Peptide presentation on primate erythroparvovirus 1 virus-like particles: In vitro assembly, stability and immunological properties
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- 作者：Areli del Carmen Morá ; n-Garcí ; aa ; Evelyn Rivera-Toledob ; Olga Echeverrí ; ac ; Gerardo Vá ; zquez-Ninc ; Beatriz Gó ; mezb ; Ismael Bustos-Jaimesa ; ismaelb@unam.mx" class="auth_mail" title="E-mail the corresponding author
- 关键词：Parvovirus B19 ; Virus-like particles ; Self-assembly ; Peptide display ; Respiratory syncytial virus
- 刊名：Virus Research
- 出版年：2016
- 出版时间：15 September 2016
- 年：2016
- 卷：224
- 期：Complete
- 页码：12-18
- 全文大小：1915 K
文摘
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N-terminal chimeras of primate erythroparvovirus 1 VP2 protein self-assemble into virus-like particles.
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VLPs are stable and 35% of their N-termini are exposed on the surface of the particles.
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N-terminal chimeras of PE1V VP2 co-assemble in vitro with non-chimeric VP2.
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PE1V VLPs constructed with different chimeras in defined ratios may lead to multifunctional particles.