ライフサイエンスコーパス: HBcAg

1 HBcAg and HBsAg IHC staining persisted despite viral sup

2 HBcAg staining was detected in 60% and HBsAg in 79%.

3 HBcAg-primed Th cells efficiently produced interleukin-2

4 HBcAg-zDIII VLPs are shown to be highly immunogenic, as

5 he primary APCs for the hepatitis B core Ag (HBcAg) were B cells and not dendritic cells (DC).

6 the viral nucleocapsid hepatitis B core Ag (HBcAg), and its function is unknown.

7 ion, a novel retrovirus vector expressing an HBcAg-neomycin phosphotransferase II (HBc-Neo) fusion pr

8 HBcAg-specific Th cells into dual HBeAg- and HBcAg-expressing Tg recipient mice.

9 eferentially deplete inflammatory HBeAg- and HBcAg-specific Th1 cells that are necessary for viral cl

10 nd their associations with hepatic HBsAg and HBcAg staining in patients coinfected with HBV and HIV.

11 ochemistry (IHC) was performed for HBsAg and HBcAg.

12 Knowledge of the binding site of our anti-HBcAg antibody bears on the molecular basis of the disti

13 undetectable intracellular HBV core antigen (HBcAg) and absence of significant levels of secreted cor

14 ent forms of hepatitis B virus core antigen (HBcAg) and e antigen (HBeAg) were analyzed.

15 s, respectively referred to as core antigen (HBcAg) and e-antigen (HBeAg), share a sequence of 149 re

16 mino acid 97 (I97L) of the HBV core antigen (HBcAg) causes it to release immature genomes.

17 human hepatitis B virus (HBV) core antigen (HBcAg) has been found in chronic carriers worldwide.

18 ction of HBV DNA, RNA, and HBV core antigen (HBcAg) in hepatocytes.

19 Additionally, HBV core antigen (HBcAg) in vitro stimulation using peripheral blood monon

20 B virus (HBV) nucleocapsid or core antigen (HBcAg) is extremely immunogenic during infection and aft

21 ing different forms of the HBV core antigen (HBcAg) or e antigen (eAg) were found to induce antigen-s

22 histochemical detection of HBV core antigen (HBcAg) revealed >99% reduction in stained hepatocytes up

23 rrier based on the hepatitis B core antigen (HBcAg) that displays the ZIKV E protein domain III (zDII

24 Core antigen (HBcAg) was much more resistant to treatment and the maxi

25 eucine at amino acid 97 of HBV core antigen (HBcAg), lost the high stringency of selectivity in genom

26 n at the C terminus of the HBV core antigen (HBcAg), was speculated to secrete immature genomes.

27 nd non-crossreactive antigens: core antigen (HBcAg), which appears early in infection as assembled ca

28 antibodies is the hepatitis B core antigen (HBcAg); that these anti-bodies display a restricted vari

29 llular nucleocapsid (hepatitis core antigen [HBcAg]) and the secreted nonparticulate form (hepatitis

30 ith the viral capsid protein "core-antigen" (HBcAg), but has an additional 10-residue, hydrophobic, c

31 rs of a 183-residue protein, 'core antigen' (HBcAg).

32 (pg) RNA within the capsid of core antigens (HBcAgs) that each contains a flexible C-terminal tail ri

33 variants, we have characterized mutations at HBcAg codons 5, 38, and 60 via site-directed mutagenesis

34 Because HBcAg and the HBeAg are cross-reactive in terms of Th ce

35 , not to processing or presentation, because HBcAg/anti-HBc immune complexes can be efficiently prese

36 -NEO[6A3]-immunized H-2k mice abrogated both HBcAg-specific antibodies and in vitro-detectable cytoto

37 es expressing wild-type HBV (containing both HBcAg and HBeAg) are more susceptible to CTL-mediated cl

38 y direct HBcAg-biotin-binding studies and by HBcAg-specific T cell activation in vitro in cultures of

39 Cytokine production by HBcAg- and HBeAg-primed Th cells was consistent with the

40 Second, in vitro cytokine production by HBcAg- and HBeAg-primed Th cells was measured.

41 Humoral and CD4+ cellular HBcAg and/or HBeAg (HBc/eAg)-specific immune responses f

42 ciently removed from the membrane containing HBcAg using DNase I digestion and gradient wash with ure

43 The membrane strip containing HBcAg and a second membrane strip containing human serum

44 genic potential of the HBV precore and core (HBcAg) proteins, HBc/HBeAg-transgenic (Tg) mice crossed

