# |
PMID |
Sentence |
1 |
6228474
|
No change in anti-HBs titer was seen and HBs, HBc, HBe Ag and/or AB could neither be detected in serum by RIA nor in liver by immunofluorescence during the 6 month follow up period.
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2 |
6694050
|
A mother and her daughter's caretaker were found to have asymptomatic acute HBV infection, and the mother developed antibodies to HBs, HBc, and HBe.
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3 |
8957676
|
In a murine transgenic model, HBc/eAg-specific Th1 cells were more readily anergized, whereas Th2 cells more easily escaped tolerization.
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4 |
9094605
|
Intramuscular injections with 10(8) CFU of the LHBc-NEO(6A3) retrovirus vector into rhesus monkeys induced HBc/eAg-specific antibody production and CD8+ CTLs.
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5 |
9094605
|
The CTL response from one of the two responder rhesus monkeys was directed against a 9-residue peptide, GELMTLATW, at positions 63 to 71 of the HBc/eAg sequence.
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6 |
9094605
|
Intramuscular injections with 10(8) CFU of the LHBc-NEO(6A3) retrovirus vector into rhesus monkeys induced HBc/eAg-specific antibody production and CD8+ CTLs.
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7 |
9094605
|
The CTL response from one of the two responder rhesus monkeys was directed against a 9-residue peptide, GELMTLATW, at positions 63 to 71 of the HBc/eAg sequence.
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8 |
9188598
|
Second, priming of H-2b mice with an HBc/eAg-derived T-helper (Th) peptide in adjuvant prior to retroviral vector immunization greatly enhanced the HBc/eAg-specific humoral responses to all three vectors, suggesting that insufficient HBc/eAg-specific CD4+ Th-cell priming limits the humoral responses.
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9 |
9188598
|
In conclusion, direct injection of retroviral vectors seems to be effective in priming HBc/eAg-specific CD8+ but comparatively inefficient in priming CD4+ Th cells and subsequently specific antibodies.
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10 |
9188598
|
However, the limited HBc/eAg-specific CD4+ cell priming can effectively be circumvented by prior administration of a recombinant or synthetic form of HBc/eAg in adjuvant.
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11 |
9188598
|
Second, priming of H-2b mice with an HBc/eAg-derived T-helper (Th) peptide in adjuvant prior to retroviral vector immunization greatly enhanced the HBc/eAg-specific humoral responses to all three vectors, suggesting that insufficient HBc/eAg-specific CD4+ Th-cell priming limits the humoral responses.
|
12 |
9188598
|
In conclusion, direct injection of retroviral vectors seems to be effective in priming HBc/eAg-specific CD8+ but comparatively inefficient in priming CD4+ Th cells and subsequently specific antibodies.
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13 |
9188598
|
However, the limited HBc/eAg-specific CD4+ cell priming can effectively be circumvented by prior administration of a recombinant or synthetic form of HBc/eAg in adjuvant.
|
14 |
9188598
|
Second, priming of H-2b mice with an HBc/eAg-derived T-helper (Th) peptide in adjuvant prior to retroviral vector immunization greatly enhanced the HBc/eAg-specific humoral responses to all three vectors, suggesting that insufficient HBc/eAg-specific CD4+ Th-cell priming limits the humoral responses.
|
15 |
9188598
|
In conclusion, direct injection of retroviral vectors seems to be effective in priming HBc/eAg-specific CD8+ but comparatively inefficient in priming CD4+ Th cells and subsequently specific antibodies.
|
16 |
9188598
|
However, the limited HBc/eAg-specific CD4+ cell priming can effectively be circumvented by prior administration of a recombinant or synthetic form of HBc/eAg in adjuvant.
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17 |
11509871
|
The interest in the HBc VLPs was reinforced by the resolution of their fine structure by electron cryomicroscopy and X-ray crystallography, which revealed an unusual alpha-helical organization of dimeric units of HBc shells, alternative packing into icosahedrons with T = 3 and T = 4 symmetry, and the existence of long protruding spikes.
