CN112522236A - 一种针对k1荚膜大肠杆菌的噬菌体内切唾液酸酶及其应用 - Google Patents
一种针对k1荚膜大肠杆菌的噬菌体内切唾液酸酶及其应用 Download PDFInfo
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Abstract
本发明公开了一种针对K1荚膜大肠杆菌的噬菌体内切唾液酸酶及其应用。所述内切唾液酸酶核苷酸序列为Seq ID No.1,氨基酸序列为Seq ID No.2所示。该裂解酶具有针对K1荚膜大肠杆菌的特性，可以作为有效的抗菌成分来特异性灭活这一类细菌，并且能够在疾病诊断、医疗卫生、食品加工等方面发挥作用；该酶制剂可以单独或复配使用，能够特异性灭活某些细菌，为细菌感染的防治和食源性细菌污染提供安全可靠的酶制剂来源。
Description
技术领域
本发明属于生物医药领域，具体涉及了一种针对K1荚膜大肠杆菌的噬菌体的内切唾液酸酶的制备方法及其作为抑菌剂成分在医疗卫生和食品加工等方面的应用。
背景技术
大肠杆菌(Escherichia coli)为埃希氏菌属(Escherichia)代表菌，它包括动物或人共生菌株和致病性菌株。致病性大肠杆菌给人和动物健康造成危害，也给农业生产带来了巨大的损失。引起新生儿细菌性脑膜炎的肠道外致病性大肠杆菌大多都有K1荚膜，它能够穿过血脑屏障致病，而K1荚膜则是主要致病因子。主要成分是由2，8唾液酸连接成的多聚体-多聚唾液酸。尽管使用了先进的抗生素，但与大肠杆菌K1脑膜炎相关的发病率和死亡率在过去几十年中保持不变。另外，由于近来耐药大肠杆菌K1株的激增，死亡率可能会进一步显着增加。
近年来，噬菌体治疗被认为是能够缓解多重耐药菌严峻形式的有效方案。由于噬菌体存在广泛，种类多样，宿主特异性强等特点，可以作为治疗细菌感染的新型生物制剂。目前已经分离到了多种具有多糖专一性的噬菌体，可以特异性降解细菌胞外多糖，从而能够使细菌毒力下降。K1专一性噬菌体可以特异性降解K1荚膜，从而使其毒力减弱，致病性减弱。同时，这些噬菌体可用于大肠杆菌的分型检测。而K1专一性噬菌体上的尾部蛋白可以发挥唾液酸内切酶的功能来专一性的分解多聚唾液酸。专利96195235.0中提及了在早期发现的内切唾液酸酶，但是没有进行抑菌功能的验证。本专利中所描述的内切唾液酸酶的基因序列和蛋白结构均与其有较大差异，制备方法也有所不用。且本专利中描述了该酶的抑菌效果，扩宽了应用范围。
发明内容
本发明目的之一在于提供了一种针对K1荚膜大肠杆菌具有裂解作用的新型噬菌体内切唾液酸酶及其制备和应用。该唾液酸内切酶可以专一性降解多聚唾液酸，而且具有一定程度的抑菌功能，具有特异性强、安全无毒、水溶性好的优点。
本发明目的之二还提供了上述内切唾液酸酶的制备方法。
本发明的目的通过以下技术方案实现：
本发明提供了一种针对K1荚膜大肠杆菌具有裂解作用的内切唾液酸酶，氨基酸序列如Seq ID No.2所示，或者与只具有至少95％同源性的具有K1荚膜大肠杆菌裂解活性的酶。
本发明还提供编码本发明所述的内切唾液酸酶的编码基因。在一种具体的实施例中，本发明所述的编码基因，其核苷酸序列如Seq ID No.1所示。需要说明的是，由于同一氨基酸可能有多种不同的密码子来决定，所以编码上述内切唾液酸酶的核苷酸序列并不局限于Seq ID No.1所示的序列，也可以是由与Seq IDNo.1所示核苷酸序列突变一个或几个核苷酸形成同义突变得到可编码相同氨基酸序列的核苷酸序列。
本发明还提供了一种载体，该载体包含可编码所述内切唾液酸酶的编码基因。
本发明还提供一种重组细胞，包含：可编码所述内切唾液酸酶的编码基因，或者包含可编码内切唾液酸酶的编码基因的载体。
在本发明的一种具体的实施例中，本发明还提供本发明所述内切唾液酸酶的具体制备方法，包括以下步骤：
(1)根据目的基因序列(Seq ID No.1)及载体pET28a酶切位点设计带有同源臂的扩增引物；用PCR方法扩增目的基因片段，将扩增产物进行胶回收；酶切载体也进行胶回收；
(2)使用同源重组试剂盒连接目的基因片段和载体，将连接产物使用热激转化的方式转入DH5α感受态细胞；经培养后，鉴定出阳性的重组质粒并进行重组质粒提取；
(3)将重组质粒经热激转化进入BL21感受态细胞，经培养后，鉴定出阳性转化子；
(4)将含有重组质粒的BL21阳性转化子扩大培养后，达到对数生长期时加入IPTG进行诱导表达。并经超声破碎后进行蛋白纯化。
本发明还提供一种扩增本发明所述内切唾液酸酶编码基因的引物对：
引物F：
5’-CAGCAAATGGGTCGCGGATCCATGTCAACTACAATTACTAATTTACCCGA-3’；
引物R：
5’-GCAAGCTTGTCGACGGAGCTCTTATTTACTTTCCAGGGTTGCAAG-3’。
本发明还提供一种包含本发明所述内切唾液酸酶的试剂。
