Development and evaluation of a time-saving RT-qRPA method for the detection of genotype 4 HEV presence in raw pork liver.

Hepatitis E virus (HEV) is a zoonotic pathogen spreading worldwide. Pig was known as its first and main animal reservoir. In China, pork consumption is very large and the risk of potential HEV contamination should not be underestimated.

Preparation and evaluation of MS2 bacteriophage-like particles packaging hepatitis E virus RNA.

Hepatitis E virus (HEV) is the pathogen causing hepatitis E (HE). It arouses global public health concern since it is a zoonotic disease. The objective of this letter is to report a cost-effective internal control prepared for monitoring procedures of HEV reverse transcriptase (RT)-PCR detection.

A recombinant polypeptide from velvet antler of Cervus nippon Temminck exhibits similar immunomodulatory effects as its natural counterpart.

Context: Velvet antler (VA) is recognized as one of the most important Chinese traditional medical herbs. To date, the immunoactivity of the single component of VA is rarely studied though its compound extracts have been well analyzed.

Objective: The current study was designed to evaluate the immunomodulatory effects of a recombinant polypeptide (rVAP32) based on the VA of the sika deer by comparison with its natural counterpart (nVAP32).

Development and evaluation of a RT-LAMP assay for rapid detection of hepatitis E virus from shellfish.

Hepatitis E virus (HEV) has becoming a well known zoonotic enteric pathogen and circulated widely inter human-animal-water-food. Generally, detection of the virus has relied on conventional reverse transcription-PCR (RT-PCR) and TaqMan/SYBR quantitative real-time RT-PCR (RT-qPCR), but these tools are usually disadvantages in time-consuming and expensive instruments required. In the present study, we report here on the development of a one-step single-tube reverse transcription-loop-mediated isothermal amplification (RT-LAMP) assay for rapid detection of HEV contamination in shellfish.

Surveillance of hepatitis E virus contamination in shellfish in China.

Background: Hepatitis E virus (HEV) has been confirmed to be a zoonotic virus of worldwide distribution. HEV contamination in the water environment has not been well examined in China. The objective of this study was to evaluate HEV contamination in shellfish in a coastal area of China.

Oral immunization with recombinant hepatitis E virus antigen displayed on the Lactococcus lactis surface enhances ORF2-specific mucosal and systemic immune responses in mice.

Hepatitis E virus (HEV) as a recognized zoonotic pathogen has posed global burden on public health, which is exacerbated by lack of efficient vaccine. In this study, we constructed a recombinant (inaQ-ORF2 gene fusion) Lactococcus lactis (L. lactis) strain NZ3900 that expresses and displays the hepatitis E virus antigen ORF2 utilizing an ice uncleation protein-based anchor system.

Immunomodulatory effects of a 3.2kDa polypeptide from velvet antler of Cervus nippon Temminck.

The objective of this study was to evaluate the immunomodulatory effects of a native 3.2kDa polypeptide of velvet antler from sika deer (nVAP32) on BALB/c mice immunocytes. In vitro tests showed that nVAP32 significantly stimulated splenocyte proliferation and enhanced the NK cytotoxicity and CD4(+)/CD8(+) cell subpopulations.

Wound healing by a 3.2 kDa recombinant polypeptide from velvet antler of Cervus nippon Temminck.

Velvet antler (VA) is used in traditional Chinese medicine to treat a wide range of ailments including the enhancement of wound healing. A 3.2 kDa recombinant polypeptide of VA from sika deer was purified and compared to native polypeptides stimulation growth of NIH3T3 cells.

High-level prokaryotic expression of envelope exterior of membrane protein of porcine epidemic diarrhea virus.

The truncated fragment M' gene, encoding the exterior of the viral envelope protein of PEDV, was subcloned into prokaryotic expression vector pGEX-6p-1. The recombinant plasmid pGEX-6p-M' was constructed and transformed into E. coli BL21(DE3)pLysS for expression.