Ramírez Rosa, Falcón Rosabel, Izquierdo Alienys, García Angélica, Alvarez Mayling, Pérez Ana Beatriz, Soto Yudira, Muné Mayra, da Silva Emiliana Mandarano, Ortega Oney, Mohana-Borges Ronaldo, Guzmán María G
PAHO/WHO Collaborating Centre for the Study of Dengue and its Vector, Institute of Tropical Medicine "Pedro Kourí", IPK, Autopista Novia del Mediodía Km 6 1/2, 17100, Havana, Cuba.
Virus Genes. 2014 Oct;49(2):185-95. doi: 10.1007/s11262-014-1087-3. Epub 2014 May 23.
The NS3 protein is a multifunctional non-structural protein of flaviviruses implicated in the polyprotein processing. The predominance of cytotoxic T cell lymphocytes epitopes on the NS3 protein suggests a protective role of this protein in limiting virus replication. In this work, we studied the antigenicity and immunogenicity of a recombinant NS3 protein of the Dengue virus 2. The full-length NS3 gene was cloned and expressed as a His-tagged fusion protein in Escherichia coli. The pNS3 protein was purified by two chromatography steps. The recombinant NS3 protein was recognized by anti-protease NS3 polyclonal antibody and anti-DENV2 HMAF by Western Blot. This purified protein was able to stimulate the secretion of high levels of gamma interferon and low levels of interleukin-10 and tumor necrosis factor-α in mice splenocytes, suggesting a predominantly Th-1-type T cell response. Immunized BALB/c mice with the purified NS3 protein showed a strong induction of anti-NS3 IgG antibodies, essentially IgG2b, as determined by ELISA. Immunized mice sera with recombinant NS3 protein showed specific recognition of native dengue protein by Western blotting and immunofluorescence techniques. The successfully purified recombinant protein was able to preserv the structural and antigenic determinants of the native dengue protein. The antigenicity shown by the recombinant NS3 protein suggests its possible inclusion into future DENV vaccine preparations.
NS3蛋白是黄病毒属的一种多功能非结构蛋白,参与多蛋白加工过程。NS3蛋白上细胞毒性T淋巴细胞表位占优势,表明该蛋白在限制病毒复制方面具有保护作用。在本研究中,我们研究了登革病毒2重组NS3蛋白的抗原性和免疫原性。将全长NS3基因克隆并在大肠杆菌中表达为His标签融合蛋白。通过两步层析法纯化pNS3蛋白。通过蛋白质印迹法,重组NS3蛋白可被抗蛋白酶NS3多克隆抗体和抗登革病毒2型人单克隆抗体识别。这种纯化蛋白能够刺激小鼠脾细胞分泌高水平的γ干扰素以及低水平的白细胞介素-10和肿瘤坏死因子-α,提示主要为Th1型T细胞应答。用纯化的NS3蛋白免疫BALB/c小鼠,通过酶联免疫吸附测定法确定,其诱导产生了强烈的抗NS3 IgG抗体,主要为IgG2b。用重组NS3蛋白免疫的小鼠血清通过蛋白质印迹法和免疫荧光技术显示出对天然登革病毒蛋白的特异性识别。成功纯化的重组蛋白能够保留天然登革病毒蛋白的结构和抗原决定簇。重组NS3蛋白显示的抗原性表明其可能被纳入未来的登革病毒疫苗制剂中。