本发明还提供所述内切唾液酸酶或所述试剂在细菌分类、细菌感染诊断、细菌感染防治、医疗卫生用品或食品添加剂中的应用。其中细菌在一些实施例中，是指K1荚膜大肠杆菌。
本发明还提供所述内切唾液酸酶或所述试剂在K1荚膜大肠杆菌防治和/或食源性细菌污染防治中的应用。
本发明在用于抑制K1型大肠杆菌时，可以选择合适的剂量进行，例如大于或等于0.1μg/mL；在一些更具体的实施例中，为大于或等于0.5μg/mL，具体可根据需要进行选择，例如包括但不限于0.5～5μg/mL。
本发明的积极效果在于：该裂解酶具有针对K1荚膜大肠杆菌的特性，可以特异性水解由2，8唾液酸单体聚合成的多聚唾液酸，具有抑制K1型大肠杆菌生长的作用。可以作为有效的抗菌成分来特异性灭活这一类细菌，并且能够在疾病诊断、医疗卫生、食品加工等方面发挥作用；该酶制剂可以单独或复配使用，能够特异性灭活某些细菌，为细菌感染的防治和食源性细菌污染提供安全可靠的酶制剂来源。
附图说明
图1为目的基因扩增及载体酶切电泳图，其中，A图为本发明中内切唾液酸酶基因的PCR扩增产物电泳图，B图为pET28a载体酶切产物电泳图。
图2为本发明中内切唾液酸酶基因与pET28连接构成的重组表达载体的鉴定电泳图。
图3为本发明中构建的重组蛋白表达SDS-PAGE图。A图中，第1泳道为Mark，第2泳道诱导前蛋白表达，第3泳道为诱导后的蛋白表达情况，第4泳道为包涵体中表达情况，第5泳道为上清中蛋白表达情况；图B为上清纯化前后的对比状态，第2泳道为纯化前，第3泳道为纯化后。
图4为本发明中内切唾液酸酶的作用效果对比图。A，B，C分别为三株K1荚膜菌株DE205B，RS218，CVCC1359，D为阴性对照菌株DH5α，E为阴性对照PBS。
图5为实施例3中不同浓度的内切唾液酸酶的动态抑菌曲线图。
具体实施方式
下面通过具体的实施例来叙述本发明方法。除非特别说明，本发明中所用的技术手段均为本领域人员所公知的方法。另外，实施方案应当理解为说明性的，非限制本发明的范围。本发明的实质和范围仅由权利要求书所限定。对本领域技术人员而言，在不背离本发明的实质和范围的前提下，对这些实施方案中的物料成分和用量进行的各种改变和改动也属于本发明的保护范围。
以下实施例中用到的宿主菌K1荚膜大肠杆菌RS218为O18:K1:H7血清型(专利CN200510005392.1中所提及RS218菌株；Effects of ompA deletion on expression oftype 1fimbriae in Escherichia coli K1 strain RS218 and on the association ofE.coli with human brain microvascular endothelial cells)，DE205B(Effects ofibeA deletion on virulence and biofilm formation of avian pathogenicEscherichia coli；nrdF基因介导禽致病性大肠杆菌DE205B的抗氧化应激)，CVCC1359购买自中国兽医微生物菌种保藏管理中心(菌种保藏编号为CVCC1359)，非K1荚膜大肠杆菌DH5α(感受态)购买自诺唯赞生物科技有限公司。
本发明实施例中所述内切唾液酸酶为一种来自噬菌体的内切唾液酸酶，核苷酸序列为Seq ID No.1,氨基酸序列为Seq ID No.2所示，也可通过人工合成。
实施例1重组质粒的构建
(1)目的基因的扩增及产物回收
按照目的基因序列Seq ID No.1设计引物，并使用pET28a载体的酶切位点BamHI和SacI设计目的基因扩增的引物同源臂。引物F和R分别为：
引物F：
5’-CAGCAAATGGGTCGCGGATCCATGTCAACTACAATTACTAATTTACCCGA-3’
引物R：
5’-GCAAGCTTGTCGACGGAGCTCTTATTTACTTTCCAGGGTTGCAAG-3’
煮沸的噬菌体来粗提DNA作为PCR的模板，使用Primestar HS(Takara)进行PCR反应。将PCR产物用1％的琼脂糖凝胶电泳进行条带鉴定，如图1A所示。将鉴定后的产物进行胶回收纯化，并测定该片段回收的浓度。
PCR体系：50μL体系
PCR反应条件：
(2)载体酶切及产物回收
使用Takara限制性内切酶BamHI和SacI进行酶切反应，酶切反应体系为50μL体系，酶切条件为37℃，3h。将产物进行琼脂糖凝胶电泳(图1B)。进行胶回收并测定产物浓度。
酶切反应体系为50μL体系：
(3)同源重组法构建重组质粒
使用诺唯赞一步同源重组试剂盒将目的基因片段和酶切产物连接，将连接产物用热激转化的方式转入DH5α中：将DH5α感受态细胞从-80℃取出置于冰上融化，向每100ul感受态细胞中加入10μL连接产物，混匀后置于冰上30min。将离心管放入42℃水浴锅中热激90s，再迅速置于冰上3min。向热激过的离心管中加入1mL LB培养基置于37℃摇床孵育1h，将细菌均匀涂在含有硫酸卡那霉素的LB平板上进行筛选，挑取单菌落进行阳性转化子鉴定。
