Zhikai Xu

Fourth Military Medical University, Xi’an, Liaoning, China

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Publications (6)17.88 Total impact

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    ABSTRACT: The aryl hydrocarbon receptor (AhR) is a ligand-activated transcription factor implicated in multiple cellular processes and its expression has been shown to play a critical role in tumorigenesis. However, the role of AhR in tumorigenesis of hepatocellular carcinoma remains unclear. In the current study, we investigated the role of AhR in hepatocellular carcinoma tumorigenesis and progression by (a) measuring the expression levels of AhR in liver lesions and (b) assessing the correlation between AhR expression and clinicopathologic parameters. The tissue microarray used in this study contained hepatocellular carcinoma tissues (n = 94), cancer adjacent normal hepatic tissues (n = 5) and normal hepatic tissues (n = 5), which were immunohistochemically assessed for AhR expression. Significantly stronger AhR staining was observed for hepatocellular carcinoma tissues than for cancer adjacent normal hepatic tissues (P = 0.003) and normal hepatic tissues (P = 0.004). In addition, AhR expression was associated with T stage (P = 0.03). The results from this study suggest that an increase in AhR expression is associated with hepatocellular carcinoma progression and may have a potential role in the treatment of hepatocellular carcinoma.
    Journal of molecular histology 04/2013; · 1.75 Impact Factor
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    ABSTRACT: CD8+ T cells play an important role in early HIV infection. However, HIV has the capacity to avoid specific CTL responses due to a high rate of mutation under selection pressure. Although the HIV proteins, gag and pol, are relatively conserved, these sequences generate low-affinity MHC-associated epitopes that are poorly immunogenic. Here, we applied an approach that enhanced the immunogenicity of low-affinity HLA-A2.1-binding peptides. The first position with tyrosine (P1Y) substitution enhanced the affinity of HLA-A2.1-associated peptides without altering their antigenic specificity. More importantly, P1Y variants efficiently stimulated in vivo native peptide-specific CTL that also recognized the corresponding naturally processed epitope. The potential to generate CTL against any low-affinity HLA-A2.1-associated peptide provides us with the necessary technique for identification of virus cryptic epitopes for development of peptide-based immunotherapy. Therefore, identification and modification of the cryptic epitopes of gal and pol provides promising candidates for HIV immunotherapy dependent upon efficient presentation by virus cells. Furthermore, this may be a breakthrough that overcomes the obstacle of immune escape caused by high rates of mutation. In this study, bioinformatics analysis was used to predict six low-affinity cryptic HIV gag and pol epitopes presented by HLA-A*0201. A HIV compound multi-CTL epitope gene was constructed comprising the gene encoding the modified cryptic epitope and the HIV p24 antigen, which induced a strong CD8+ T cell immune response regardless of the mutation. This approach represents a novel strategy for the development of safe and effective HIV prophylactic and therapeutic vaccines.
    Molecular Biology Reports 03/2013; · 2.51 Impact Factor
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    ABSTRACT: Hantaan virus (HTNV) of the Bunyaviridae family is a major agent causing hemorrhagic fever with renal syndrome (HFRS), a high-mortality-rate disease threatening approximately 150,000 people around the world yearly. The 3D8 monoclonal antibody displays a neutralizing activity to HTNV infection. In this study, the B-cell epitopes of HTNV glycoproteins (GPs) were finely mapped by peptide scanning. A new B-cell epitope (882)GFLCPEFPGSFRKKC(896) of HTNV, which locates on Gc, has been screened out from a set of 15-mer synthesized peptides covering the full length of HTNV-GPs. It has been shown by the alanine-scanning technique that (885)C, (893)R, (894)K, (895)K, and (896)C are the key amino acids of the binding sites of the GPs. The implications of identifying a novel B-cell epitope for hantavirus immunology and vaccinology are discussed.
    Journal of General Virology 08/2012; · 3.13 Impact Factor
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    ABSTRACT: To investigate the role of viral load in the pathogenesis of hemorrhagic fever with renal syndrome, the Hantaan virus RNA load in plasma from 101 patients was quantified, and the relationships between viral load and disease course, severity, and level of specific humoral immunity were analyzed. The viral load, detectable in 79 patients, ranged from 3.43 to 7.33 log(10) copies/mL of plasma. In the early stage of disease, patients in severe/critical group were found to have higher viral loads than those in the mild/moderate group (5.90 vs 5.03 log(10) copies/mL; P = .001), suggesting an association between Hantaan virus load and disease severity.
    The Journal of Infectious Diseases 08/2012; · 5.85 Impact Factor
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    ABSTRACT: Botulinum neurotoxins (BoNTs) are classified as category A biological threat agents by the Centers for Disease Control and Prevention (CDC) in the United States for its hazardous and potential bioterrorist threat to the public. About 1% naturally occurring botulisms are caused by Botulinum neurotoxin serotype F (BoNT/F). Most of the immunoassays for detecting BoNTs focus on the serotypes A and B, but few methods have been established for the detection of BoNT/F. Recently, the recombinant Hc subunit of botulinum neurotoxin type F (rFHc) was expressed as an effective vaccine against BoNT/F, indicating that this rFHc could be an effective immunogen to raise monoclonal antibodies (MAbs) for the detection and neutralization of BoNT/F. Here we present a novel sandwich enzyme-linked immunosorbent assay (ELISA) based on two MAbs against rFHc, which were FMMU-BTF-8 and FMMU-BTF-29 as capture antibody and detection antibody, respectively. The limit of detection (LOD) of this ELISA reached 12.09 pg/mL, much less than that of the other reported immunoassays. A simple, sensitive ELISA for detecting and quantifying BoNT/F was established, which can be used as a valuable method to detect and quantify BoNT/F.
    Hybridoma (2005) 08/2012; 31(4):233-9. · 0.33 Impact Factor
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    ABSTRACT: Botulinum neurotoxins (BoNTs) are the most poisonous substances ever known. The early detection of these toxins could bear more time for appropriate medical intervention. The standard method for detecting BoNTs is the mouse bioassay, which is time consuming (up to 4 days) and requires a large number of laboratory animals. The immunologic detection methods could detect the toxins within a day, but most of these methods are less sensitive compared with the mouse bioassay due to the lack of high-affinity antibodies. Recently, the recombinant H(C) subunit of botulinum neurotoxin type A (rAH(C)) was expressed as an effective vaccine against botulism, indicating that the rAH(C) could be an effective immunogen that raises the monoclonal antibody (mAb) for detecting BoNT/A. After immunized BALB/c mice with rAH(C), 56 mAbs were generated. Two of these mAbs were selected to establish a highly sensitive sandwich chemiluminescence enzyme immunoassay (CLEIA), in which FMMU-BTA-49 and FMMU-BTA-22 were used as capture antibody and detection antibody, respectively. The calculated limit of detection (LOD) based on molecular weight of rAH(C) and BoNT/A reached 0.45 pg mL(-1). This CLEIA can be used in the detection of BoNT/A in matrices such as milk and beef extract. This method has 20-40 fold lower LOD than that of the mouse bioassay and takes only 3 h to complete the detection, indicating that it can be used as a valuable method to detect and quantify BoNT/A.
    Analytica chimica acta 07/2012; 735:23-30. · 4.31 Impact Factor