Song L.-W.,National Institute of Diagnostics and Vaccine Development in Infectious Diseases |
Liu P.-G.,Xiamen University |
Liu C.-J.,National Taiwan University |
Zhang T.-Y.,National Institute of Diagnostics and Vaccine Development in Infectious Diseases |
And 13 more authors.
Clinical Microbiology and Infection
We previously demonstrated that pretreatment quantitative anti-hepatitis B core protein (qAnti-HBc) levels can predict the treatment response for both interferon and nucleoside analogue therapy, but the characteristics of qAnti-HBc during chronic hepatitis B virus (HBV) infection remain poorly understood. To understand this issue, the qAnti-HBc levels were evaluated in individuals with past HBV infection, occult HBV infection and chronic HBV infection in the immune tolerance phase, immune clearance phase, low-replicative phase and hepatitis B e antigen (HBeAg)-negative hepatitis phase. Individuals with hepatitis B surface antigen (n=598, 3.74±0.90 log10 IU/mL) had significantly higher (p<0.001, approximately 1000-fold) serum qAnti-HBc levels than those who had occult HBV, and serum qAnti-HBc levels were significantly higher in the occult HBV group than in the past HBV infection group (p<0.001). qAnti-HBc levels were positively correlated with alanine aminotransferase levels (R=0.663, p<0.001), and subjects with an abnormal alanine aminotransferase level had a higher qAnti-HBc level (p<0.001). Serum qAnti-HBc level varied in different phases of HBV infection, as determined by host immune status. Serum qAnti-HBc level is strongly associated with hepatitis activity in subjects with chronic HBV infection. © 2014 European Society of Clinical Microbiology and Infectious Diseases. Source
Zhao M.,National Institute of Diagnostics and Vaccine Development in Infectious Diseases |
Li X.-J.,National Institute of Diagnostics and Vaccine Development in Infectious Diseases |
Tang Z.-M.,Xiamen University |
Yang F.,Xiamen University |
And 6 more authors.
Journal of Biological Chemistry
The hepatitis E virus (HEV) ORF2 encodes a single structural capsid protein. The E2s domain (amino acids 459-606) of the capsid protein has been identified as the major immune target. All identified neutralizing epitopes are located on this domain; however, a comprehensive characterization of antigenic sites on the domain is lacking due to its high degree of conformation dependence. Here, we used the statistical software SPSS to analyze cELISA (competitive ELISA) data to classify monoclonal antibodies (mAbs), which recognized conformational epitopes on E2s domain. Using this novel analysis method, we identified various conformational mAbs that recognized the E2s domain. These mAbs were distributed into 6 independent groups, suggesting the presence of at least 6 epitopes. Twelve representative mAbs covering the six groups were selected as a tool box to further map functional antigenic sites on the E2s domain. By combining functional and location information of the 12 representative mAbs, this study provided a complete picture of potential neutralizing epitope regions and immune-dominant determinants on E2s domain. One epitope region is located on top of the E2s domain close to the monomer interface; the other is located on the monomer side of the E2s dimer around the groove zone. Besides, two non-neutralizing epitopes were also identified on E2s domain that did not stimulate neutralizing antibodies. Our results help further the understanding of protective mechanisms induced by the HEV vaccine. Furthermore, the tool box with 12 representative mAbs will be useful for studying the HEV infection process. © 2015 by The American Society for Biochemistry and Molecular Biology, Inc. Source