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单纯疱疹病毒

(重定向自疱疹

单纯疱疹病毒(herpes simplex virus; HSV) 12 (HSV-1HSV-2),也叫人类单纯疱疹病毒 12 (HHV-1 and -2),是疱疹病毒科(Herpesviridae)中的感染人类的两类。[1] HSV-1 和 -2都是普遍存在且接触传染的。当患者产生和释放病毒时,单纯疱疹病毒就会传播。第一類型單純疱疹(HSV-1)與口腔周圍、眼角膜結膜炎及上半身感染的皮膚炎有關;第二類型單純疱疹(HSV-2)則與生殖器、新生兒疱疹及下半身感染的皮膚炎有關。[2]

 
单纯疱疹病毒
TEM 单纯疱疹病毒显微照片 .
TEM 单纯疱疹病毒显微照片 .
病毒分類
組: Group IdsDNA
科: 疱疹病毒
亞科: Alphaherpesvirinae
屬: 单纯疱疹病毒
Species

Herpes simplex virus 1 (HSV-1)
Herpes simplex virus 2 (HSV-2)


单纯疱疹病毒感染症状包括口、唇或生殖器的皮肤粘液膜上出现水泡[1] 病灶显示疱疹状的病毒典型的。在病发时,病毒会产生非常轻微或异常症状。 然而,作为亲神经的和神经侵入性的病毒,HSV-1和-2通过潜伏并避开免疫系统,驻留在人体神经细胞内。在第一次感染后,部分患者经历病毒再激活或暴发散发期。 发病时,神经细胞中的病毒变得活跃,通过神经轴突转移到皮肤,出现病毒复制和释放,导致新的疼痛。[3]

目录

传播编辑

HSV-1和-2是通过接触病毒复发期皮肤感染区而传染的。潜伏期,疱疹病毒并不传染。在病毒症状复发期,伴有可见的和典型的皮肤疼痛,传染很可能发生。无症状的复发是指病毒导致非典型的、轻微的或不明显的症状,不能确认为发病疱疹症状。非典型症状通常归咎于其他原因,如酵母菌感染[4] [5] 。HSV-1是通常幼儿期口传染的,但也可能是性传染的。 HSV-2主要是性传染的,但HSV-1生殖器感染率正不断增长[4]

尽管可能性很小,两种病毒也都可能通过分娩传染的[6] 。如果母亲在分娩时没有症状或爆开的水泡,传染的可能性极小。母亲在怀妊晚期首次得此病毒,传染的可能性极大[7]

通常第一次感染HSV时,疱疹症状会最严重,因为身体里还没有生殖器疱疹抗体来帮助你抵抗疱疹病毒。首次口腔疱疹(口腔疼痛)发作≈1%可能发展成无菌性脑膜炎[1]

微生物学编辑

病毒结构编辑

動物疱疹病毒有相同的特性。疱疹病毒的結構包含了相當大的雙絞股、線性的DNA基因組,以稱為衣殼正二十面體蛋白質外殼,衣殼又被稱為病毒包膜envelope)的脂雙層lipid bilayer)包起。

The open reading frames (ORFs) of HSV-1[8][9]
基因 蛋白質 功能/描述 基因 蛋白質 功能/描述
UL1 糖蛋白 L [1] Surface and membrane UL38 UL38; VP19C [2] Capsid assembly and DNA maturation
UL2 UL2 [3] Uracil-DNA glycosylase UL39 UL39 [4] Ribonucleotide reductase (Large subunit)
UL3 UL3 [5] unknown UL40 UL40 [6] Ribonucleotide reductase (Small subunit)
UL4 UL4 [7] unknown UL41 UL41; VHS [8] Tegument protein; Virion host shutoff[10]
UL5 UL5 [9] DNA複製 UL42 UL42 [10] DNA polymerase processivity factor
UL6 UL6 [11] Processing and packaging DNA UL43 UL43 [12] Membrane protein
UL7 UL7 [13] Virion maturation UL44 Glycoprotein C [14] Surface and membrane
UL8 UL8 [15] DNA helicase/引发酶 complex-associated protein UL45 UL45 [16] Membrane protein; C-type lectin[11]
UL9 UL9 [17] Replication origin-binding protein UL46 VP11/12 [18] Tegument proteins
UL10 Glycoprotein M [19] Surface and membrane UL47 UL47; VP13/14 [20] Tegument protein
UL11 UL11 [21] virion exit and secondary envelopment UL48 VP16 (Alpha-TIF) [22] Virion maturation; activate IEGs by interacting with the cellular transcription factors Oct-1 and HCF. Binds to the sequence 5'TAATGARAT3'.
UL12 UL12 [23] Alkaline exonuclease UL49 UL49A [24] Envelope protein
UL13 UL13 [25] Serine-threonine protein kinase UL50 UL50 [26] dUTP diphosphatase
UL14 UL14 [27] Tegument protein UL51 UL51 [28] Tegument protein
UL15 Terminase [29] Processing and packaging of DNA UL52 UL52 [30] DNA helicase/primase complex protein
UL16 UL16 [31] Tegument protein UL53 Glycoprotein K [32] Surface and membrane
UL17 UL17 [33] Processing and packaging DNA UL54 IE63; ICP27 [34] Transcriptional regulation
UL18 VP23 [35] Capsid protein UL55 UL55 [36] Unknown
UL19 VP5 [37] Major capsid protein UL56 UL56 [38] Unknown
UL20 UL20 [39] Membrane protein US1 ICP22; IE68 [40] Viral replication
UL21 UL21 [41] Tegument protein[12] US2 US2 [42] Unknown
UL22 Glycoprotein H [43] Surface and membrane US3 US3 [44] Serine/threonine-protein kinase
UL23 Thymidine kinase [45] Peripheral to DNA replication US4 Glycoprotein G [46] Surface and membrane
UL24 UL24 [47] unknown US5 Glycoprotein J [48] Surface and membrane
UL25 UL25 [49] Processing and packaging DNA US6 Glycoprotein D [50] Surface and membrane
UL26 P40; VP24; VP22A [51] Capsid protein US7 Glycoprotein I [52] Surface and membrane
UL27 Glycoprotein B [53] Surface and membrane US8 Glycoprotein E [54] Surface and membrane
UL28 ICP18.5 [55] Processing and packaging DNA US9 US9 [56] Tegument protein
UL29 UL29; ICP8 [57] Major DNA-binding protein US10 US10 [58] Capsid/Tegument protein
UL30 DNA polymerase [59] DNA replication US11 US11; Vmw21 [60] Binds DNA and RNA
UL31 UL31 [61] Nuclear matrix protein US12 ICP47; IE12 [62] Inhibits MHC class I pathway by preventing binding of antigen to TAP
UL32 UL32 [63] Envelope glycoprotein RS1 ICP4; IE175 [64] Activates gene transcription
UL33 UL33 [65] Processing and packaging DNA ICP0 ICP0; IE110; α0 [66] E3 ubiquitin ligase that activates viral gene transcription and counteracts the interferon response
UL34 UL34 [67] Inner nuclear membrane protein LRP1 LRP1 [68] Latency-related protein
UL35 VP26 [69] Capsid protein LRP2 LRP2 [70] Latency-related protein
UL36 UL36 [71] Large tegument protein RL1 RL1; ICP34.5 [72] Neurovirulence factor. Antagonizes PKR by de-phosphorylating eIF4a.
UL37 UL37 [73] Capsid assembly LAT none [74] Latency-associated transcript