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18 |
12566707
|
We selectively expressed antigen fragments encoding the linear e2 epitope (C(79-149)) of hepatitis B virus (pre)core antigen (HBc/eAg) and the conformational 'a' epitope (S(80-180)) of hepatitis B surface antigen (HBsAg) in a novel system.
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19 |
12566707
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The linear e2 epitope of HBc/eAg was efficiently expressed as an intracellular, hsp73-binding fusion protein, and efficiently primed an HBc/eAg-specific antibody response when delivered in this form.
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20 |
12566707
|
We selectively expressed antigen fragments encoding the linear e2 epitope (C(79-149)) of hepatitis B virus (pre)core antigen (HBc/eAg) and the conformational 'a' epitope (S(80-180)) of hepatitis B surface antigen (HBsAg) in a novel system.
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21 |
12566707
|
The linear e2 epitope of HBc/eAg was efficiently expressed as an intracellular, hsp73-binding fusion protein, and efficiently primed an HBc/eAg-specific antibody response when delivered in this form.
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22 |
12602354
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Previously, we described a new system to generate HBc mosaic particles based on a read-through mechanism in an Escherichia coli suppressor strain [J Gen Virol 1997;78:2049-2053].
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23 |
16697088
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Intramuscular immunization with a DNA vaccine encoding a 26-amino acid CETP epitope displayed by HBc protein and containing CpG DNA inhibits atherosclerosis in a rabbit model of atherosclerosis.
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24 |
16697088
|
Rabbits were intramuscularly immunized with the plasmid pCR-X8-HBc-CETP encoding a B-cell epitope of cholesteryl ester transfer protein (CETP) C-terminal fragment (CETPC) displayed by Hepatitis B virus core (HBc) particle.
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25 |
16697088
|
Intramuscular immunization with a DNA vaccine encoding a 26-amino acid CETP epitope displayed by HBc protein and containing CpG DNA inhibits atherosclerosis in a rabbit model of atherosclerosis.
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26 |
16697088
|
Rabbits were intramuscularly immunized with the plasmid pCR-X8-HBc-CETP encoding a B-cell epitope of cholesteryl ester transfer protein (CETP) C-terminal fragment (CETPC) displayed by Hepatitis B virus core (HBc) particle.
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27 |
17707782
|
The major aim of the project was to develop the virus-like particles (VLPs) displaying single or multi-epitope of hepatocellular carcinomas (HCC) in Escherichia coli and to evaluate the effect on inducing Ag-specific CD8(+) T cell response and antitumor efficacy as candidate vaccines.
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28 |
17707782
|
Four HCC epitopes MAGE-1(278-286aa), MAGE-3(271-279aa), AFP1 (158-166aa) or AFP2 (542-550aa) were fused to the 3' terminus of the truncated HBV core gene, respectively, or conjunctively.
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29 |
17707782
|
E. coli-derived truncated HBc(1-144) chimeric protein self-assembled into VLPs that both morphologically and physically are similar to the wild-type ones and they still remained activity after purification and refolding from 6M urea solution.
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30 |
18367580
|
Recent findings are suggesting the potential of the HBc VLPs as an oral immunogen.
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31 |
18367580
|
Here, we focus on the induction of serum humoral responses by oral administration of HBc VLPs in preparations substantially free of lipopolysaccharide and immunomodulating encapsidated RNA.
|
32 |
18367580
|
Serum antibody levels and isotypes were determined following oral administration of the HBc VLPs with the perspective of using the HBc VLP as an immunostimulatory and carrier molecule for epitopes of blood-borne diseases in oral immunization vaccination strategies.
|
33 |
18367580
|
Following oral administration of the HBc VLP preparations to mice, a strong serum humoral response was induced with mainly immunoglobulin G2a (IgG2a) antibodies, pointing toward a Th1 response which is essential in the control of intracellular pathogens.
