Zika virus (ZIKV), a mosquito-borne flavivirus, is a current global public health concern. The flavivirus envelope (E) glycoprotein is responsible for virus entry and represents a major target of neutralizing antibodies for other flaviviruses. Here, we report the structures of ZIKV E protein at 2.0 Å and in complex with a flavivirus broadly neutralizing murine antibody 2A10G6 at 3.0 Å. ZIKV-E resembles all the known flavivirus E structures but contains a unique, positively charged patch adjacent to the fusion loop region of the juxtaposed monomer, which may influence host attachment. The ZIKV-E-2A10G6 complex structure reveals antibody recognition of a highly conserved fusion loop. 2A10G6 binds to ZIKV-E with high affinity in vitro and neutralizes currently circulating ZIKV strains in vitro and in mice. The E protein fusion loop epitope represents a potential candidate for therapeutic antibodies against ZIKV.

Since April 2010, a severe outbreak of duck viral infection, with egg drop, feed uptake decline and ovary-oviduct disease, has spread around the major duck-producing regions in China. A new virus, named BYD virus, was isolated in different areas, and a similar disease was reproduced in healthy egg-producing ducks, infecting with the isolated virus. The virus was re-isolated from the affected ducks and replicated well in primary duck embryo fibroblasts and Vero cells, causing the cytopathic effect. The virus was identified as an enveloped positive-stranded RNA virus with a size of approximately 55 nm in diameter. Genomic sequencing of the isolated virus revealed that it is closely related to Tembusu virus (a mosquito-borne Ntaya group flavivirus), with 87–91% nucleotide identity of the partial E (envelope) proteins to that of Tembusu virus and 72% of the entire genome coding sequence with Bagaza virus, the most closely related flavivirus with an entirely sequenced genome. Collectively our systematic studies fulfill Koch's postulates, and therefore, the causative agent of the duck egg drop syndrome occurring in China is a new flavivirus. Flavivirus is an emerging and re-emerging zoonotic pathogen and BYD virus that causes severe egg-drop, could be disastrous for the duck industry. More importantly its public health concerns should also be evaluated, and its epidemiology should be closely watched due to the zoonotic nature of flaviviruses.

Carbon dots (CDs) have significant potential for use in various fields including biomedicine, bioimaging, and optoelectronics. However, inefficient excitation and emission of CDs in both near-infrared (NIR-I and NIR-II) windows remains an issue. Solving this problem would yield significant improvement in the tissue-penetration depth for in vivo bioimaging with CDs. Here, an NIR absorption band and enhanced NIR fluorescence are both realized through the surface engineering of CDs, exploiting electron-acceptor groups, namely molecules or polymers rich in sulfoxide/carbonyl groups. These groups, which are bound to the outer layers and the edges of the CDs, influence the optical bandgap and promote electron transitions under NIR excitation. NIR-imaging information encryption and in vivo NIR fluorescence imaging of the stomach of a living mouse using CDs modified with poly(vinylpyrrolidone) in aqueous solution are demonstrated. In addition, excitation by a 1400 nm femtosecond laser yields simultaneous two-photon-induced NIR emission and three-photon-induced red emission of CDs in dimethyl sulfoxide. This study represents the realization of both NIR-I excitation and emission as well as two-photon- and three-photon-induced fluorescence of CDs excited in an NIR-II window, and provides a rational design approach for construction and clinical applications of CD-based NIR imaging agents.

We have developed an efficient chemical exfoliation approach for the high-throughput synthesis of solution-processable, high-quality graphene sheets that are noncovalently functionalized by alkylamine. Purely coherent nonlinear optical response of these graphene sheets has been investigated, using near-infrared, visible, and ultraviolet continous wave and ultrafast laser beams. Spatial self-phase modulation has been unambiguously observed in the solution dispersions. Our results suggest that this coherent light scattering is due to a broadband, ultrafast, and remarkably huge third-order optical nonlinearity χ(3), which is a manifestation of the graphene's cone-shaped large-energy-scale band structure. Our experimental findings endow graphene new potentials in nonlinear optical applications.

We have used scanning tunneling microscopy and spectroscopy to study the electronic structure of individual C 60 molecules adsorbed onto the Au(111) and Ag(100) surfaces. C 60 molecules on Au (111) show an increase in the HOMO-LUMO gap of 0.6 eV compared to C 60 on Ag(100). Splitting of the C 60 LUMO manifold is suppressed for C 60 on Au(111), in contrast to the strong splitting observed for C 60 on Ag(100). Our data implies a 0.6 eV increase in intramolecular Coulomb energy for C 60 on Au(111) as compared to C 60 on Ag(100). Topographs and energy-resolved spectral maps, however, show nearly identical features and indicate a similar influence of the two substrates on molecular-orbital geometry. C 60 -substrate bonding and charge transfer is further investigated by calculating C 60 charge redistribution using ab initio pseudopotential densityfunctional theory methods. These calculations indicate that a negligible amount of charge is transferred from Au(111) to adsorbed C 60 , while about 0.2 electron is transferred to C 60 resting on Ag (100), although the precise amount depends on the definition used. This charge transfer likely changes the electronic screening properties of C 60 , providing an explanation for observed spectroscopic differences on these two substrates.

We have used scanning tunneling spectroscopy to spatially map the energy-resolved local density of states of individual C60 molecules on the Ag(100) surface. Spectral maps were obtained for molecular states derived from the C60 HOMO, LUMO, and LUMO+1 orbitals, revealing new details of the spatially inhomogeneous C60 local electronic structure. Spatial inhomogeneities are explained using ab initio pseudopotential density functional calculations. These calculations emphasize the need for explicitly including the C60-Ag interaction and STM tip trajectory to understand the observed C60 local electronic structure.

Recent studies have identified several mutations in the hemagglutinin (HA) protein that allow the highly pathogenic avian H5N1 influenza A virus to transmit between mammals by airborne route. Here, we determined the complex structures of wild-type and mutant HAs derived from an Indonesia H5N1 virus bound to either avian or human receptor sialic acid analogs. A cis/trans conformational change in the glycosidic linkage of the receptor analog was observed, which explains how the H5N1 virus alters its receptor-binding preference. Furthermore, the mutant HA possessed low affinities for both avian and human receptors. Our findings provide a structural and biophysical basis for the H5N1 adaptation to acquire human, but maintain avian, receptor-binding properties.

A new influenza-like virus genome (H17N10) was recently discovered in bats and offers a new perspective about the origin and evolution of influenza viruses. The viral envelope glycoprotein hemagglutinin (HA) is responsible for influenza virus receptor binding, fusion, and entry into the cell; therefore, the structure and function of HA H17 was characterized. The 2.70 Å resolution crystal structure revealed that H17 has a typical influenza A virus HA fold, but with some special features, including a distorted putative sialic acid (SA) binding site and low thermostability. No binding to either the canonical human α2,6 SA-linkage or avian α2,3 SA-linkage receptor was observed. Furthermore, H17 glycan binding was not detected using a chip covering more than 600 glycans. Our results demonstrate that H17 is unique among characterized HAs and that the bat-derived influenza virus may use a different entry mechanism compared to canonical influenza viruses.