The giant panda (Ailuropoda melanoleuca) and red panda (Ailurus fulgens), two obligate bamboo feeders, have distinct phylogenetic positions in the order Carnivora. Bamboo is extraordinarily rich in plant secondary metabolites, such as allied phenolic and polyphenolic compounds and even toxic cyanide compounds. Here, the enrichment of putative cyanide-digesting gut microbes, in combination with adaptations related to morphology (e.g., pseudothumbs) and genomic signatures, show that the giant panda and red panda have evolved some common traits to adapt to their bamboo diet. Thus, here is another story of diet-driven gut microbiota in nature.

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Developing cost‐effective and high‐performance catalysts for oxygen evolution reaction (OER) is essential to improve the efficiency of electrochemical conversion devices. Unfortunately, current studies greatly depend on empirical exploration and ignore the inherent relationship between electronic structure and catalytic activity, which impedes the rational design of high‐efficiency OER catalysts. Herein, a series of bimetallic Ni‐based metal‐organic frameworks (Ni‐M‐MOFs, M = Fe, Co, Cu, Mn, and Zn) with well‐defined morphology and active sites are selected as the ideal platform to explore the electronic‐structure/catalytic‐activity relationship. By integrating density‐functional theory calculations and experimental measurements, a volcano‐shaped relationship between electronic properties (d‐band center and eg filling) and OER activity is demonstrated, in which the NiFe‐MOF with the optimized energy level and electronic structure situated closer to the volcano summit. It delivers ultra‐low overpotentials of 215 and 297 mV for 10 and 500 mA cm−2, respectively. The identified electronic‐structure/catalytic activity relationship is found to be universal for other Ni‐based MOF catalysts (e.g., Ni‐M‐BDC‐NH2, Ni‐M‐BTC, Ni‐M‐NDC, Ni‐M‐DOBDC, and Ni‐M‐PYDC). This work widens the applicability of d band center and eg filling descriptors to activity prediction of MOF‐based electrocatalysts, providing an insightful perspective to design highly efficient OER catalysts.

Sorting nexins (SNXs) are phosphoinositide-binding proteins implicated in the sorting of various membrane proteins in vitro, but the in vivo functions of them remain largely unknown. We reported previously that SNX10 is a unique member of the SNX family genes in that it has vacuolation activity in cells. We investigate the biological function of SNX10 by loss-of-function assay in this study and demonstrate that SNX10 is required for the formation of primary cilia in cultured cells. In zebrafish, SNX10 is involved in ciliogenesis in the Kupffer's vesicle and essential for left-right patterning of visceral organs. Mechanistically, SNX10 interacts with V-ATPase complex and targets it to the centrosome where ciliogenesis is initiated. Like SNX10, V-ATPase regulates ciliogenesis in vitro and in vivo and does so synergistically with SNX10. We further discover that SNX10 and V-ATPase regulate the ciliary trafficking of Rab8a, which is a critical regulator of ciliary membrane extension. These results identify an SNX10/V-ATPaseregulated vesicular trafficking pathway that is crucial for ciliogenesis, and reveal that SNX10/V-ATPase, through the regulation of cilia formation in various organs, play an essential role during early embryonic development.

Highly efficient recovery of uranium from seawater is of great concern because of the growing demand for nuclear energy. The use of amidoximebased polymeric fiber adsorbents is considered to be a promising approach because of their relatively high specificity and affinity to uranyl. The surface area, hydrophility, and surface charge of the adsorbent are reported to be critical factors that influence uranium recovery efficiency. Here, a porous amidoxime-based nanofiber adsorbent (SMON-PAO) that exhibits the highest uranium recovery capacity among the existing fiber adsorbents both in 8 ppm uranium spiked seawater (1089.36 ± 64.31 mg-U per g-Ads) and in natural seawater (9.59 ± 0.64 mg-U per g-Ads) is prepared by blow spinning. These nanofibers are obtained by compositing polyacrylamidoxime with montmorillonite and exhibit the increased surface area and more exposed functional amidoxime moieties for uranyl adsorption. The residual montmorillonite enhances the hydrophility and reduces the negative surface charge, thereby increasing the contact of the adsorbent with seawater and reducing the charge repulsion between negative amidoxime group and negative uranyl species ([UO 2 (CO 3 ) 3 ] 4− ). The finding of this study indicates that rational design of uranium recovery adsorbents by comprehensive utilizing the key factors that influence uranium recovery performance is a promising approach for developing economically feasible uranium recovery materials.