进入细胞编辑

免疫编辑

复制编辑

潜伏性感染编辑

HSV-1 → 三叉神经节,颈上神经节和迷走神经

HSV-2 → 骶神经节区域

治疗和疫苗开发编辑

作用機轉:由遭受疱疹病毒感染之細胞選擇性吸收,並由細胞內病毒胸苷激酶(thymidine kinase)轉變成活性三磷酸鹽型式,併入病毒DNA鏈中,干擾病毒DNA聚合酶(DNA polymerase),終結DNA鏈,阻斷病毒複製,胸苷激酶僅存於病毒中,因此本藥對人體毒性小,可選擇性抗病毒,且藥效佳;本藥除口服、靜脈注射給藥,亦可外用塗抹,吸收後分布廣,可進入中樞神經系統作用,以原型藥物由腎臟排出。[2]

作用機轉:又稱Ara-A,有效對抗DNA病毒,是嘌呤核苷酸類似物,可抑制病毒DNA聚合酶,阻斷病毒DNA複製與合成。[2]

作用機轉:又稱IDU,構造與胸腺嘧啶類似,可嵌入病毒的DNA中,而阻斷病毒DNA合成與複製,治療指數小,限用於單純疱疹性角膜炎。[2]

和阿尔茨海默病的关系编辑

参考文献编辑

  1. 1.0 1.1 1.2 Ryan KJ, Ray CG (editors). Sherris Medical Microbiology 4th. McGraw Hill. 2004: 555–62. ISBN 0838585299. 
  2. 2.0 2.1 2.2 2.3 蔡秋帆、湯念湖、王耀宏合著. 藥理學 2014. 新文京開發有限公司. 2014. 
  3. Herpes simplex. DermNet NZ — New Zealand Dermatological Society. 2006-09-16 [2006-10-15]. 
  4. 4.0 4.1 Gupta R, Warren T, Wald A. Genital herpes. Lancet. 2007, 370 (9605): 2127–37. PMID 18156035. doi:10.1016/S0140-6736(07)61908-4. 
  5. Koelle DM, Corey L. Herpes simplex: insights on pathogenesis and possible vaccines. Annual Review of Medicine. 2008, 59: 381–95. PMID 18186706. doi:10.1146/annurev.med.59.061606.095540. 
  6. Corey L, Wald A. Maternal and Neonatal Herpes Simplex Virus Infections. New England Journal of Medicine. 2009, 361 (14): 1376–85. PMC 2780322. PMID 19797284. doi:10.1056/NEJMra0807633. 
  7. Kimberlin DW. Herpes simplex virus infections of the newborn. Semin. Perinatol. 2007, 31 (1): 19–25. PMID 17317423. doi:10.1053/j.semperi.2007.01.003. 
  8. McGeoch DJ, Rixon FJ, Davison AJ. Topics in herpesvirus genomics and evolution. Virus Res. 2006, 117 (1): 90–104. PMID 16490275. doi:10.1016/j.virusres.2006.01.002. 
  9. Search in UniProt Knowledgebase (Swiss-Prot and TrEMBL) for: HHV1
  10. Matis J, Kúdelová M. Early shutoff of host protein synthesis in cells infected with herpes simplex viruses. Acta Virol. 2001, 45 (5-6): 269–77. PMID 12083325. 
  11. Wyrwicz LS, Ginalski K, Rychlewski L. HSV-1 UL45 encodes a carbohydrate binding C-type lectin protein. Cell Cycle. 2007, 7 (2): 269–71. PMID 18256535. 
  12. Vittone V, Diefenbach E, Triffett D, Douglas MW, Cunningham AL, Diefenbach RJ. Determination of interactions between tegument proteins of herpes simplex virus type 1. J. Virol. 2005, 79 (15): 9566–71. PMC 1181608. PMID 16014918. doi:10.1128/JVI.79.15.9566-9571.2005. 

外部連結编辑