Increasing cellular immunogenicity to peptide-based vaccine candidates using a fluorocarbon antigen delivery system

Francis, James N.; Thaburet, Jean-François; Bron, Dominique; Sizer, Philip J.H.; Brown, Carlton B.; Georges, Bertrand

doi:10.1016/j.vaccine.2014.12.061

Cited by 6 publications

(6 citation statements)

References 20 publications

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“…Sequentially conserved epitopes, which are generally less exposed, can elicit antibodies that are broadly cross reactive [36,37]. In recent years, small peptides corresponding to conserved epitopes of antibodies have been considered as potential vaccine candidates [32,38]. In this study we characterized the conserved linear epitope specificity of NAbs potentially involved in spontaneous viral clearance by detecting the reactivity of the serum samples…”

Section: Discussionmentioning

confidence: 99%

Characterization of linear epitope specificity of antibodies potentially contributing to spontaneous clearance of hepatitis C virus

Ahsan

Dar²,

Hassan³

et al. 2021

PLoS ONE

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Background Around 30% of the HCV infected patients can spontaneously clear the virus. Cumulative evidence suggests the role of neutralizing antibodies in such spontaneous resolution. Understanding the epitope specificity of such antibodies will inform the rational vaccine design as such information is limited to date. In addition to conformational epitope targeted antibodies, linear epitope specific antibodies have been identified that are broadly cross reactive against diverse HCV strains. In this study, we have characterized the potential role of three conserved linear epitopes in the spontaneous clearance of HCV. Methods We tested the reactivity of sera from chronic patients (CP) and spontaneous resolvers (SR) with linear peptides corresponding to three conserved regions of HCV envelope protein E2 spanning amino acids 412–423, 523–532 and 432–443 using ELISA. Subsequently, we characterized the dependency of HCV neutralization by the reactive serum samples on the antibodies specific for these epitopes using pseudoparticle-based neutralization assay. In ELISA most of the CP sera showed reactivity to multiple peptides while most of the SR samples were reactive to a single peptide suggesting presence of more specific antibodies in the SR sera. In most of the HCVpp neutralizing sera of particular peptide reactivity the neutralization was significantly affected by the presence of respective peptide. HCV neutralization by CP sera was affected by multiple peptides while 75% of the HCVpp neutralizing SR sera were competed by the 432 epitope. Conclusions These findings suggest that individuals who spontaneously resolve HCV infection at the acute phase, can produce antibodies specific for conserved linear epitopes, and those antibodies can potentially play a role in the spontaneous viral clearance. The epitope present in the 432–443 region of E2 was identified as the primary neutralizing epitope with potential role in spontaneous viral clearance and this epitope potentiates for the design of immunogen for prophylactic vaccine.

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Section: Discussionmentioning

confidence: 99%

Characterization of linear epitope specificity of antibodies potentially contributing to spontaneous clearance of hepatitis C virus

Ahsan

Dar²,

Hassan³

et al. 2021

PLoS ONE

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“…In addition, fluoropeptides are stable and resistant to proteolytic degradation. The binding of an eight-carbon chain to either the amino or carboxyl terminus induces greater CD4+ and CD8+ T cell responses in mice than native peptides ( 31 ).…”

Section: Universal Influenza Vaccine Candidatesmentioning

confidence: 99%

Multi-Epitope Peptide-Based and Vaccinia-Based Universal Influenza Vaccine Candidates Subjected to Clinical Trials

Romeli

Hassan

Yap

2020

MJMS

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In light of the limited protection conferred by current influenza vaccines, immunisation using universal influenza vaccines has been proposed for protection against all or most influenza sub-types. The fundamental principle of universal influenza vaccines is based on conserved antigens found in most influenza strains, such as matrix 2, nucleocapsid, matrix 1 and stem of hemagglutinin proteins. These antigens trigger cross-protective immunity against different influenza strains. Many researchers have attempted to produce the conserved epitopes of these antigens in the form of peptides in the hope of generating universal influenza vaccine candidates that can broadly induce cross-reactive protection against influenza viral infections. However, peptide vaccines are poorly immunogenic when applied individually owing to their small molecular sizes. Hence, strategies, such as combining peptides as multi-epitope vaccines or presenting peptides on vaccinia virus particles, are employed. This review discusses the clinical and laboratory findings of several multi-epitope peptide vaccine candidates and vaccinia-based peptide vaccines. The majority of these vaccine candidates have reached the clinical trial phase. The findings in this study will indeed shed light on the applicability of universal influenza vaccines to prevent seasonal and pandemic influenza outbreaks in the near future.

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“…The addition of F chain to peptides was applied in the development of vaccines as well. Thus, the presence of F chain in peptides derived from HIV, influenza and hepatitis C virus increased their cellular immunogenicity by controlling their ability to form micelles in solution [12] . More recently, we have shown that the conjugation of therapeutic peptides targeting GPCR with F chain provided a promising approach to enhance their plasma stability and in vivo activity [13] .…”

Section: Figurementioning

confidence: 99%

Self‐organization Properties of a GPCR‐Binding Peptide with a Fluorinated Tail Studied by Fluorine NMR Spectroscopy

Muizon¹,

Ramanoudjame

Esteoulle

et al. 2020

ChemBioChem

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Conjugation of the bioactive apelin‐17 peptide with a fluorocarbon chain results in self‐organization of the peptide into micelles. Fluorine NMR spectroscopy studies show that the fluoropeptide‘s micelles are monodisperse, while proton NMR indicates that the peptide moiety remains largely disordered despite micellization. A very fast exchange rate is measured between the free and micellar states of the peptide which enables the number of molecules present in the micelle to be estimated as 200, in agreement with values found by dynamic light scattering measurements.

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Increasing cellular immunogenicity to peptide-based vaccine candidates using a fluorocarbon antigen delivery system

Cited by 6 publications

References 20 publications

Characterization of linear epitope specificity of antibodies potentially contributing to spontaneous clearance of hepatitis C virus

Characterization of linear epitope specificity of antibodies potentially contributing to spontaneous clearance of hepatitis C virus

Multi-Epitope Peptide-Based and Vaccinia-Based Universal Influenza Vaccine Candidates Subjected to Clinical Trials

Self‐organization Properties of a GPCR‐Binding Peptide with a Fluorinated Tail Studied by Fluorine NMR Spectroscopy

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