CN110229221A - 一种用于检测侵袭性白色念珠菌病的抗原及其用途 - Google Patents
一种用于检测侵袭性白色念珠菌病的抗原及其用途 Download PDFInfo
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Abstract
本发明提供了一种用于检测侵袭性白色念珠菌病的抗原，其氨基酸序列如SEQ ID NO.4所示。本发明还提供了一种抗上述用于检测侵袭性白色念珠菌病的抗原的抗体。本发明提供了上述抗原在制备检测侵袭性白色念珠菌病的试剂中的用途。在临床已经确诊的患者中进行验证，模拟肽a的灵敏度分别为70.59%；特异度为85%。因此本发明的抗原可用于侵袭性白色念珠菌病的早期发现。
Description
技术领域
本发明属于生物医药领域，涉及一种抗原及其用途，具体来说是一种用于检测侵袭性白色念珠菌病的抗原及其用途。
背景技术
近年来，随着皮质类固醇、免疫抑制剂和抗生素的广泛应用，侵袭性真菌病(invasive fugus disease，IFD)呈现不断上升趋势，感染发病率越来越高，在免疫抑制患者中感染率列居第一位[Nielsen M，Lundegaard C，Blicher T，Peters B，Sette A，Justesen S，Buus S，Lund O.Quantitative predictions of peptide binding to anyHLA-DR molecule of known sequence:NetMHCIIpan.PLoS Comput Biol，2008，4(7):1000-1107.][Singh H，Raghava GP.ProPred:prediction of HLA-DR bindingsites.Bioninformatics，2001，17(12):1236-1237.]，在IFD中，酵母菌感染占绝大数，而酵母菌感染中又以白色念珠菌最常见，占50％，其归因死亡率约40％-50％。
白色念珠菌是一种酵母样真菌，在不同的条件下以孢子、酵母、和增殖的菌丝体等多种形态存在，可分别表达不同抗原，临床证据表明，侵袭性白色念珠菌病极难准确诊断，临床无特异性的临床表现和特异性的肺部影像学改变，其早期发现非常困难。而该菌在形态转变早期阶段形成芽管是该菌由定植菌向致病菌转变的标志，HWP1等菌丝蛋白在这一转变过程中为特异性表达的蛋白，因此通过检测HWP1抗体的存在可以判断患者是否是侵袭性白色念珠菌感染。
当前，由于HWP1菌丝抗原制备程序复杂，相应的抗体制备与纯化也因此难以实现，因此，通过分析HWP1菌丝蛋白的一级结构氨基酸序列，对其抗原表位进行分析预测，并通过人工合成抗原模拟肽，为解决这一问题提供了可能的途径。本发明对B细胞与Th细胞表位同时进行分析预测，试图选取能够同时诱导体液免疫和细胞免疫的HWP1抗原表位供进一步分析研究。
发明内容
本发明的目的在于提供一种用于检测侵袭性白色念珠菌病的抗原及其用途，所述的这种用于检测侵袭性白色念珠菌病的抗原及其用途要解决现有技术中极难准确诊断侵袭性白色念珠菌感染的技术问题。
本发明提供了一种用于检测侵袭性白色念珠菌病的抗原，其氨基酸序列如SEQ IDNO.4所示。
本发明还提供了一种抗上述用于检测侵袭性白色念珠菌病的抗原的抗体。
本发明提供了上述抗原在制备检测侵袭性白色念珠菌病的试剂中的用途。
本发明通过对B细胞与Th细胞表位同时进行分析预测，选取能够同时诱导体液免疫和细胞免疫的HWP1抗原表位。结果显示在HWP1蛋白中，位于265～286AA处的“SGSSILATTSESSSAPATTPN”，如SEQ ID NO.4所示；位于533～556AA的“APAGPGASSSPKSSVLASETSPIA”，如SEQ ID NO.5所示；以及位于560～579AA的“ETAPAGSSGAITIPESSAVV”序列，如SEQ ID NO.6所示；具备B细胞表位的潜力，同时也在一定程度上存在作为Th细胞表位的可能性，因此可用于模拟HWP1蛋白抗原进行抗原抗体的筛选反应。
本发明和已有技术相比，其技术效果是积极和明显的。将上述序列用化学合成法生成模拟肽，分别命名为模拟肽a，b和c。在临床已经确诊的患者中进行验证，模拟肽a，b和c的灵敏度分别为：70.59％，52.94％和41.18％。特异度分别为：85％，85％和95％。因此模拟肽a可用于侵袭性白色念珠菌病的早期发现。