45 ral nucleoprotein, the particulate HBV core (HBcAg) and the nonparticulate HBeAg, may preferentially

46 GC1alpha is a subtle increase in cytoplasmic HBcAg/p21 polypeptide translation, which shifts the equi

47 s apparent that the synthesis of cytoplasmic HBcAg/p21 above a critical threshold level is required f

48 This was demonstrated by direct HBcAg-biotin-binding studies and by HBcAg-specific T cel

49 RNAi rapidly suppressed HBV-DNA, HBcAg, and HBsAg expression, impairing recognition by HB

50 This enables HBcAg-specific B cells from unprimed mice to take up, pr

51 and CD8(+) T cell priming with DNA encoding HBcAg does not require B cell APCs.

52 al and nonhelical loop regions of the entire HBcAg molecule is important for virion secretion.

53 he HBcAg is highly immunogenic, the existing HBcAg-based platform technology has a number of theoreti

54 lity of DC to function as APCs for exogenous HBcAg relates to lack of uptake of HBcAg, not to process

55 ed for HBsAg was 4.66 +/- 0.19 h(-1) and for HBcAg 0.10 +/- 0.01 h(-1).

56 sidated pgRNA from nuclease was observed for HBcAg 1-171.

57 ter nuclease treatment was observed only for HBcAg 164 and 167.

58 subset of HepaRG cells stained positive for HBcAg at comparable or even higher mge.

59 studies with immunohistochemical stains for HBcAg and HBsAg also being negative.

60 Furthermore, HBcAg elicited primarily IgG2a and IgG2b anti-HBc antibo

61 Furthermore, HBcAg-specific CD4(+) and CD8(+) T cell priming with DNA

62 This study revealed three phenotypes of HBe/HBcAg-specific T-cell tolerance: (i) profound T-cell tol

63 cells was also examined by transferring HBe/HBcAg-specific Th cells into dual HBeAg- and HBcAg-expre

64 and low A3B expression correlated with high HBcAg, potentially representing a reservoir for HBV surv

65 Higher HBV RNA was associated with higher HBcAg and HBsAg IHC grades (both p < 0.0001).

66 In HBcAg dimers, the subunits pair by forming a four-helix

67 cleocapsid spikes differentiated contacts in HBcAg for the two binding domains in L-HBsAg and implied

68 -Tg mice but elicited a weak CTL response in HBcAg-Tg mice.

69 y greater in HBeAg-Tg recipient mice than in HBcAg-Tg mice.

70 Individually, HBcAg-p67C (chimeric hepatitis B core Ag virus-like part

71 of recombinant retrovirus vectors to induce HBcAg- and eAg-specific CTL responses may prove benefici

72 For example, during many chronic infections, HBcAg is the only antigen capable of eliciting an immune

73 creted HBeAg (HBe[5A2]), or an intracellular HBcAg-neomycin phosphoryltransferase fusion protein (HBc

74 vectors induced expression of intracellular HBcAg (HBc[3A4]), secreted HBeAg (HBe[5A2]), or an intra

75 cantly more efficient than the intracellular HBcAg at eliciting T-cell tolerance.

76 lication markers, undetectable intracellular HBcAg, and by the lack of considerable levels of secrete

77 Full-length (HBcAg(183)), truncated (HBcAg(149)), and the nonparticul

78 istidine tagging at the C terminus of mutant HBcAg, which is presumably in the capsid interior.

79 ell activation in vitro in cultures of naive HBcAg-specific T cells and resting B cell subpopulations

80 capsids of HBcAg 154, 164, and 167, but not HBcAg 183, exhibited nuclease sensitivity; however, caps

81 Notably, HBcAg-zDIII VLPs-elicited antibodies did not enhance the

82 Surprisingly, the nuclear HBcAg of mutants I97E and I97W, produced from either a r

83 ledge, this is the first report of nucleolar HBcAg in culture.

84 of this study was to evaluate the ability of HBcAg- and HBeAg-specific genetic immunogens to induce H

85 an immune response, and nanogram amounts of HBcAg elicit antibody production in mice.

86 Binding of HBcAg particles by L-HBsAg displayed two widely differin

87 capsidated in Escherichia coli by capsids of HBcAg 154, 164, and 167, but not HBcAg 183, exhibited nu

88 by disulfide bonding of the last cysteine of HBcAg.

89 APC, explain the enhanced immunogenicity of HBcAg, and may have relevance for the induction and/or m

90 The immunogenicity of HBcAg, in contrast to that of HBeAg, did not require the

91 r apoptotic, suggesting that the presence of HBcAg in the nucleolus may perturb cytokinesis.