(4)鉴定阳性表达菌株
将含有重组质粒的DH5α置于37℃过夜培养，提取重组质粒后进行浓度测定，用热激转化的方式将其转入BL21感受态细胞中。使用扩增引物F、R来进行PCR鉴定阳性转化子，鉴定后，保存阳性转化子。鉴定结果如图2所示，第6、7泳道在2766bp处出现较亮的目的条带，鉴定为阳性转化子，进行保存。
实施例2内切唾液酸酶的表达及纯化
将经鉴定后的BL21的阳性转化子扩增培养至OD600约为0.8左右，，取样作为诱导前对照样品。然后按照1：1000加入IPTG诱导剂进行诱导，16℃过夜诱导。取诱导后的菌液作为诱导后对照样品。将诱导的菌液用PBS洗涤三次，加入含有咪唑的BindBuffer重悬，进行超声破碎，至液体澄清经超声破碎的悬液离心后获取上清及沉淀，进行SDS-PAGE电泳，判断该蛋白的表达情况。如图3A所示，第2泳道表示诱导前样品，第3泳道表示诱导后样品，第4泳道表示离心后的沉淀表达情况，第5泳道表示上清中的表达情况。可以发现该蛋白在沉淀和上清中均有表达。为了使获得的蛋白具有活性，选择对上清中的蛋白进行纯化。将菌液扩增后转接至1L LB培养基中进行培养，待OD600达到0.8左右时加入IPTG进行诱导，16℃过夜培养。将菌液用PBS洗涤3次后，使用含有20nm咪唑的Binding Buffer重悬，进行超声破碎至澄清液体。然后进行10,000g，4℃，15min离心，获取上清。使用0.45μm和0.22μm滤器过滤后将液体置于冰上，将镍柱连接到ATKA纯化仪进行蛋白纯化，设置咪唑浓度为70nm、150nm、200nm、300nm、500nm进行蛋白梯度洗脱，然后收取纯化后的蛋白，进行浓度和纯度测定。纯化前后的蛋白对比如3B所示，第2泳道为纯化前的蛋白表达情况，第3泳道为蛋白纯化后的表达情况。
实施例3内切唾液酸的抑菌作用效果
(1)内切唾液酸酶的抑菌效果
将无菌空白药敏片置于涂有不同细菌琼脂平板上，用移液枪取内切唾液酸酶(5mg/ml)5ul滴在空白药敏片上，等量的PBS作为阴性对照。待晾干后，倒置在37℃温箱中进行培养，每小时观察一次实验状况，检测8小时。该酶的作用效果如图4所示：三种K1荚膜大肠杆菌分别为宿主菌DE205B(A)，RS218(B)，CVCC1359(C)。非K1荚膜大肠杆菌DH5α(D)和以PBS作为对照滴在宿主菌DE205B(E)作为两个阴性对照。以证明酶的作用效果及酶的专一性。为了排除蛋白纯化过程中咪唑可能带来的影响，用超滤的方法将蛋白储存液置换为PBS。结果表明，内切唾液酸酶组在培养6小时左右，抑菌圈达到最大，在6-8小时抑菌圈不变(图4)。
(2)内切唾液酸酶的动态抑菌效果
将纯化后的内切唾液酸酶按照倍比稀释加入96孔板，宿主菌DE205B经PBS洗涤后调节OD600为0.5左右，按照每孔100ul加入等量的细菌。不加内切唾液酸酶的孔作为阴性对照。每孔重复3次。将96孔板放入酶标仪，设置37℃，180rpm摇动孵育。每隔15分钟检测一次OD600，持续监测540min，绘制动态的抑菌曲线如图5，可以发现，在观察时间内，当该酶的浓度在0.5mg/mL以上时，具有显著的抑制细菌生长的作用。
序列表
<110> 南京农业大学
<120> 一种针对K1荚膜大肠杆菌的噬菌体内切唾液酸酶及其应用
<160> 2
<170> SIPOSequenceListing 1.0
<210> 1
<211> 2766
<212> DNA
<213> 人工序列(Artificial Sequence)
<400> 1
atgtcaacta caattactaa tttacccgaa acatcaaaag ttaatggttc tgattacctg 60
gttttagatc aacctgataa gactgttaaa agcacagttt ccaactttct tactgacact 120
ggggtggttt tagccaccca gctaaaagat acttctggag ctaccaagta tccagaactt 180
caaatgtcac gttggagaga tgaaggtgat cctagaggat ggggagcagt aggtgacgga 240
gcaacagacg atactaatgc cataacacag cttcttgctg ctatgcctga tggatggatt 300
gttgatgggc gtaatctcac tttcaaggtt acaacactac cagatataag caagtttaaa 360
aacgctgctt ttgtttacga gcgtattgtt ggacaacccc ttacttacgt atctgagggt 420
