Galβ (Adi), (Neu5Acα)3 and three mannose-reach glycans; 3) subpopulation of CD14low/-CD16+ cells preferentially bound 4’-O-Su-LacdiNAc. Considering the published data on specificity of DCs binding, the glycans showing particular selectivity for the CD14 low/-CD16+CD83+ cells are likely interacting with macrophage galactose binding lectin (MGL), siglec-7 and dectin-2. In contrast, DC-SIGN is not apparently involved, even in case of mannose-rich glycans. Taking into consideration potential in vivo competition between glycan “vectors” and glycans within glycocalyx, attempting to target vaccine to DCs glycan-binding receptors should focus on Adi and (Neu5Acα)3 as the most promising vectors.

The synthetic function‐spacer‐lipid (FSL) amphiphile biotin‐CMG‐DOPE is widely used for delicate ligation of living cells with biotin residues under physiological conditions. Since this molecule has an “apolar‐polar‐hydrophobic” gemini structure, the supramolecular organization is expected to differ significantly from the classical micelle. Its organization is investigated with experimental methods and molecular dynamics simulations (MDS). Although the linear length of a single biotin‐CMG‐DOPE molecule is 9.5 nm, the size of the dominant supramer globule is only 14.6 nm. Investigations found that while the DOPE tails form a hydrophobic core, the polar CMG spacer folds back upon itself and predominantly places the biotin reside inside the globule or planar layer. MDS demonstrates that <10 % of biotin residues on the highly water dispersible globules and only 1 % of biotin residues in layer coatings are in an linear conformation and exposing biotin into the aqueous medium. This explains why in biotin‐CMG‐DOPE apolar biotin residues both in water dispersible globules and coatings on solid surfaces are still capable of interacting with streptavidin. Binding cells together: Gemini amphiphile biotin‐CMG‐DOPE when coated on a surface forms a monolayer where quite non‐polar biotin residues are hidden in the hydrophobic DOPE zone, however ∼1 % of biotins are able to dynamically pop‐up and, therefore, bind to streptavidin.

Invited for this month's cover is the group of Prof. Nicolai Bovin from the Russian Academy of Sciences. The cover picture shows how a biotin residue initially hidden in a monolayer formed on the surface of a material by biot‐CMG‐DOPE (see top left) is pulled out of the layer by the streptavidin molecule (Str) that has come close to it (see below). This can be considered as a model of certain events (in particular, cis protein‐ligand interactions) occurring on the surface of a living cell when it is necessary to hide the ligand from undesirable interactions, but leave the possibility of its recognition by a high‐affinity protein. The picture is inspired by the legendary Yellow Submarine cartoon. Read the full text of their Full Paper at 10.1002/open.201900276. “…In real‐life biology, this is an ordinary scenario. For scientists, it is practically unexplored… Find out more about the story behind the front cover research at 10.1002/open.201900276.