Production and characterization of virus-like particles of grapevine fanleaf virus presenting L2 epitope of human papillomavirus minor capsid protein.

Yazdani, Razieh; Shams-Bakhsh, Masoud; Hassani-Mehraban, Afshin; Arab, Seyed Shahriar; Thelen, Nicolas; Thiry, Marc; Crommen, Jacques; Fillet, Marianne; Jacobs, Nathalie; Brans, Alain; Servais, Anne-Catherine

doi:10.1186/s12896-019-0566-y

Article (Scientific journals)

Production and characterization of virus-like particles of grapevine fanleaf virus presenting L2 epitope of human papillomavirus minor capsid protein.

Yazdani, Razieh; Shams-Bakhsh, Masoud; Hassani-Mehraban, Afshin et al.

2019 • In BMC Biotechnology, 19 (1), p. 81

Peer Reviewed verified by ORBi

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https://hdl.handle.net/2268/245410

DOI
10.1186/s12896-019-0566-y

PubMed
31752839

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Keywords :

Bionanoparticles; HPV; Heterologous expression systems; Nepovirus; Protein refolding; Vaccine antigen

Abstract :

[en] BACKGROUND: Virus-like particle (VLP) platform represents a promising approach for the generation of efficient and immunogenic subunit vaccines. Here, the feasibility of using grapevine fanleaf virus (GFLV) VLPs as a new carrier for the presentation of human papillomavirus (HPV) L2 epitope was studied. To achieve this goal, a model of the HPV L2 epitope secondary structure was predicted and its insertion within 5 external loops in the GFLV capsid protein (CP) was evaluated. RESULTS: The epitope sequence was genetically inserted in the alphaB-alphaB(") domain C of the GFLV CP, which was then over-expressed in Pichia pastoris and Escherichia coli. The highest expression yield was obtained in E. coli. Using this system, VLP formation requires a denaturation-refolding step, whereas VLPs with lower production yield were directly formed using P. pastoris, as confirmed by electron microscopy and immunostaining electron microscopy. Since the GFLV L2 VLPs were found to interact with the HPV L2 antibody under native conditions in capillary electrophoresis and in ELISA, it can be assumed that the inserted epitope is located at the VLP surface with its proper ternary structure. CONCLUSIONS: The results demonstrate that GFLV VLPs constitute a potential scaffold for surface display of the epitope of interest.

Research Center/Unit :

CIRM - Centre Interdisciplinaire de Recherche sur le Médicament - ULiège

Disciplines :

Pharmacy, pharmacology & toxicology

Author, co-author :

Yazdani, Razieh

Shams-Bakhsh, Masoud

Hassani-Mehraban, Afshin

Arab, Seyed Shahriar

Thelen, Nicolas ; Université de Liège - ULiège > Département des sciences de la vie > Biologie cellulaire

Thiry, Marc ; Université de Liège - ULiège > Département des sciences de la vie > Biologie cellulaire

Crommen, Jacques ; Université de Liège - ULiège > Département de pharmacie > Département de pharmacie

Fillet, Marianne ; Université de Liège - ULiège > Département de pharmacie > Analyse des médicaments

Jacobs, Nathalie ; Université de Liège - ULiège > Département des sciences biomédicales et précliniques > Virologie

Brans, Alain ; Université de Liège - ULiège > Département des sciences de la vie > Centre d'ingénierie des protéines

Servais, Anne-Catherine ; Université de Liège - ULiège > Département de pharmacie > Analyse des médicaments

Language :

English

Title :

Production and characterization of virus-like particles of grapevine fanleaf virus presenting L2 epitope of human papillomavirus minor capsid protein.

Publication date :

2019

Journal title :

BMC Biotechnology

eISSN :

1472-6750

Publisher :

BioMed Central, United Kingdom

Volume :

Issue :

Pages :

Peer reviewed :

Peer Reviewed verified by ORBi

Funders :

Fonds Léon Fredericq

Available on ORBi :

since 27 February 2020

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