Protein-mediated bioadhesion is one of the crucial physiological processes in marine organisms, by which they can firmly adhere to underwater substrates. Most marine adhesive organisms are biofoulers, causing negative effects on marine ecosystems and huge economic losses to aquaculture and maritime industries. Furthermore, adhesive proteins in these organisms are promising bionic candidates for high-performance artificial materials with great application value. In-depth understanding of the bioadhesion in marine ecosystems is of dual significance for resolving biofouling issue and developing marine bionic products. Here, we review the research progress of protein-mediated bioadhesion in marine organisms. The adhesion processes such as protein biosynthesis and secretion are similar among organisms, but the detailed features such as compositions, structures, and molecular functions of adhesive proteins are distinct. Hydroxylation, glycosylation, and phosphorylation are important post-translational modifications during the processes of adhesion. The contents of some amino acids such as glycine, tyrosine and cysteine involved in underwater adhesion are significantly higher, which is a sequence feature of barnacle cement and mussel foot proteins. The amyloid structures and conserved domains/motifs such as EGF and vWFA distributed in adhesive proteins are involved in the underwater adhesion. In addition, the oxidative cross-linking also plays an important role in marine bioadhesion. Overall, the unique and common features identified for the protein-mediated bioadhesion in diverse marine organisms here provide background information and essential reference for characterizing marine adhesive proteins and associated functional domains, formulating antifouling strategies, and developing novel biomimetic adhesives.A large (~2450 km2) offshore (~75 km) targeted fisheries closure (TFC) area was implemented on the North West Shelf of Australia (NWS) in 1998 as part of a suite of management controls to address overfishing concerns, and in the process to potentially mitigate any impacts of trawling to benthic habitats. Twelve years later, the benthic biota and fish assemblages in the TFC were assessed using stereo-video and compared with adjacent areas that have been consistently fished with a range of commercial fishing methods.  https://www.selleckchem.com/products/ozanimod-rpc1063.html  The remote nature of the region has meant that these areas would be inaccessible to recreational fishers. After 12 years of protection there were significant differences between the TFC and comparable fished areas in both the composition and the height of biogenic structures, however the magnitude of these differences were subtle, except for branching soft corals, which were significantly taller in the TFC area. Despite the relatively young age of the TFC, significant differences in the fish abunda to examine the natural variability, growth and recovery of benthic biota and fish assemblages after the cessation of fishing.Candida auris is an emerging yeast pathogen with worldwide distribution and a great propensity for nosocomial spread. Recent reports have warned of the significant emergence of C. auris in several healthcare facilities. In order to stop its nosocomial transmission, use of antiseptics constitutes the first-line lever of action in the fighting against C. auris skin colonization. However, little is known about the efficacy of these products, and moreover no antiseptics are currently registered for use against C. auris. This study investigated the in vitro yeasticidal activity of povidone-iodine against C. auris, and compared the findings to C. albicans and C. glabrata, according to the EN standard 12752005. Results support the use of such commercial antiseptics in the context of colonization with this yeast.Three undescribed oleanane type triterpenoid saponins (1-3), along with one known saponin (4) were isolated from the whole herb of Hylomecon japonica. Their structures were elucidated by analysis of 1D and 2D-NMR (1H-1H COSY, HSQC, and HMBC) spectroscopic data, mass spectrometry (HR-ESI-MS) and chromatographic date (GC and LC) as 3-O-β-d-glucopyranosyl-(1 → 2)-β-d-glucuronopyranosyl gypsogenin 28-O-β-d-galactopyranosyl-(1 → 3)-[β-d-xylopyranosyl-(1 → 4)]-α-l-rhamnopyranosyl-(1 → 2)-β-l-arabinopyranosyl ester (1), 3-O-β-d-galactopyranosyl-(1 → 2)-β-d-glucuronopyranosyl gypsogenin 28-O-α-l-arabinopyranosyl-(1 → 3)-[β-d-xylopyranosyl-(1 → 4)]-α-l-rhamnopyranosyl-(1 → 2)-β-l-arabinopyranosyl ester (2), 3-O-β-d-galactopyranosyl-(1 → 2)-β-d-glucuronopyranosyl gypsogenin 28-O-β-d-galactopyranosyl-(1 → 3)-[β-d-xylopyranosyl-(1 → 4)]-α-l-rhamnopyranosyl-(1 → 2)-β-d-galactopyranosyl ester (3), 3-O-β-d-galactopyranosyl-(1 → 2)-[α-l-arabinopyranosyl-(1 → 3)]-β-d-glucuronopyranosyl gypsogenin 28-O-β-d-glucopyranosyl-(1 → 3)-[β-d-xylopyranosyl-(1 → 4)]-α-l-rhamnopyranosyl-(1 → 2)-β-d-fucopyranosyl ester (4). All saponins possess a partial sequence β-d-galactopyranosyl-(1 → 2)-β-d-glucuronopyranosyl at C-3 of the aglycon. Compound 1 has cytotoxic activity against human colon cancer cell lines HT29, 3 against human gastric cancer cell lines AGS, and 4 against human lung cancer cell lines A549, AGS and HT29. Among them, compounds 3 and 4 showed significant inhibitory effect against AGS with IC50 value of 6.01 ± 1.4 μM, 3.66 ± 1.8 μM, respectively. These results represent a contribution to the chemotaxonomy of the saponins of Hylomecon japonica and their bioactivities.Considering the importance of bacterial glycoconjugates on virulence and host mimicry, there is a need to better understand the biosynthetic pathways of these unusual sugars to identify critical targets involved in bacterial pathogenesis. In this report, we describe the cloning, overexpression, purification, and biochemical characterization of the four central enzymes in the biosynthesis pathway for UDP-2-acetamido-4-formamido-2,4,6-trideoxy-hexose, WekG, WekE, WekF, and WekD. Product peaks from enzyme-substrate reactions were detected by using a combination of capillary electrophoresis (CE) and electrospray ionization-mass spectrometry (ESI-MS). Putative enzyme assignments were provided by protein sequence analysis. Combined with the mass spectrometric characterization of pathway intermediates, we propose a biosynthetic pathway for UDP-2-acetamido-4-formamido-2,4,6-trideoxy-hexose. This process involves C-4, C-6 dehydration, C-4 amination, and formylation. CID-ESI-MSn result confirmed that the final product is a 4 formamido derivative too rather than the 3 formamido derivatives as reported earlier.