Objectives
Patients receiving hemodialysis (HD) are at increased risk of acquiring hepatitis B virus (HBV) and hepatitis C virus (HCV) due to repeated blood exposure, vascular access procedures, and blood transfusions. The study aimed to determine the seroconversion rates of HBV and HCV among patients undergoing dialysis and to identify associated risk factors.
Methods
A total of 220 adult patients receiving dialysis who were seronegative for hepatitis B surface antigen (HBsAg) and anti-HCV antibodies at baseline were enrolled. Serologic testing was repeated at 6 months.
Results
Sixteen patients (7.3%) seroconverted to HBsAg positivity, and 23 (10.5%) seroconverted to anti-HCV positivity. HBV seroconversion was significantly associated with multiple dialysis center visits. HCV seroconversion was significantly associated with dialyzer reuse, multiple dialysis center visits, and dialysis duration ≥2 years. Elevated liver enzyme levels were strongly correlated with seroconversion for both viruses.
Conclusion
HBV and HCV seroconversion remain concerns in HD units. Standardized infection control practices, minimization of patient transfers, and strict adherence to national guidelines are essential to reducing risk.

Objectives
Hepatitis B virus (HBV) is a member of the hepadnavirus family. The HBV genome contains four genes designated as S, C, P, and X. The HBV X (HBx) gene encodes for a 16.5-kDa regulatory protein that enhances HBV replication and exerts multifunctional activities. The aim of this study is to describe the rapid and easy purification of HBx using ELP (elastin-like polypeptide) fusion protein.
Methods
The ELP–HBx fusion protein was overexpressed in <i>Escherichia coli</i>. Environmental sensitivity was demonstrated via turbidity and dynamic light scattering as a function of temperature. HBx was purified as an ELP fusion protein. ELPs are biopolymers of the pentapeptide repeat Val-Pro-Gly-Xaa-Gly that undergo an inverse temperature phase transition. ELP follows in temperature and salt consistency, precipitation, and solution repetition (inverse transition cycling) with polypeptide, where it purifies the protein in a simple manner.
Results
Fusion proteins underwent supramolecular aggregation at 40 ℃ in 1 M NaCl and slowly resolubilized at subphysiologic temperatures. ELP domain proteolysis liberated a peptide of comparable size and immunoreactivity to the commercial HBx.
Conclusion
This study suggests that HBx can be purified rapidly and easily using inverse transition cycling, and that this method can be applied in determination of HBx 3D structures and HBx stability study.