|
34 |
18367580
|
Intraperitoneal immunization with the HBc VLP induced a stronger, mixed Th1/Th2 response.
|
35 |
18367580
|
These data suggest that the HBc VLP can be an interesting carrier molecule in oral vaccine development.
|
36 |
18367580
|
Recent findings are suggesting the potential of the HBc VLPs as an oral immunogen.
|
37 |
18367580
|
Here, we focus on the induction of serum humoral responses by oral administration of HBc VLPs in preparations substantially free of lipopolysaccharide and immunomodulating encapsidated RNA.
|
38 |
18367580
|
Serum antibody levels and isotypes were determined following oral administration of the HBc VLPs with the perspective of using the HBc VLP as an immunostimulatory and carrier molecule for epitopes of blood-borne diseases in oral immunization vaccination strategies.
|
39 |
18367580
|
Following oral administration of the HBc VLP preparations to mice, a strong serum humoral response was induced with mainly immunoglobulin G2a (IgG2a) antibodies, pointing toward a Th1 response which is essential in the control of intracellular pathogens.
|
40 |
18367580
|
Intraperitoneal immunization with the HBc VLP induced a stronger, mixed Th1/Th2 response.
|
41 |
18367580
|
These data suggest that the HBc VLP can be an interesting carrier molecule in oral vaccine development.
|
42 |
18367580
|
Recent findings are suggesting the potential of the HBc VLPs as an oral immunogen.
|
43 |
18367580
|
Here, we focus on the induction of serum humoral responses by oral administration of HBc VLPs in preparations substantially free of lipopolysaccharide and immunomodulating encapsidated RNA.
|
44 |
18367580
|
Serum antibody levels and isotypes were determined following oral administration of the HBc VLPs with the perspective of using the HBc VLP as an immunostimulatory and carrier molecule for epitopes of blood-borne diseases in oral immunization vaccination strategies.
|
45 |
18367580
|
Following oral administration of the HBc VLP preparations to mice, a strong serum humoral response was induced with mainly immunoglobulin G2a (IgG2a) antibodies, pointing toward a Th1 response which is essential in the control of intracellular pathogens.
|
46 |
18367580
|
Intraperitoneal immunization with the HBc VLP induced a stronger, mixed Th1/Th2 response.
|
47 |
18367580
|
These data suggest that the HBc VLP can be an interesting carrier molecule in oral vaccine development.
|
48 |
18367580
|
Recent findings are suggesting the potential of the HBc VLPs as an oral immunogen.
|
49 |
18367580
|
Here, we focus on the induction of serum humoral responses by oral administration of HBc VLPs in preparations substantially free of lipopolysaccharide and immunomodulating encapsidated RNA.
|
50 |
18367580
|
Serum antibody levels and isotypes were determined following oral administration of the HBc VLPs with the perspective of using the HBc VLP as an immunostimulatory and carrier molecule for epitopes of blood-borne diseases in oral immunization vaccination strategies.
|
51 |
18367580
|
Following oral administration of the HBc VLP preparations to mice, a strong serum humoral response was induced with mainly immunoglobulin G2a (IgG2a) antibodies, pointing toward a Th1 response which is essential in the control of intracellular pathogens.
|
52 |
18367580
|
Intraperitoneal immunization with the HBc VLP induced a stronger, mixed Th1/Th2 response.
|
53 |
18367580
|
These data suggest that the HBc VLP can be an interesting carrier molecule in oral vaccine development.
|
54 |
18367580
|
Recent findings are suggesting the potential of the HBc VLPs as an oral immunogen.
|
55 |
18367580
|
Here, we focus on the induction of serum humoral responses by oral administration of HBc VLPs in preparations substantially free of lipopolysaccharide and immunomodulating encapsidated RNA.
