Whole recombinant yeast-based immunotherapy induces potent T cell responses targeting HCV NS3 and Core proteins

Haller, Aurelia A.; Lauer, Georg M.; King, Thomas H.; Kemmler, Charles B.; Fiolkoski, Valerie; Lu, Yingnian; Bellgrau, Don; Rodell, Timothy C.; Apelian, David; Franzusoff, Alex; Duke, Richard C.

doi:10.1016/j.vaccine.2006.10.035

Cited by 97 publications

(70 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These specifi cations make them attractive for peptide-based therapeutic vaccine design (35). But, full length of NS3 by protease and helicase enzymatic activities may disturb the APCs activities and reduce suffi cient immune responses (36). Moreover, C-terminal domain of core is essential for processing of HCV, and previous studies showed a suppression of immune response by full length of core in murine model (37,38), and also, both terminals of core HCV have autoimmune sequences that are deleterious for vaccine activity (39).…”

Section: A B Cmentioning

confidence: 99%

From in-silico immunogenicity verification to in vitro expression of recombinant Core-NS3 fusion protein of HCV

Hekmat¹,

Siadat²,

Aghasadeghi³

et al. 2017

BLL

View full text Add to dashboard Cite

BACKGROUND AND OBJECTIVE: Hepatitis C virus (HCV) is a serious global health burden. There is no effective vaccine against HCV and new direct acting antivirals (DAAs) are so expensive and virtually unavailable to the public. Therefore, seeking for therapeutic or prophylactic vaccines is exigent and reliever. METHODS: The secondary and tertiary structures of the recombinant Core-NS3 (rC-N) fusion protein of HCV and its B and T-cells epitopes were evaluated with bioinformatics software. Cloning and in vitro expression of rC-N were performed by pET24a(+) and E.coli BL21-DE3 expression host, respectively. The recombinant protein purifi cation was done by affi nity chromatography method and then identifi ed by Western blotting using anti-His monoclonal antibody. RESULTS: The sequences of rC-N protein consist of 1-118 amino acid parts of Core and 1095-1384 amino acids of NS3 were connected by a fl exible linker (AAY) with proteasome cleavable site. The expressed and purifi ed 46.7292 kDa rC-N protein had antigenic value up to threshold and conservancy found in this chimeric protein. Ramchandran Plot analysis represented that most residues were fallen in favourable regions. It also interacted with both type I and II major histocompatibility complex (MHC I, II) molecules. The rC-N had antigenic behaviour to create T cell responses. CONCLUSION: The results indicated that conserved rC-N protein had the ability to induce T-cell-mediated immune responses and it could be utilized as a therapeutic vaccine candidate against HCV (Tab. 3, Fig. 4, Ref. 40). Text in PDF www.elis.sk.

show abstract

Section: A B Cmentioning

confidence: 99%

From in-silico immunogenicity verification to in vitro expression of recombinant Core-NS3 fusion protein of HCV

Hekmat¹,

Siadat²,

Aghasadeghi³

et al. 2017

BLL

View full text Add to dashboard Cite

show abstract

“…E.coli is the first host for recombinant gene expression which has been used more than 40 years but Pichia pastoris within the past 15 years, has been the second most-used host for recombinant gene expression. From1995 to 2009, using of P. pastoris has been increased from 4% to 17% but in the same time usage of E. coli remained 60% constantly (Falcón et al, 1999;Acosta-Rivero, Aguilar et al, 2001;Acosta-Rivero et al, 2003;Haller, Lauer et al, 2007;Mizukoshi et al, 2009;Lunsdorf et al, 2011). Yeast can secrete the protein in a form that mimics its native conformational structure and immunogenicity and in this condition the majority of antigenic epitopes with neutralization activity of antibodies be preserved.…”

Section: Vlp Productionmentioning

confidence: 99%

Hepatitis C Virus - Proteins, Diagnosis, Treatment and New Approaches for Vaccine Development

Keyvani

Fazlalipour²,

Monavari³

et al. 2012

Asian Pacific Journal of Cancer Prevention

View full text Add to dashboard Cite

“…Interactions between yeast and DCs result in DC maturation, and whole recombinant yeast internalized by DCs can deliver heterologous antigens to both MHC class I and class II pathways and induce potent cell-mediated immunity [Capilla et al, 2009;Bian et al, 2010;Haller et al, 2007]. Vaccination with Saccharomyces cerevisiae (S.cerevisiae) expressing tumor-associated antigens can induce antigen-specific T-cell responses and protect animals against tumor challenge.…”

Section: Yeast As An Efficient Tool In Vaccine Developmentmentioning

confidence: 99%

“…Yeast can be easily engineered to express multiple antigens and the inherent adjuvant properties of S. cerevisiae avoid the need for additional adjuvants. These characteristics make S. cerevisiae a potential vaccine vehicle for cancer and infectious diseases [Capilla et al, 2009;Bian et al, 2010;Haller et al, 2007]. There are some limitations and drawback in S. cerevisiae expression systems.…”

Section: Yeast As An Efficient Tool In Vaccine Developmentmentioning

confidence: 99%

Non-Viral Delivery Systems in Gene Therapy and Vaccine Development

Bolhassani¹,

Rafati²

2011

Non-Viral Gene Therapy

View full text Add to dashboard Cite

Whole recombinant yeast-based immunotherapy induces potent T cell responses targeting HCV NS3 and Core proteins

Cited by 97 publications

References 29 publications

From in-silico immunogenicity verification to in vitro expression of recombinant Core-NS3 fusion protein of HCV

From in-silico immunogenicity verification to in vitro expression of recombinant Core-NS3 fusion protein of HCV

Hepatitis C Virus - Proteins, Diagnosis, Treatment and New Approaches for Vaccine Development

Non-Viral Delivery Systems in Gene Therapy and Vaccine Development

Contact Info

Product

Resources

About