Hepatitis C virus core region: helper T cell epitopes recognized by BALB/c and C57BL/6 mice

Kakimi, Kazuhiro; Kuribayashi, Kagemasa; Iwashiro, Michihiro; Masuda, Tohru; Sakai, Masahiko; Wang, Ling; Kubo, Yasuo; Kobayashi, Hidekazu; Higo, Kyoko; Seki, Makoto; Honda, Yoshikazu; Yamada, Erika; Matsuura, Yoshiharu; Miyamura, Tatsuo; Okuma, Minoru; Ishimoto, Akinori

doi:10.1099/0022-1317-76-5-1205

Cited by 17 publications

(11 citation statements)

References 64 publications

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“…However, peptidic NS3-specific reactivities of a much lower magnitude can also be found in both hosts (Khudyakov eta]., 1995 ;Zhang et al, 1994). This is in contrast to the human and murine serological responses to the HCV core and NS4 proteins in which reactivities directed towards linear determinants are frequently observed (Kakimi et al, 1995;Khudyakov et al, 1995;Simmonds et at., 1993;S~illberg et al, 1992Zhang et al, 1995). Also, with respect to the phenotype of the primed NS3-specific T cells, similarities can be found between mice and humans.…”

Section: Discussionmentioning

confidence: 75%

Immunogenicity and antigenicity of the ATPase/helicase domain of the hepatitis C virus non-structural 3 protein

Sällberg

Zhang²,

Chen

et al. 1996

Journal of General Virology

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The immunogenicity and antigenicity of an enzymatically functional (ATPase/helicase) recombinant protein encompassing residues 1207-1612 of the hepatitis C virus (HCV) non-structural 3 (NS3) protein was characterized using B10 congenic mice. Previous studies have indicated a high frequency of NS3-specific antibodies in HCV-infected humans. Similarly, all six immunized murine haplotypes were antibody responders to the NS3 ATPase/helicase domain, with the H-2 k and H-2" haplotypes as high responders. As also observed in HCV-infected humans, the murine NS3 antibodies were predominantly directed to conformational determinants. Irrespective of the murine haplotype, IgG1 predominated in the primary anti-NS3 response, whereas IgG1 and IgG2b predominated in the secondary response. The antibody responder hierarchy was reiterated at the T cell level, with the H-2 k and the H-2' hapIotypes as the best responders. In both the H-2 d and H-2" hapIotypes ATPase/ helicase-primed T cells secreted interleukin 2 and interferon y, corroborating observations from HCVinfected humans. In the H-2 d, H-2 k and H-2' hapIotypes the fine specificity of the T cell recognition of the ATPase/helicase domain was further characterized. Multiple, although generally weak, T cell recognition sites were found for all three haplotypes. The large size of the NS3 protein together with the presence of multiple class II binding motifs explain the high prevalence of NS3 antibodies in immunized mice and predict a similar explanation for the observed high frequency of NS3-specific antibodies in HCV-infected humans.

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Section: Discussionmentioning

confidence: 75%

Immunogenicity and antigenicity of the ATPase/helicase domain of the hepatitis C virus non-structural 3 protein

Sällberg

Zhang²,

Chen

et al. 1996

Journal of General Virology

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“…In addition, HCcAg.120-VLPs/Montanide ISA888 immunization induced a differential epitope proliferative response (positive to A1 but not to A2 and A3 peptides) regarding the other immunogens, suggesting that this formulation modulated the HCcAg.120-specific immune response in BALB/c mice. Peptides A1, A2 and A3 comprise HCV epitopes previously described in mice and humans (Harase et al, 1995, Kakimi et al, 1995, Jackson et al, 1997. Particularly, A1 and A2 comprise epitopes specific for mouse T CD4+ lymphocytes (Kakimi et al, 1995, Harase et al, 1995.…”

Section: Control Of Infection In a Surrogate Challenge Modelmentioning

confidence: 99%

“…Peptides A1, A2 and A3 comprise HCV epitopes previously described in mice and humans (Harase et al, 1995, Kakimi et al, 1995, Jackson et al, 1997. Particularly, A1 and A2 comprise epitopes specific for mouse T CD4+ lymphocytes (Kakimi et al, 1995, Harase et al, 1995. Peptide A1 also encompasses an epitope specific for human B lymphocytes (Jackson et al, 1997).…”

Section: Control Of Infection In a Surrogate Challenge Modelmentioning

confidence: 99%

Recombinant in vitro assembled hepatitis C virus core particles induce strong specific immunity enhanced by formulation with an oil-based adjuvant

Acosta‐Rivero¹,

Poutou²,

Alvarez‐Lajonchere³

et al. 2009

Biol. Res.

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In the present work, immunogenicity of recombinant in vitro assembled hepatitis C virus core particles, HCcAg.120-VLPs, either alone or in combination with different adjuvants was evaluated in BALB/c mice. HCcAg.120-VLPs induced high titers of anti-HCcAg.120 antibodies and virus-specific cellular immune responses. Particularly, HCcAg.120-VLPs induced specific delayed type hypersensitivity, and generated a predominant T helper 1 cytokine profile in immunized mice. In addition, HCcAg.120-VLPs prime splenocytes proliferate in vitro against different HCcAg.120-specific peptides, depending on either the immunization route or the adjuvant used. Remarkably, immunization with HCcAg.120-VLPs/Montanide ISA888 formulation resulted in a significant control of vaccinia virus titer in mice after challenge with a recombinant vaccinia virus expressing HCV core protein, vvCore. Animals immunized with this formulation had a marked increase in the number of IFN-γ producing spleen cells, after stimulation with P815 cells infected with vvCore. These results suggest the use of recombinant HCV core particles as components of therapeutic or preventive vaccine candidates against HCV.

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“…Most reports have focused on the murine recognition of truncated recombinant versions of the HCV core protein (Chen et al, 1995 ;Harase et al, 1995 ;Kakimi et al, 1995) or naked DNA constructs containing the core gene (Lagging et al, 1995 ;Major et al, 1995). Interestingly, endogenously produced HCV core protein does not seem very immunogenic in mice (Lagging et al, 1995 ;Major et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

Immune responses to the hepatitis C virus NS4A protein are profoundly influenced by the combination of the viral genotype and the host major histocompatibility complex.

Chen

Hultgren³

et al. 1997

Journal of General Virology

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Hepatitis C virus core region: helper T cell epitopes recognized by BALB/c and C57BL/6 mice

Cited by 17 publications

References 64 publications

Immunogenicity and antigenicity of the ATPase/helicase domain of the hepatitis C virus non-structural 3 protein

Immunogenicity and antigenicity of the ATPase/helicase domain of the hepatitis C virus non-structural 3 protein

Recombinant in vitro assembled hepatitis C virus core particles induce strong specific immunity enhanced by formulation with an oil-based adjuvant

Immune responses to the hepatitis C virus NS4A protein are profoundly influenced by the combination of the viral genotype and the host major histocompatibility complex.

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