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H9N2 influenza virus is undergoing extensive genetic and antigenic evolution, warranting detailed antigenic mapping of its hemagglutinin (HA). Through examining antibody escape mutants of an Asian avian H9N2 virus, we identified 9 critical amino acid positions in H9 antigenic sites. Five of these positions, 164, 167, 168, 196, and 207, have not been reported previously and, thus, represent novel molecular markers for monitoring the antigenic change of H9N2 virus. H9N2 influenza virus is circulating in poultry worldwide. H9N2 virus infection is usually mild in nature but may lead to higher mortality if it is associated with secondary infection (1, 2). In Asia, since its introduction into land-based poultry in the late 1980s, H9N2 virus has been spreading to various avian and mammalian species, including pigs (3, 4). Due to the Q226L mutation (change of Gln to Leu at position 226) in the hemagglutinin (HA) (5-7), a significant proportion of H9N2 isolates have acquired human virus-like receptor specificity (5,8). Consistent with this receptor specificity change, multiple human cases of H9N2 virus infection have been reported (9-12). Moreover, H9N2 virus has provided internal genes for the highly pathogenic H5N1 (9, 13, 14) and novel H7N9 (15) viruses. These have put H9N2 virus high on the list of influenza viruses with pandemic potential.Although the crystal structure of H9 has been solved (16), no details for H9 antigenic epitopes have been elucidated. Previous investigations by other groups have identified multiple amino acids in H9 antigenic sites (17, 18). These are nevertheless far from being sufficient for understanding the H9 antigenic structure. To identify more amino acids constituting H9 antigenic sites, we performed an antigenic mapping of the HA of an avian H9N2 virus A/Chicken/Jiangsu/X1/2004 (hereinafter called X1) (GenBank nucleotide sequence accession number KF688983) with monoclonal antibodies (MAbs).H9-specific MAbs were generated through the fusion of myeloma Sp2/0 cells with splenocytes from a BALB/c mouse immunized with X1 virus (19). The immunization included 3 intraperitoneal inoculations at 2-week intervals and a final boost with live X1 virus (on day 3 before the fusion). Hybridomas were screened by indirect immunofluorescence assay using chicken embryo fibroblast cells infected with X1 virus as the antigen, followed by screening with a hemagglutination inhibition (HI) assay using 4 hemagglutination units of X1 virus (20). Ascitic fluid of each selected hybridoma was generated in mice and used directly (e.g., without further purification or treatment with receptor-destroying enzyme) in the characterization of each MAb. All animal experiments were done in accordance with the institutional animal care guidelines, and the protocol (number 06R015) was approved by the Animal Care Committee at Yangzhou University. A microneutralization (MN) assay was performed in Madin-Darby canine kidney (MDCK) cells, following a previous protocol (21), except that 100 median tissue infectious doses (TCID 50 ) o...

Sorting nexin 33 (SNX33) is a novel member of the sorting nexin superfamily with three predicted structural domains, SH3-PX-BAR. Very little is known about the cellular function of SNX33. In an effort to analyze its structure/function relationship, we attempted but failed to generate stable cell lines for short hairpin RNA or overexpression SNX33. Transient knockdown of SNX33 induces both HeLa and MCF7 cells to grow multiple long processes, delay the G 1 /M transition, and become more apoptotic, implying that SNX33 may control cell cycle process through influence the cytoskeleton. In vitro cell lineage analysis revealed that cells transfected with SNX33 failed to divide and became micronucleated, suggesting a specific defect in cytokinesis. Further analysis revealed that SNX33 induced the accumulation of actin at the perinuclear space, which might have disabled the cytokinetic machinery. However, SNX33 appears to mediate actin polymerization indirectly, as they do not interact with each other. SNX33 interacts with itself and SNX9. Interestingly, it also interacts with VCA domain of Wiskott-Aldrich syndrome protein (WASp), a protein known to be involved in actin polymerization. Indeed, cells overexpressing WASp failed to divide and form stable colonies as SNX33, consistent with the notion that SNX33 may interfere with cytokinesis. On the other hand, knockdown of WASp alleviates the phenotype induced by SNX33. Taken together, our results suggest that SNX33 plays a role in maintaining cell shape and cell cycle progression through its interaction with WASp.Among SNX (sorting nexin) family, SNX1 was first identified by yeast two-hybrid selection for epidermal growth factor receptor binding partners (1), which also include SNX2, SNX3, and SNX4 (2). Interestingly, SNX1, SNX2 and SNX4 appear to interact with each other (3-5). Subsequently, more SNXs were discovered based on sequence homology, including SNX5 as a putative Fanconi anemia complementation group A-binding protein (6), SNX6 (7), and SNX9 (8, 9). SNX10 was discovered by its ability to induce vacuoles in mammalian cells (10). To date, 33 SNXs have been reported in mammalian genomes, and they can be classified into three major groups; (i) SNX PX (SNX3, -10, -12, -22, and -24); (ii) SNX PX-BAR (SNX1, -2, -4 -9, -18, -30, -32, and -33); (iii) SNX PX-other (SNX11, -13-17, -19 -21, -25, -27, -29, and -31) (11). The physiological function of these SNXs remains poorly understood.SNX33 is a novel SNX with three conserved domains: SH3, PX, and BAR. Recent studies suggest that SNX33 may function to regulate endocytic process and ␣-secretase cleavage process of the amyloid precursor protein (12) and the formation of PrP (13). These functions are similar to those reported for SNX9, a close relative of SNX33. SNX9 was identified as a binding partner for MDC9 and MDC15 (8). It appears that SNX9 functions through ACK2 to regulate epidermal growth factor receptor degradation with necessary dimerization of itself (9, 14), Wiskott-Aldrich syndrome protein (WASp) in T cells (15),...