|
56 |
18367580
|
Serum antibody levels and isotypes were determined following oral administration of the HBc VLPs with the perspective of using the HBc VLP as an immunostimulatory and carrier molecule for epitopes of blood-borne diseases in oral immunization vaccination strategies.
|
57 |
18367580
|
Following oral administration of the HBc VLP preparations to mice, a strong serum humoral response was induced with mainly immunoglobulin G2a (IgG2a) antibodies, pointing toward a Th1 response which is essential in the control of intracellular pathogens.
|
58 |
18367580
|
Intraperitoneal immunization with the HBc VLP induced a stronger, mixed Th1/Th2 response.
|
59 |
18367580
|
These data suggest that the HBc VLP can be an interesting carrier molecule in oral vaccine development.
|
60 |
18367580
|
Recent findings are suggesting the potential of the HBc VLPs as an oral immunogen.
|
61 |
18367580
|
Here, we focus on the induction of serum humoral responses by oral administration of HBc VLPs in preparations substantially free of lipopolysaccharide and immunomodulating encapsidated RNA.
|
62 |
18367580
|
Serum antibody levels and isotypes were determined following oral administration of the HBc VLPs with the perspective of using the HBc VLP as an immunostimulatory and carrier molecule for epitopes of blood-borne diseases in oral immunization vaccination strategies.
|
63 |
18367580
|
Following oral administration of the HBc VLP preparations to mice, a strong serum humoral response was induced with mainly immunoglobulin G2a (IgG2a) antibodies, pointing toward a Th1 response which is essential in the control of intracellular pathogens.
|
64 |
18367580
|
Intraperitoneal immunization with the HBc VLP induced a stronger, mixed Th1/Th2 response.
|
65 |
18367580
|
These data suggest that the HBc VLP can be an interesting carrier molecule in oral vaccine development.
|
66 |
18927587
|
Hepatitis B virus core protein inhibits TRAIL-induced apoptosis of hepatocytes by blocking DR5 expression.
|
67 |
18927587
|
TRAIL, the TNF-related apoptosis-inducing ligand, has recently been implicated in hepatocyte death during HBV infection.
|
68 |
18927587
|
We report here that the HBV core protein (HBc) is a potent inhibitor of TRAIL-induced apoptosis.
|
69 |
18927587
|
Overexpressing HBc significantly decreased TRAIL-induced apoptosis of human hepatoma cells, whereas knocking-down HBc expression in hepatoma cells transfected with HBV genome enhanced it.
|
70 |
18927587
|
The resistance of HBc-expressing cells to TRAIL-induced apoptosis was associated with a significant reduction in death receptor 5 (DR5) expression.
|
71 |
18927587
|
Upon transfection, HBc significantly repressed the promoter activity of the human DR5 gene.
|
72 |
18927587
|
Importantly, HBc gene transfer inhibited hepatocyte death in a mouse model of HBV-induced hepatitis; and in patients with chronic hepatitis, DR5 expression in the liver was significantly reduced.
|
73 |
18927587
|
These results indicate that HBc may prevent hepatocytes from TRAIL-induced apoptosis by blocking DR5 expression, which in turn contributes to the development of chronic hepatitis and HCC.
|
74 |
18927587
|
Hepatitis B virus core protein inhibits TRAIL-induced apoptosis of hepatocytes by blocking DR5 expression.
|
75 |
18927587
|
TRAIL, the TNF-related apoptosis-inducing ligand, has recently been implicated in hepatocyte death during HBV infection.
|
76 |
18927587
|
We report here that the HBV core protein (HBc) is a potent inhibitor of TRAIL-induced apoptosis.
|
77 |
18927587
|
Overexpressing HBc significantly decreased TRAIL-induced apoptosis of human hepatoma cells, whereas knocking-down HBc expression in hepatoma cells transfected with HBV genome enhanced it.
|
78 |
18927587
|
The resistance of HBc-expressing cells to TRAIL-induced apoptosis was associated with a significant reduction in death receptor 5 (DR5) expression.