ttctttgatg gaaatctgac aaaaattacg gatacaccat tttacaatgc ttggacgcaa 480
gataagacgt ttgtttatga caatgttata tatgcaccat ttatggctgg cgaacgtcat 540
ggtgtacaaa acctccatgt agcgtgggtt aaatcaggag atgatggaca aacttggtct 600
atgccagaat ggttaactcc aattcatcct gattataatg cctcttcagc aaacaaagtt 660
aactatcatt gtatgagtat gggtgtatgt ggtaatcgct tatatgcggt gatcgaaacc 720
cgttacttat ctaacatgcg attgaagaaa gcagaacttt ggtcacgtcc aatgccttat 780
tatagaaggc caactggagg cataacaatt agttctgggt ctactacagc gacaattgtt 840
ttagaaaagc atggtcttaa agttggagat gctgttaact tttccaattc aggtgcaact 900
ggcgtatctg gaaatatgac tgttgcatct gtaattaaca aggatacatt tactgttaca 960
ttagcgagtg ctgccacatc taatatagat aatacaggaa ctacttggca ttttggaaca 1020
cgtttctggg atagcccttg ggaaattaca gaattaccag atgttgccta ttctactaat 1080
gcagatttat gtgttacaga aacccatagt tttacagtta tagatgatga taattacact 1140
tttgctgttg gttatcacaa tggtgatgtt tccccaagaa gattaggtat tttgtatttc 1200
aataatgctt actctgaccc aagttctttt actcgtagaa caattagtca agaatatgct 1260
gacaatgcag cagaaccctg cattaaatat tatgatggaa ttttatattt aactaccagg 1320
ggtacttcaa cttctgctgc tggttctaca ttagcaatga gtaccgacct tggagaaaac 1380
tggaactact taagattccc taacaacgtt catcatacaa acttaccatt tgcaaaagtt 1440
ggtaactacc tttatatctt tggtacagaa cgttcattcg gagaatggga aggagaagaa 1500
ctagataata gatataaagg cacgtatcct cgaacgttta tgtgcaagat taatgtatct 1560
tcatggccta catctttatc cgatgttcaa tggtttaata tcactgatca gatgtatcaa 1620
gggcatattg ttaattctgc atgtggtgtt ggttcggtat gtgttaaaga tggttggtta 1680
tattatatct ttggaggcga agatttctta tctccttggt ctattgggga taatagtaaa 1740
aaattatggt acaagcatga tggtcatcca gccgatttat atagttatag actaaagatt 1800
accgaacatg attttgtatc acgtgatttc aaatatggag ctacgccaaa ccgtacattg 1860
cctgtatcta tgggtacaga tggggtaagg catgtctcag cccctgtaac ttttgataat 1920
gatgtacaag tatactcttt aacagttact ggccttgagc atgatgggac acaacaatct 1980
gccgttagaa taaaattaga tggtgattat ggggttgttg caaaaaatgt cccaataaaa 2040
aatccttcta aacagcgact aatcctatgt ggaggagaaa ctccttacgt tactgatgga 2100
tcgctattac aactatatgg ttcaaaccat acgtatccaa acagagcagt tttatatgcc 2160