附图说明
图1显示了HWP1氨基酸序列相似性搜索比对结果。
图2为Th细胞表位在线预测的一个参数设置图。
图3为Th细胞表位在线预测的另外一个参数设置图。
具体实施方式
实施例1序列选取
利用NCBI(http://www.ncbi.nlm.nih.gov)整合的蛋白检索功能，以“HWP1”为检索字段，搜索hyphal wall protein 1(Candida albicans)氨基酸序列，排除干扰项，选取GenBank accession No.为AAC96368的HWP1作为分析序列(序列全长634aa)，序列如SEQ IDNO.1所示：
使用NCBI氨基酸序列BLAST功能，对所选序列进行在线比对。
如图1序列对比结果显示：查询序列与NCBI所收录全序列同源性为100％，与收录的非全长序列在各自相应的长度内同源性也为100％，表明所选HWP1蛋白质一级结构氨基酸序列具有代表性，序列可用。
实施例2B细胞表位预测
综合对比多种抗原预测分析软件[Godkin A J，Smith KJ，Willis A，etal.Naturally processed HLA class II peptides reveal highly conservedimmunogenic flanking region sequence preferences that reflect antignprocessing rather than peptide-MHC interactions.J Immumol，2001，166(11):6720-6727][Nielsen M，Lund O.NN-align-A neural network-based alignment algorithmfor MHC class II peptide binding prediction.BMC Bioinformatics.2009，18；10:296.][Nielsen M，Lundegaard C，Lund O.Prediction of MHC class II bindingaffinity using SMM-align，a novel stabilization matrix alignment method.BMCBioinformatics.2007，8:238.]。
B细胞表位预测采用网络服务器PREDICTED ANTIGENIC PEPTIDES，Bcepred(http://www.imtech.res.in/raghava/bcipep)进行，参数设置如下：Immunogenicity＝"Immunodominant"；Mesure of Neutralization＝"YES"；Pathogen Group＝"Fungi"/
在综合分析了蛋白质亲水性(hydrophilicity)、转角(turns)、表面(surface)、极性(polar)、柔韧性(flexibility)、可及性(accessibility)等抗原构成的特征要素后，B细胞表位的在线预测结果如下，下划线部分氨基酸序列即为推荐的B细胞抗原表位：
MRLSTAQLIAIAYYMLSIGATVP(23)QVDGQGET(31)EEALIQKRSYDYYQEPCDDYPQQQQQQEPCDYPQQQQQEEPCDYPQQQPQEPCDYPQQPQEPCDYPQQPQEPCDYPQQPQEPCDNPPQPDVPCDNPPQPDVPCDNPPQPDIPCDNPPQPDIPCDNPPQPDQPDDNPPIPNIPTDWIPNIPTDWIPDIPEKPTTPATTPNI(201) PATTTTSESSSSSSSSSSSTTPKTSASTTPE(232)SSV(235)PATTPNTSVPTTSSESTTPATSPESSVPVTSGS (268)SI(270)LATTSESSSAPATTPN(286)TSV(289)PTTTTETKSSS(300)TPLTTTTEHDTTVV(314) TVTSCS(320)NSVCTESEVTTGVIVITSKDTIYTTYCPLTETTPVSTAPATETPTG(366)TVSTSTEQS(375)TTVI(379)TVTSCSESSCTE(391)SEVTTGVVVVTSEETVYTTFCPLT(415)ENTPGTDST(424)PEASIPPMET(434)IPAGSESS(442)MPAGETSPAVPKSDVPATESAPVPEMTPAGSQPSIPAGETSPAVPKSDVPATESAPAPEMT(503)PAGTET(509)KPAAPKSSAPATEPSPVAPGTESA(533)PAGPGASSSPKS(545)SVLASETSPIAPGAE(560)TAPAGS(566)SGAITIPESSAVVSTTEGAIPTTLESVPLMQPSANYSSVAPISTFEGAGNNMRLTFGAAIIGIAAFLI。
在综合分析了蛋白质亲合反应半抑制浓度(affinity IC50value)、耦联中心(binding core)等抗原表位的特征要素后不同位点亲合活性排序结果显示，与各类Th细胞表位结合后表现为结合强(SB)或次强结合(WB)的氨基酸序列抗原表位主要集中在两个区段：其中之一位于328…340…354AA；其二为607…617…634AA。因此，328～354AA以及607～634AA区段可作为Th细胞表位的候选抗原，其氨基酸序列分别为“EVTTGVIVITSKDTIYTTYCPLTETTP，如SEQ ID NO.2所示”和“PISTFEGAGNNMRLTFGAAIIGIAAFLI，如SEQ ID NO.3所示”。
实施例3 Th细胞表位预测
MHC II类分子Th抗原表位预测采用网络服务器NetMHCII(http:// www.cbs.dtu.dk/services/NetMHCII)进行在线分析[Saha.S，Raghava GP.BcePred:Prediction of Continuous B-Cell Epitopes in Antigenic Sequences Usingrecurrent neural network.Proteins.2006，65(1):40-48.]。
选取具有广泛代表意义的人类白细胞抗原(human leukocyte antigen，HLA)DR座子(loci)上的6个表位HLA-DRB1*0101，HLA-DRB1*0301，HLA-DRB1*0401，HLA-DRB1*0701，HLA-DRB1*1101，HLA-DRB1*1501作为结合位点，以每15个氨基酸残基作为步查单位(walking unit)提交查询任务，下载Ecexl工作表，分析查证可能成为广泛MHC II抗原表位的HWP1氨基酸序列。Th细胞表位在线预测的参数设置图解如图2、图3所示。
实施例4氨基酸序列的同源建模评估
选取B细胞表位预测结果理想、同时尽可能满足Th细胞预测效果的氨基酸序列，登录瑞士生物信息研究所关于已知结构的蛋白质晶体衍射数据库(http:// swissmodel.expasy.org/workspace)网站提交任务，采用自动搜索方式进行蛋白质空间结果的同源建模评估。
经与B细胞表位预测结果对照分析，未发现同时满足所有检测的Th细胞表位和B细胞表位的区段，但在265～286AA处发现能够满足B细胞表位和多数Th细胞表位(3个等位基因)要求的区段，其氨基酸序列(模拟肽a)为“SGSSILATTSESSSAPATTPN”序列，如SEQ IDNO.4所示，其余两段氨基酸序列在满足B细胞表位的前提之下，也能较好地与Th表位预测结果吻合，分别是位于533～556AA的(模拟肽b)“APAGPGASSSPKSSVLASETSPIA序列，如SEQ IDNO.5所示”和位于560～579AA的(模拟肽c)“ETAPAGSSGAITIPESSAVV序列，如SEQ ID NO.6所示”。
实施例5
根据HWP1位于265～286AA、533～556AA和560～579AA的序列采用现有技术的化学合成法分别合成模拟肽a、b和c。