|
79 |
18927587
|
Upon transfection, HBc significantly repressed the promoter activity of the human DR5 gene.
|
80 |
18927587
|
Importantly, HBc gene transfer inhibited hepatocyte death in a mouse model of HBV-induced hepatitis; and in patients with chronic hepatitis, DR5 expression in the liver was significantly reduced.
|
81 |
18927587
|
These results indicate that HBc may prevent hepatocytes from TRAIL-induced apoptosis by blocking DR5 expression, which in turn contributes to the development of chronic hepatitis and HCC.
|
82 |
18927587
|
Hepatitis B virus core protein inhibits TRAIL-induced apoptosis of hepatocytes by blocking DR5 expression.
|
83 |
18927587
|
TRAIL, the TNF-related apoptosis-inducing ligand, has recently been implicated in hepatocyte death during HBV infection.
|
84 |
18927587
|
We report here that the HBV core protein (HBc) is a potent inhibitor of TRAIL-induced apoptosis.
|
85 |
18927587
|
Overexpressing HBc significantly decreased TRAIL-induced apoptosis of human hepatoma cells, whereas knocking-down HBc expression in hepatoma cells transfected with HBV genome enhanced it.
|
86 |
18927587
|
The resistance of HBc-expressing cells to TRAIL-induced apoptosis was associated with a significant reduction in death receptor 5 (DR5) expression.
|
87 |
18927587
|
Upon transfection, HBc significantly repressed the promoter activity of the human DR5 gene.
|
88 |
18927587
|
Importantly, HBc gene transfer inhibited hepatocyte death in a mouse model of HBV-induced hepatitis; and in patients with chronic hepatitis, DR5 expression in the liver was significantly reduced.
|
89 |
18927587
|
These results indicate that HBc may prevent hepatocytes from TRAIL-induced apoptosis by blocking DR5 expression, which in turn contributes to the development of chronic hepatitis and HCC.
|
90 |
18927587
|
Hepatitis B virus core protein inhibits TRAIL-induced apoptosis of hepatocytes by blocking DR5 expression.
|
91 |
18927587
|
TRAIL, the TNF-related apoptosis-inducing ligand, has recently been implicated in hepatocyte death during HBV infection.
|
92 |
18927587
|
We report here that the HBV core protein (HBc) is a potent inhibitor of TRAIL-induced apoptosis.
|
93 |
18927587
|
Overexpressing HBc significantly decreased TRAIL-induced apoptosis of human hepatoma cells, whereas knocking-down HBc expression in hepatoma cells transfected with HBV genome enhanced it.
|
94 |
18927587
|
The resistance of HBc-expressing cells to TRAIL-induced apoptosis was associated with a significant reduction in death receptor 5 (DR5) expression.
|
95 |
18927587
|
Upon transfection, HBc significantly repressed the promoter activity of the human DR5 gene.
|
96 |
18927587
|
Importantly, HBc gene transfer inhibited hepatocyte death in a mouse model of HBV-induced hepatitis; and in patients with chronic hepatitis, DR5 expression in the liver was significantly reduced.
|
97 |
18927587
|
These results indicate that HBc may prevent hepatocytes from TRAIL-induced apoptosis by blocking DR5 expression, which in turn contributes to the development of chronic hepatitis and HCC.
|
98 |
18927587
|
Hepatitis B virus core protein inhibits TRAIL-induced apoptosis of hepatocytes by blocking DR5 expression.
|
99 |
18927587
|
TRAIL, the TNF-related apoptosis-inducing ligand, has recently been implicated in hepatocyte death during HBV infection.
|
100 |
18927587
|
We report here that the HBV core protein (HBc) is a potent inhibitor of TRAIL-induced apoptosis.
|
101 |
18927587
|
Overexpressing HBc significantly decreased TRAIL-induced apoptosis of human hepatoma cells, whereas knocking-down HBc expression in hepatoma cells transfected with HBV genome enhanced it.
