Madhumathi Jayaprakasam, Prince Prabhu Rajaiah, Gayatri Subash Chellam, Aparnaa Ramanathan, Kaliraj Perumal
Centre for Biotechnology, Anna University, Chennai 600025, India.
J Parasitol. 2010 Dec;96(6):1228-9. doi: 10.1645/GE-2532.1. Epub 2010 Jul 29.
Filarial thiordoxin peroxidase is a major antioxidant that plays a crucial role in parasite survival. Although Brugia malayi TPx has been shown to be a potential vaccine candidate, it shares 63% homology with its mammalian counterpart, limiting its use as a vaccine or drug target. In silico analysis of TPx sequence revealed a linear B epitope in the host's nonhomologous region. The peptide sequence (TPx peptide(27-48)) was synthesized, and its reactivity with clinical sera from an endemic region was analyzed. The peptide showed significantly high reactivity (P < 0.05) against the sera of putatively immune individuals compared to the nonendemic control sera. It also showed high reactivity against the sera of patients with chronic pathology and patent infection. The high reactivity of the peptide with endemic immune sera equivalent to that of whole protein shows that it forms a dominant B epitope of TPx protein and thus could be utilized for incorporation into a multiepitope vaccine construct for filariasis.
丝虫硫氧还蛋白过氧化物酶是一种主要的抗氧化剂，在寄生虫存活中起关键作用。尽管马来布鲁线虫TPx已被证明是一种潜在的疫苗候选物，但其与哺乳动物对应物有63%的同源性，限制了其作为疫苗或药物靶点的应用。对TPx序列的计算机分析揭示了宿主非同源区域中的一个线性B表位。合成了肽序列（TPx肽(27 - 48)），并分析了其与来自流行地区临床血清的反应性。与非流行对照血清相比，该肽对假定免疫个体的血清显示出显著高的反应性（P < 0.05）。它对患有慢性病理和显性感染患者的血清也显示出高反应性。该肽与流行免疫血清的高反应性等同于全蛋白，表明它形成了TPx蛋白的显性B表位，因此可用于纳入丝虫病的多表位疫苗构建体。