合成短肽最佳浓度确定：称取合成短肽各1mg，双蒸水溶解至1mg/ml。用NaHCO3溶液分别将1mg/ml的短肽依次稀释至2ug/100ul，1ug/100ul，0.5ug/100ul和0.5ug/100ul，于酶标板内，每孔加入100ul，NaHCO3溶液做阴性对照，4度孵育过夜，去包被液，3％脱脂奶粉37度封闭2h；去封闭液，PBST洗板3次，每次5min。分别取侵袭性病人血清和正常血清，用PBST作1:50、1:100、1:200和1:400稀释，每孔加入100ul，37度作用2h；PBST洗板6次，每次10min；各孔加入1:3000稀释的HRP-羊抗人IgG100ul，37度作用1h；PBST洗板6次，每次10min；各孔加TMB显色液A和B各1滴，显色10min，加终止液1滴终止反应。置酶标板上读取OD450，将侵袭性白色念病患者血清/正常人血清OD450值(P/N)≥2.0且为最大时的浓度为最佳反应。
合成短肽a、b和c用于侵袭性念珠菌病诊断效能的评估。结果如下：
最佳包被浓度的测定：
经ELISA检测显示，当合成短肽a，b和c浓度为0.5μg/100ul且病人血清和正常人血清的工作浓度为1:200稀释时，P/N值＝2.13(b为2.04，c为2.03)为最大。表示最佳反应浓度为合成短肽0.5μg/100ul，血清一抗做1:200稀释，见表1、表2和表3。
表1合成短肽a的实际浓度测定OD450值
表2合成短肽b的实际浓度测定OD450值
表3合成短肽c的实际浓度测定OD450值
实施例7
ELISA诊断侵袭性念珠菌病：用于临床病人的诊断效能评估，选取经血培养、骨髓培养或者胸水培养确诊的侵袭性白色念珠菌患者17例，健康体检者20例。
以0.5ug/孔分别包被合成肽，于4度孵育过夜，弃去包被液，3％脱脂奶粉于37度封闭2h，弃去封闭液，PBST洗板3次，每次5min。分别加入PBST1:100稀释侵袭性白色念病患者和正常人血清，于37度作用2h。PBST洗板6次，每次10min。各孔加入1:3000稀释的HRP-羊抗人IgG100ul，37度作用1h。PBST洗板6次，每次10min。各孔滴加TMB显色剂A、B液各1滴，显色10min，加1滴终止液终止反应。酶标仪检测OD450值+2SD作为阳性结果的阈值。
表4合成短肽的ELISA结果
结论与分析：
分析结果显示，在HWP1蛋白中，位于265～286AA处的“SGSSILATTSESSSAPATTPN”、位于533～556AA的“APAGPGASSSPKSSVLASETSPIA”以及位于560～579AA的“ETAPAGSSGAITIPESSAVV”序列具备B细胞表位的潜力，同时也在一定程度上存在作为Th细胞表位的可能性，因此可用于模拟HWP1蛋白抗原进行抗原抗体的筛选反应。
选取经血培养、骨髓培养或者胸水培养确诊的侵袭性白色念珠菌患者17例，健康体检者20例对合成的短肽进行诊断效率验证。结果模拟肽a的诊断灵敏度最高是41.18％，而其特异度为95％。因此，HWP1模拟肽a能用于对侵袭性白色念珠菌病的早期发现。
序列表
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Claims (3)
1.一种用于检测侵袭性白色念珠菌病的抗原，其特征在于：其氨基酸序列如SEQ IDNO.4所示。
2.一种抗权利要求1所述的一种用于检测侵袭性白色念珠菌病的抗原的抗体。
3.权利要求1所述的抗原在制备检测侵袭性白色念珠菌病的试剂中的用途。
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| CN1645145A (zh) * | 2004-08-09 | 2005-07-27 | 中国人民解放军南京军区南京总医院 | 检测白念珠菌菌丝蛋白抗体的方法及试剂盒 |
| CN102574895A (zh) * | 2009-07-03 | 2012-07-11 | 加州大学洛杉矶海滨分校医学中心的洛杉矶生物医学研究所 | 作为针对念珠菌的主动和被动免疫接种的靶标的hyr1 |
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| CN1645145A (zh) * | 2004-08-09 | 2005-07-27 | 中国人民解放军南京军区南京总医院 | 检测白念珠菌菌丝蛋白抗体的方法及试剂盒 |
| CN102574895A (zh) * | 2009-07-03 | 2012-07-11 | 加州大学洛杉矶海滨分校医学中心的洛杉矶生物医学研究所 | 作为针对念珠菌的主动和被动免疫接种的靶标的hyr1 |
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