ccaggaggag catataccca aaataatttc atgccgtatt tagatggaca agttgcatta 2220
ggcggtgcgt ctaacagatg gtcagaagtg tacgcatcta caggaaccat taatacttca 2280
gatggaacat taaaaactaa acctacagag attgaagata ttttactgaa agcatgggaa 2340
gatattcatg taatctctta ccaatggctt agtgctgtcg cggagaaagg agattctgcg 2400
cgtattcatt ttggtgttat agctcaagat gtaagagata ttctgattaa ttatggctta 2460
atggatgaaa atagcactga ttgtaagtat gcttttctgt gttatgatga ataccctgct 2520
atgtacgata gtgttgttac gggacaaaaa gaaatccctt tatttgatga tgaagggaat 2580
gttgtaattg atgaagaagg taatccagta acaatcgtag aagatgttgt agaaactatc 2640
gaaataattc cagcaggatc gcgatggggt atccgcgctg accaaatgtt ttttattgag 2700
atggcttatc aacgtaaaaa gttaaaagct cttgaagaaa gacttgcaac cctggaaagt 2760
aaataa 2766
<210> 2
<211> 921
<212> PRT
<213> 人工序列(Artificial Sequence)
<400> 2
Met Ser Thr Thr Ile Thr Asn Leu Pro Glu Thr Ser Lys Val Asn Asp
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Ser Asp Tyr Leu Val Leu Asp Gln Pro Asp Lys Thr Val Lys Ser Thr
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Val Ser Asn Phe Leu Thr Asp Thr Gly Val Val Leu Ala Thr Gln Leu
35 40 45
Lys Asp Thr Asp Gly Ala Thr Lys Tyr Pro Glu Leu Gln Met Ser Arg
50 55 60
Trp Arg Asp Glu Gly Asp Pro Arg Gly Trp Gly Ala Val Gly Asp Gly
65 70 75 80
Ala Thr Asp Asp Thr Asn Ala Ile Thr Gln Leu Leu Ala Ala Met Pro
85 90 95
Asp Gly Trp Ile Val Asp Gly Arg Asn Leu Thr Phe Lys Val Thr Thr
100 105 110
Leu Pro Asp Ile Ser Lys Phe Lys Asn Ala Ala Phe Val Tyr Glu Arg
115 120 125
Ile Val Gly Gln Pro Leu Thr Tyr Val Ser Ala Gly Phe Phe Asp Gly
130 135 140
Asn Leu Thr Lys Ile Thr Asp Thr Pro Phe Tyr Asn Ala Trp Thr Gln
145 150 155 160
Asp Lys Thr Phe Val Tyr Asp Asn Val Ile Tyr Ala Pro Phe Met Ala
165 170 175
Gly Glu Arg His Gly Val Gln Asn Leu His Val Ala Trp Val Lys Ser
180 185 190
Gly Asp Asp Gly Gln Thr Trp Ser Met Pro Glu Trp Leu Thr Pro Ile
195 200 205
His Pro Asp Tyr Asn Ala Ser Ser Ala Asn Lys Val Asn Tyr His Cys
210 215 220
Met Ser Met Gly Val Cys Gly Asn Arg Leu Tyr Ala Val Ile Glu Thr
225 230 235 240
Arg Tyr Leu Ser Asn Met Arg Leu Lys Lys Ala Glu Leu Trp Ser Arg
245 250 255
