Division of Viral Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, MD 20892, USA.
J Virol. 2011 Nov;85(21):10945-54. doi: 10.1128/JVI.05406-11. Epub 2011 Aug 24.
Transmission of pathogenic avian influenza viruses (AIV) from wild birds to domestic poultry and humans is continuing in multiple countries around the world. In preparation for a potential AIV pandemic, multiple vaccine candidates are under development. In the case of H5N1 AIV, a clear shift in transmission from clade 1 to clade 2 viruses occurred in recent years. The virus-like particle (VLP) represents an economical approach to pandemic vaccine development. In the current study, we evaluated the humoral immune response in humans vaccinated with H5N1 A/Indonesia/05/2005 (clade 2.1) VLP vaccine manufactured in Sf9 insect cells. The VLPs were comprised of the influenza virus hemagglutinin (HA), neuraminidase (NA), and matrix 1 (M1) proteins. In an FDA-approved phase I/II human clinical study, two doses of H5N1 VLPs at 15, 45, or 90 μg HA/dose resulted in seroconversion and production of functional antibodies. Moreover, cross-reactivity against other clade 2 subtypes was demonstrated using virus neutralization assays. H5N1 whole-genome fragment phage display libraries (GFPDL) were used to elucidate the antibody epitope repertoire in postvaccination human sera. Diverse epitopes in HA1/HA2 and NA were recognized by postvaccination sera from the two high-dose groups, including large segments spanning the HA1 receptor binding domain. Importantly, the vaccine elicited sera that preferentially bound to an oligomeric form of recombinant HA1 compared with monomeric HA1. The oligomeric/monomeric HA1 binding ratios of the sera correlated with the virus neutralizing titers. Additionally, the two high-dose VLP vaccine groups generated NA-inhibiting antibodies that were associated with binding to a C-terminal epitope close to the sialic acid binding site. These findings represent the first report describing the quality of the antibody responses in humans following AIV VLP immunization and support further development of such vaccines against emerging influenza virus strains.
致病性禽流感病毒(AIV)从野生鸟类向家禽和人类传播在世界多个国家仍在继续。为应对潜在的 AIV 大流行,多种疫苗候选物正在开发中。在 H5N1 AIV 的情况下,近年来病毒传播明显从 1 分支转变为 2 分支病毒。病毒样颗粒(VLP)是开发大流行疫苗的经济方法。在当前的研究中,我们评估了在 Sf9 昆虫细胞中制造的 H5N1 A/印度尼西亚/05/2005(2.1 分支)VLP 疫苗接种的人类中的体液免疫反应。VLPs 由流感病毒血凝素(HA)、神经氨酸酶(NA)和基质 1(M1)蛋白组成。在 FDA 批准的 I/II 期人类临床研究中,两剂 15、45 或 90 μg HA/剂量的 H5N1 VLPs 导致血清转化和功能性抗体的产生。此外,使用病毒中和测定法证明了对其他 2 分支亚型的交叉反应性。使用 H5N1 全基因组片段噬菌体展示文库(GFPDL)阐明了接种疫苗后的人类血清中的抗体表位谱。HA1/HA2 和 NA 中的不同表位被来自两个高剂量组的接种疫苗后血清识别,包括跨越 HA1 受体结合域的大片段。重要的是,疫苗诱导的血清优先与重组 HA1 的寡聚形式结合,而不是单体 HA1。血清的寡聚体/单体 HA1 结合比与病毒中和滴度相关。此外,两个高剂量 VLP 疫苗组产生了与结合接近唾液酸结合位点的 C 末端表位相关的 NA 抑制抗体。这些发现代表了描述 AIV VLP 免疫接种后人类抗体反应质量的首次报告,并支持针对新兴流感病毒株进一步开发此类疫苗。