92 idate the structure-function relationship of HBcAg at amino acid 97, we systematically replaced the i

93 re constructed of dimers resembling those of HBcAg capsids.

94 mmunogen characteristics similar to those of HBcAg, comparative antigenicity and immunogenicity studi

95 exogenous HBcAg relates to lack of uptake of HBcAg, not to processing or presentation, because HBcAg/

96 unity problem that is inherent in the use of HBcAg for human vaccine development.

97 The effect of circulating HBeAg on HBcAg-specific Th1 cells was also examined by transferri

98 d clearance than hepatocytes expressing only HBcAg suggest that the HBeAg-negative variant may have a

99 hepatitis B virus core antigen polypeptide (HBcAg/p21) synthesis, it mediates a dramatic increase in

100 primed mice to take up, process, and present HBcAg to naive Th cells in vivo and to T cell hybridomas

101 no acid 97 of the HBV core (capsid) protein (HBcAg).

102 The hepatitis B virus core protein (HBcAg) is a uniquely immunogenic particulate antigen and

103 to MHBs, a VLV expressing HBV core protein (HBcAg) neither induced a CD8 T cell response in mice nor

104 The particulate hepatitis core protein (HBcAg) represents an efficient carrier platform with man

105 A crude Hepatitis B virus core protein (HBcAg) was separated using polyacrylamide gel electropho

106 the virus envelope and nucleocapsid protein (HBcAg).

107 urpose, mice were immunized with recombinant HBcAg and HBeAg in the presence and absence of adjuvants

108 stream indicators of cccDNA such as HBV RNA, HBcAg, and HBeAg were similarly reduced.

109 d B1b cells more efficiently present soluble HBcAg to naive CD4(+) T cells than splenic B2 cells.

110 n immunogenicity to or more immunogenic than HBcAg at the B-cell and T-cell levels; (ii) major histoc

111 itopes at a greater number of positions than HBcAg.

112 The results indicate that HBcAg preferentially, but not exclusively, elicits Th1-l

113 and IgM anti-HBc antibodies, indicating that HBcAg is the target of a germline human V(H) gene.

114 Although the HBcAg is highly immunogenic, the existing HBcAg-based pl

115 t T-cell tolerance between the HBeAg and the HBcAg and the clonal heterogeneity of HBc/HBeAg-specific

116 Both the HBcAg- and HBeAg-specific plasmids primed comparable imm

117 reveal a structure-function relation for the HBcAg, confirm that B cells can function as primary APC,

118 Our analysis of how the HBcAg is presented to the immune system revealed that th

119 The pleiotropic effects of the HBcAg codon 97 mutation were observed consistently in se

120 inal binding domain contacts the tips of the HBcAg spikes.

121 The HBeAg capsids are less regular than the HBcAg capsids; nevertheless, cryo-electron microscopy re

122 ented to the immune system revealed that the HBcAg binds to specific membrane Ig (mIg) antigen recept

123 re not significantly cross-reactive with the HBcAg at the antibody level (however, the nonparticulate

124 h oppositely charged C-terminal tails of the HBcAgs, and that the net charge of the capsid and C-term

125 synergistically to high-affinity binding to HBcAg, but disruption of either of these segments result

126 and enhance the adaptive immune response to HBcAg and have important implications for the use of hep

127 The T-cell proliferative response to HBcAg did not differ between the three groups.

128 ers have higher PBMCs IFN-gamma secretion to HBcAg stimulation (P= .0002).

129 the wild-type HBV and mutants with truncated HBcAg C-termini.

130 Full-length (HBcAg(183)), truncated (HBcAg(149)), and the nonparticulate HBeAg were screened

131 this colocalization occurred with wild-type HBcAg only to a limited extent.

132 Upon HBcAg(core) or HBsAg(env)-stimulation, 85% and 60% of HB

133 the residues necessary for association with HBcAg.

134 iculocyte lysates and their interaction with HBcAg was examined with an immunoprecipitation assay and

135 teins are only partially cross-reactive with HBcAg at the CD4+ T-cell level, depending on MHC haploty

136 Coimmunization of cattle (Bos taurus) with HBcAg-p67C and SV-p67C resulted in stimulation of both h

137 However, the ssRNA contained within HBcAg(183) does function as a TLR-7 ligand, as demonstra

138 ast, and mammalian ssRNA encapsidated within HBcAg(183) all function as TLR-7 ligands.