|
102 |
18927587
|
The resistance of HBc-expressing cells to TRAIL-induced apoptosis was associated with a significant reduction in death receptor 5 (DR5) expression.
|
103 |
18927587
|
Upon transfection, HBc significantly repressed the promoter activity of the human DR5 gene.
|
104 |
18927587
|
Importantly, HBc gene transfer inhibited hepatocyte death in a mouse model of HBV-induced hepatitis; and in patients with chronic hepatitis, DR5 expression in the liver was significantly reduced.
|
105 |
18927587
|
These results indicate that HBc may prevent hepatocytes from TRAIL-induced apoptosis by blocking DR5 expression, which in turn contributes to the development of chronic hepatitis and HCC.
|
106 |
19004949
|
The aim of this study was to evaluate the ability of HBcAg- and HBeAg-specific genetic immunogens to induce HBc/HBeAg-specific CD4(+)/CD8(+) T-cell immune responses and the potential to induce liver injury in HBV-transgenic (Tg) mice.
|
107 |
19004949
|
Both CD4(+) and CD8(+) T cells were important for priming/effector functions of HBc/HBeAg-specific cytotoxic T-lymphocyte (CTL) responses.
|
108 |
26113394
|
Although HBc VLPs and their numerous derivatives are produced in highly efficient bacterial and yeast expression systems, the existing purification and packaging protocols are not sufficiently optimised and standardised.
|
109 |
26113394
|
Here, a simple alkaline treatment method was employed for the complete removal of internal RNA from bacteria- and yeast-produced HBc VLPs and for the conversion of these VLPs into empty particles, without any damage to the VLP structure.
|
110 |
26113394
|
The empty HBc VLPs were able to effectively package the added DNA and RNA sequences.
|
111 |
26113394
|
Although HBc VLPs and their numerous derivatives are produced in highly efficient bacterial and yeast expression systems, the existing purification and packaging protocols are not sufficiently optimised and standardised.
|
112 |
26113394
|
Here, a simple alkaline treatment method was employed for the complete removal of internal RNA from bacteria- and yeast-produced HBc VLPs and for the conversion of these VLPs into empty particles, without any damage to the VLP structure.
|
113 |
26113394
|
The empty HBc VLPs were able to effectively package the added DNA and RNA sequences.
|
114 |
26113394
|
Although HBc VLPs and their numerous derivatives are produced in highly efficient bacterial and yeast expression systems, the existing purification and packaging protocols are not sufficiently optimised and standardised.
|
115 |
26113394
|
Here, a simple alkaline treatment method was employed for the complete removal of internal RNA from bacteria- and yeast-produced HBc VLPs and for the conversion of these VLPs into empty particles, without any damage to the VLP structure.
|
116 |
26113394
|
The empty HBc VLPs were able to effectively package the added DNA and RNA sequences.
|
117 |
26446016
|
In contrast to natural HBc VLPs and recombinant HBc VLP variants carrying native CT domain, the HBcG VLPs demonstrated a lowered capability to pack bacterial RNA during expression in Escherichia coli cells.
|
118 |
26446016
|
The C-terminal addition of a model foreign epitope from the HBV preS1 sequence to the HBcG vectors resulted in the exposure of the inserted epitope on the VLP surface, whereas the same preS1 sequences added to the native CT of the natural HBc protein remained buried within the HBc VLPs.
|
119 |
26446016
|
In contrast to natural HBc VLPs and recombinant HBc VLP variants carrying native CT domain, the HBcG VLPs demonstrated a lowered capability to pack bacterial RNA during expression in Escherichia coli cells.
|
120 |
26446016
|
The C-terminal addition of a model foreign epitope from the HBV preS1 sequence to the HBcG vectors resulted in the exposure of the inserted epitope on the VLP surface, whereas the same preS1 sequences added to the native CT of the natural HBc protein remained buried within the HBc VLPs.
|