Vomiting and wasting disease associated with hemagglutinating encephalomyelitis viruses infection in piglets in jilin, china

One coronavirus strain was isolated from brain tissues of ten piglets with evident clinical manifestations of vomiting, diarrhea and dyskinesia in Jilin province in China. Antigenic and genomic characterizations of the virus (isolate PHEV-JLsp09) were based on multiplex PCR and negative staining electron microscopy and sequence analysis of the Hemagglutinin-esterase (HE) gene. These piglets were diagnosed with Porcine hemagglutinating encephalomyelitis virus (PHEV)

LysGH15, a Novel Bacteriophage Lysin, Protects a Murine Bacteremia Model Efficiently against Lethal Methicillin-Resistant Staphylococcus aureus Infection▿

Phage-coded lysin is an enzyme that destroys the cell walls of bacteria. Phage lysin could be an alternative to conventional antibiotic therapy against pathogens that are resistant to multiple antibiotics. In this study, a novel staphylococcal phage, GH15, was isolated, and the endogenous lytic enzyme (LysGH15) was expressed and purified. The lysin LysGH15 displayed a broad lytic spectrum; in vitro treatment killed a number of Staphylococcus aureus strains rapidly and completely, including methicillin-resistant S. aureus (MRSA). In animal experiments, a single intraperitoneal injection of LysGH15 (50 μg) administered 1 h after MRSA injections at double the minimum lethal dose was sufficient to protect mice (P < 0.01). Bacteremia in unprotected mice reached colony counts of about 107 CFU/ml within 3.5 h after challenge, whereas the mean colony count in lysin-protected mice was less than 104 CFU/ml (and ultimately became undetectable). These results indicate that LysGH15 can kill S. aureus in vitro and can protect mice efficiently from bacteremia in vivo. The phage lysin LysGH15 might be an alternative treatment strategy for infections caused by MRSA

Low-Temperature Growth of InGaAs Quantum Wells Using Migration-Enhanced Epitaxy

The growth of InGaAs quantum wells (QWs) epitaxially on InP substrates is of great interest due to their wide application in optoelectronic devices. However, conventional molecular beam epitaxy requires substrate temperatures between 400 and 500 °C, which can lead to disorder scattering, dopant diffusion, and interface roughening, adversely affecting device performance. Lower growth temperatures enable the fabrication of high-speed optoelectronic devices by increasing arsenic antisite defects and reducing carrier lifetimes. This work investigates the low-temperature epitaxial growth of InAs/GaAs short-period superlattices as an ordered replacement for InGaAs quantum wells, using migration-enhanced epitaxy (MEE) with low growth temperatures down to 200–250 °C. The InAs/GaAs multi-quantum wells with InAlAs barriers using MEE grown at 230 °C show good single crystals with sharp interfaces, without mismatch dislocations found. The Raman results reveal that the MEE mode enables the growth of (InAs)4(GaAs)3/InAlAs QWs with excellent periodicity, effectively reducing alloy scattering. The room temperature (RT) photoluminescence (PL) measurement shows the strong PL responses with narrow peaks, revealing the good quality of the MEE-grown QWs. The RT electron mobility of the sample grown in low-temperature MEE mode is as high as 2100 cm2/V∗s. In addition, the photoexcited band-edge carrier lifetime was about 3.3 ps at RT. The high-quality superlattices obtained confirm MEE’s effectiveness for enabling advanced III-V device structures at reduced temperatures. This promises improved performance for applications in areas such as high-speed transistors, terahertz imaging, and optical communications

Identification of NCAM that interacts with the PHE-CoV spike protein

Abstract Background The spike proteins of coronaviruses associate with cellular molecules to mediate infection of their target cells. The characterization of cellular proteins required for virus infection is essential for understanding viral life cycles and may provide cellular targets for antiviral therapies. Results We identified Neural Cell Adhesion Molecule (NCAM) as a novel interacting partner of the PHE-CoV S protein. A T7 phage display cDNA library from N2a cells was constructed, and the library was screened with the soluble PHE-CoV S glycoproteins. We used a coimmunoprecipitation assay to show that only the NCAM was a binding partner of spike protein. We found that a soluble form of anti-NCAM antibody blocked association of the PHE-CoV with N2a cells. Furthermore, double-stranded siRNA targeted against NCAM inhibited PHE-CoV infection. Conclusions A novel interaction was identified between NCAM and spike protein and this association is critical during PHE-CoV infection.</p