Pro Met Pro Tyr Tyr Arg Arg Pro Thr Gly Gly Ile Thr Ile Ser Ser
260 265 270
Gly Ser Thr Thr Ala Thr Ile Val Leu Glu Lys His Gly Leu Lys Val
275 280 285
Gly Asp Ala Val Asn Phe Ser Asn Ser Gly Ala Thr Gly Val Ser Gly
290 295 300
Asn Met Thr Val Ala Ser Val Ile Asn Lys Asp Thr Phe Thr Val Thr
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Leu Ala Ser Ala Ala Thr Ser Asn Ile Asp Asn Thr Gly Thr Thr Trp
325 330 335
His Phe Gly Thr Arg Phe Trp Asp Ser Pro Trp Glu Ile Thr Glu Leu
340 345 350
Pro Asp Val Ala Tyr Ser Thr Asn Ala Asp Leu Cys Val Thr Glu Thr
355 360 365
His Ser Phe Thr Val Ile Asp Asp Asp Asn Tyr Thr Phe Ala Val Gly
370 375 380
Tyr His Asn Gly Asp Val Ser Pro Arg Arg Leu Gly Ile Leu Tyr Phe
385 390 395 400
Asn Asn Ala Tyr Ser Asp Pro Ser Ser Phe Thr Arg Arg Thr Ile Ser
405 410 415
Gln Glu Tyr Ala Asp Asn Ala Ala Glu Pro Cys Ile Lys Tyr Tyr Asp
420 425 430
Gly Ile Leu Tyr Leu Thr Thr Arg Gly Thr Ser Thr Ser Ala Ala Gly
435 440 445
Ser Thr Leu Ala Met Ser Thr Asp Leu Gly Glu Asn Trp Asn Tyr Leu
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Arg Phe Pro Asn Asn Val His His Thr Asn Leu Pro Phe Ala Lys Val
465 470 475 480
Gly Asn Tyr Leu Tyr Ile Phe Gly Thr Glu Arg Ser Phe Gly Glu Trp
485 490 495
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500 505 510
Phe Met Cys Lys Ile Asn Val Ser Ser Trp Pro Thr Ser Leu Ser Asp
515 520 525
Val Gln Trp Phe Asn Ile Thr Asp Gln Met Tyr Gln Gly His Ile Val
530 535 540
Asn Ser Ala Cys Gly Val Gly Ser Val Cys Val Lys Asp Gly Trp Leu
545 550 555 560
Tyr Tyr Ile Phe Gly Gly Glu Asp Phe Leu Ser Pro Trp Ser Ile Gly
565 570 575
Asp Asn Ser Lys Lys Leu Trp Tyr Lys His Asp Gly His Pro Ala Asp
580 585 590
Leu Tyr Ser Tyr Arg Leu Lys Ile Thr Glu His Asp Phe Val Ser Arg
595 600 605
Asp Phe Lys Tyr Gly Ala Thr Pro Asn Arg Thr Leu Pro Val Ser Met
610 615 620
Gly Thr Asp Gly Val Arg His Val Ser Ala Pro Ile Thr Phe Asp Asn
625 630 635 640
Asp Val Gln Val Tyr Ser Leu Thr Val Thr Gly Leu Glu His Asp Gly
645 650 655
Thr Gln Gln Ser Ala Val Arg Ile Lys Leu Asp Gly Asp Tyr Gly Val
660 665 670
Val Ala Lys Asn Val Pro Ile Lys Asn Pro Ser Glu Gln Arg Leu Ile
