Screening and identification of T helper 1 and linear immunodominant antibody-binding epitopes in spike 1 domain and membrane protein of feline infectious peritonitis virus.
Screening and identification of T helper 1 and linear immunodominant antibody-binding epitopes in spike 1 domain and membrane protein of feline infectious peritonitis virus.
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DOI：
10.1016/j.vaccine.2014.01.074
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发表时间：
2014-04-01
期刊：
影响因子：
5.5
通讯作者：
Hohdatsu T
中科院分区：
文献类型：
--
作者：
Takano T;Morioka H;Gomi K;Tomizawa K;Doki T;Hohdatsu T
FIPV属于α冠状病毒，在野猫和家猫中引起致命疾病。Th 1细胞活性在FIPV感染的保护中起重要作用。我们鉴定了FIPV S1区和M蛋白的Th 1和抗体结合表位。我们从FIPV结构蛋白中筛选出3种能强烈诱导Th 1活性的肽。将3种肽与CpG-ODNs一起注射SPF猫，其中2种肽诱导了Th 1细胞活性。猫传染性腹膜炎病毒（FIP病毒：FIPV）在野生和家养猫中引起致命疾病。FIP预防性疫苗的开发需要不诱导抗体依赖性增强的抗原，并且辅助性T（Th）1活性在保护免受FIPV感染中起重要作用。在本研究中，我们确定了合成肽，包括Th 1和线性免疫显性抗体结合表位的S1结构域和M蛋白的FIPV。我们还根据这项研究和以前的研究（Satoh等）从FIPV的结构蛋白（S、M和N蛋白）衍生的肽中鉴定出强烈诱导Th 1活性的肽。在I型FIPV的S1结构域衍生的肽中没有鉴定出含Th 1表位的肽。与此相反，7 Th 1表位的肽被确定在S1结构域的II型FIPV，没有线性的免疫显性抗体结合表位包含在任何这些肽。在M蛋白衍生的肽中鉴定出11种各血清型共有的含Th 1表位的肽，并且2种肽（M-11和M-12）含有线性免疫显性抗体结合表位。在来自FIPV的S、M和N蛋白的肽中，对诱导比FIPV抗原的Th 1活性显著更强的那些肽进行了再筛选，并且鉴定了4种肽。当这些肽中的3种（M-9、I-S2-15和II-S1-24）被选择并与CpG-ODN一起给予SPF猫时，M-9和II-S1-24诱导Th 1活性。本研究结果可为开发抗FIPV感染的肽疫苗提供重要信息。
FIPV, belongs to Alphacoronavirus, causes a fatal disease in wild and domestic cats. Th1 activity plays an important role in protect against FIPV infection. We identified the Th1 and antibody-binding epitopes in S1 domain and M protein of FIPV. We selected 3 peptides that strongly induced Th1 activity from FIPV structural proteins. 3 peptides were administered with CpG-ODNs to SPF cats, 2 peptides induced Th1 activity. Feline infectious peritonitis virus (FIP virus: FIPV) causes a fatal disease in wild and domestic cats. The development of an FIP-preventive vaccine requires an antigen that does not induce antibody-dependent enhancement, and T helper (Th)1 activity plays an important role in protect against FIPV infection. In the present study, we identified synthetic peptides including Th1 and a linear immunodominant antibody-binding epitope in the S1 domain and M protein of FIPV. We also identified peptides that strongly induce Th1 activity from those derived from the structural proteins (S, M, and N proteins) of FIPV based on this and previous studies (Satoh et al.). No Th1 epitope-containing peptide was identified in the peptides derived from the S1 domain of type I FIPV. In contrast, 7 Th1 epitope-containing peptides were identified in the S1 domain of type II FIPV, and no linear immunodominant antibody-binding epitope was contained in any of these peptides. Eleven Th1 epitope-containing peptides common to each serotype were identified in the M protein-derived peptides, and 2 peptides (M-11 and M-12) contained the linear immunodominant antibody-binding epitope. Of the peptides derived from the S, M, and N proteins of FIPV, those that induced significantly stronger Th1 activity than that of the FIPV antigen were rescreened, and 4 peptides were identified. When 3 of these peptides (M-9, I-S2-15, and II-S1-24) were selected and administered with CpG-ODNs to SPF cats, M-9 and II-S1-24 induced Th1 activity. Our results may provide important information for the development of a peptide-based vaccine against FIPV infection.
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