Helix Stabilization in the C-Terminal Peptide of Chicken Riboflavin Carrier Protein Enhances Immunogenicity and Prolongs Contraceptive Potential as an Epitope-Based Vaccine in Female Rats

Subramanian, S.; Karande, Anjali A.; Adiga, P. Radhakantha

doi:10.1006/bbrc.2001.5571

Cited by 10 publications

(3 citation statements)

References 31 publications

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“…For example, using network protein sequence analysis (5) it was predicted that 3A4-TR peptide contains high content of α-helix and contrarily 3A4-TR/P and 3A4-TR/PP peptides have almost all random structure, which are probably due to the presence of Pro residues in the peptide sequence. Therefore, the current study seems to contradict previous reports suggesting that peptide antigenicity may be enhanced by helix stabilization in the C-terminal peptide of chicken riboflavin carrier protein (6,7). However, many peptide antigens contain Pro residue(s) in epitope sequences that have a potential helix structure.…”

Section: Figcontrasting

confidence: 99%

Effects of epitope sequence tandem repeat and proline incorporation on polyclonal antibody production against cytochrome 1A2 and 3A4

Ahn¹,

Yun²

2009

BMB Reports

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We describe a method for producing polyclonal antibodies against peptide antigen cytochrome P450 1A2 and 3A4 using a tandem repeat of the epitope region and incorporation of proline residue between the repeated sequences. An ELISA assay revealed more efficient generation of polyclonal antibodies to tandem repeat peptide antigens than mono-epitope peptides. The incorporation of proline residues further stimulated antibody production. [BMB reports 2009; 42(7): 418-420]

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Section: Figcontrasting

confidence: 99%

Effects of epitope sequence tandem repeat and proline incorporation on polyclonal antibody production against cytochrome 1A2 and 3A4

Ahn¹,

Yun²

2009

BMB Reports

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“…The presence of antibodies directed to the denatured conformation of a protein is thought to be the cause of the often observed problem of nonneutralizing antibody responses, which nevertheless can be positive for the presence of antibody as measured by immunocapture techniques against plate-bound antigen [34]. Production of antibodies against the correct protein conformation is critical to the generation of a neutralizing antibody response [35][36][37].…”

Section: Discussionmentioning

confidence: 99%

Mutational effects on protein folding stability and antigenicity: the case of streptococcal pyrogenic exotoxin A

Carra

Welcher

Schokman

et al. 2003

Clinical Immunology

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“…Hydrophobic and α-helical modifications on peptides change their physicochemical properties that in turn modulate the immunogenicity and the production of neutralizing antibodies via its ability to interact with cell membranes and/or MHC class II-peptide-TCR complex (Espejo et al, 2004). A very good correlation is observed between helipticity of a synthetic or chimeric peptide antigen and the relative affinities of the derived antibody for the native protein, with similar affinities being observed for the analogs with the highest helical content (Subramanian et al, 2001;Lelievre et al, 1997;Gurunah et al, 1995).…”

Section: Enhanced Liposomal Vaccine Formulation and Performance 223mentioning

confidence: 93%

Enhanced Liposomal Vaccine Formulation and Performance: Simple Physicochemical and Immunological Approaches

Silva¹,

Takata

Sant’Anna

et al. 2006

Journal of Liposome Research

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The Dtxd (Diphtheria toxoid) was the first antigen encapsulated within liposomes, their adjuvant properties were discovered (their capacity to enhance the vaccine immunogenicity). The point here is not to propose a new method to prepare this lipossomal vaccine. The central idea is to give new dresses for old vaccines by using classical and well-established liposome preparation method changing only the encapsulation pH and the immunization protocol. The most appropriate method of Dtxd encapsulation within liposome was based on lipid film hydration in 100 mM citrate buffer, pH 4.0. This was accompanied by changes on protein hydrophobicity, observed by CD and fluorescence spectroscopies. Whenever the Dtxd exposed its hydrophobic residues at pH 4.0, it interacted better with the lipossomal (observed by electrophoretic mobility) film than when its hydrophobic residues were buried (pH 9.0). The Dtxd partition coefficient in Triton-X114 and the acrylamide fluorescence quenching were also pH dependent. Both were bigger at pH 4.0 than at pH 9.0. The relationship protein structure and lipid interaction was pH dependent and now it can be easily maximized to enhance encapsulation of antigens in vaccine development. Mice were primed with formulations containing 5 mug of Dtxd within liposomes prepared in pH 4.0 or 7.0 or 9.0. The boosters were done 38 or 138 days after the first immunization. The IgM produced by immediate response of all lipossomal formulations were higher than the control (free protein). The response patterns and the immune maturity were measured by IgG1 and IgG2a titrations. The IgG1 titers produced by both formulations at pH 4.0 and 7.0 were at least 22 higher than those produced by mice injected lipossomal formulation at pH 9.0. When the boosters were done, 138 days after priming the mice produced a IgG2a titer of 29 and the group that received the booster 30 days after priming produced a titer of 25. The strongest antibody production was the neutralizing antibody (245 higher than the control) produced by those mice injected with lipossomal formulation at pH 4.0 with the booster done 138 days after priming. The simple change on lipossomal pH formulation and timing of the booster enhanced both antibody production and selectivity.

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Helix Stabilization in the C-Terminal Peptide of Chicken Riboflavin Carrier Protein Enhances Immunogenicity and Prolongs Contraceptive Potential as an Epitope-Based Vaccine in Female Rats

Cited by 10 publications

References 31 publications

Effects of epitope sequence tandem repeat and proline incorporation on polyclonal antibody production against cytochrome 1A2 and 3A4

Effects of epitope sequence tandem repeat and proline incorporation on polyclonal antibody production against cytochrome 1A2 and 3A4

Mutational effects on protein folding stability and antigenicity: the case of streptococcal pyrogenic exotoxin A

Enhanced Liposomal Vaccine Formulation and Performance: Simple Physicochemical and Immunological Approaches

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