675 680 685
Leu Cys Gly Gly Glu Thr Pro Tyr Val Thr Asp Gly Ser Leu Leu Gln
690 695 700
Leu Tyr Gly Ser Asn His Thr Tyr Pro Asn Arg Ala Val Leu Tyr Ala
705 710 715 720
Pro Gly Gly Ala Tyr Thr Gln Asn Asn Phe Met Pro Tyr Leu Asp Gly
725 730 735
Gln Val Ala Leu Gly Gly Ala Ser Asn Arg Trp Ser Glu Val Tyr Ala
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Ser Thr Gly Thr Ile Asn Thr Ser Asp Gly Thr Leu Lys Thr Lys Pro
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Thr Glu Ile Glu Asp Ile Leu Leu Lys Ala Trp Glu Asp Ile His Val
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Ile Ser Tyr Gln Trp Leu Ser Ala Val Ala Glu Lys Gly Asp Ser Ala
785 790 795 800
Arg Ile His Phe Gly Val Ile Ala Gln Asp Val Arg Asp Ile Leu Ile
805 810 815
Asn Tyr Gly Leu Met Asp Glu Asn Ser Thr Asp Cys Lys Tyr Ala Phe
820 825 830
Leu Cys Tyr Asp Glu Tyr Pro Ala Met Tyr Asp Ser Val Val Thr Gly
835 840 845
Gln Lys Glu Ile Pro Leu Phe Asp Asp Glu Gly Asn Val Val Ile Asp
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Glu Glu Gly Asn Pro Val Thr Ile Val Glu Asp Val Val Glu Thr Ile
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Glu Ile Ile Pro Ala Gly Ser Arg Trp Gly Ile Arg Ala Asp Gln Met
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Phe Phe Ile Glu Met Ala Tyr Gln Arg Lys Lys Leu Lys Ala Leu Glu
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Claims (10)
1.一种针对K1荚膜大肠杆菌具有裂解作用的内切唾液酸酶，其特征在于：氨基酸序列如Seq ID No.2所示，或者与只具有至少95％同源性的具有K1荚膜大肠杆菌裂解活性的酶。
2.权利要求1所述的内切唾液酸酶的编码基因。
3.根据权利要求2所述的编码基因，其特征在于，核苷酸序列如Seq ID No.1所示。
4.一种载体，其特征在于，该载体包含权利要求2所述的编码基因。
5.一种重组细胞，其特征在于，包含权利要求2所述的编码基因或者包含权利要求4所述的载体。
6.一种扩增权利要求2所述编码基因的引物对，其特征在于：
引物F：
5’-CAGCAAATGGGTCGCGGATCCATGTCAACTACAATTACTAATTTACCCGA-3’；
引物R：
5’-GCAAGCTTGTCGACGGAGCTCTTATTTACTTTCCAGGGTTGCAAG-3’。
7.一种包含权利要求1所述内切唾液酸酶的试剂。
8.权利要去1所述的内切唾液酸酶或权利要求7所述的试剂在细菌分类、细菌感染诊断、细菌感染防治、医疗卫生用品或食品添加剂中的应用。
9.根据权利要求8所述的应用，其特征在于，细菌为K1荚膜大肠杆菌。
10.权利要去1所述的内切唾液酸酶或权利要求7所述的试剂在在K1荚膜大肠杆菌防治和/或食源性细菌污染防治中的应用；优选的内切唾液酸酶大于或等于0.1μg/mL；更优选的为大于或等于0.5μg/mL，进一步优选的为0.5～5μg/mL。
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