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宫颈癌是全球第四大常见的女性恶性肿瘤，人乳头瘤病毒（Human papillomavirus,HPV）是已知导致宫颈癌的主要病原体，特别是高危型HPV16和HPV18。HPV入胞及胞内转运过程尚存在争论。近期，研究人员发现除了经典的逆转复合体（Retromer），寻回复合体（Retriever）也参与HPV的胞内转运。本文主要综述了近十年HPV16进入宿主细胞的早期过程，概述了病毒粒子如何从细胞外基质通过黏膜上皮进入宿主细胞，并描述了内化后所经历的一系列复杂信号转导和胞内转运过程。HPV16病毒粒子首先与硫酸乙酰肝素蛋白聚糖（Heparan sulfate proteoglycan,HSPG）结合，经历构象变化形成入胞复合物进入内体，经逆转复合体和寻回复合体转运至高尔基体并在有丝分裂期G2/M期入核。深入理解该病毒的宿主侵染机制及其产生的免疫反应对设计针对HPV感染相关及其导致的宫颈癌等的治疗策略具有重要的意义，本综述将为HPV治疗性疫苗设计和宫颈癌的抗病毒药物开发提供基础的病毒学信息。
Abstract：Cervical cancer ranks as the fourth most prevalent malignancy among women globally, primarily attributed to infection by human papillomavirus(HPV), notably high-risk strains HPV16 and HPV18. The mechanisms governing HPV virion entry and subsequent intracellular trafficking remain a subject of ongoing research. Recent studies have identified that alongside the well-known retromer complex, the retriever complex is also implicated in the intracellular transport of HPV. This review systematically summarized the initial steps of HPV16 cell entry reported over the last decade, detailing the entry of virus particles from the extracellular matrix into host cells via the mucosal epithelium and elaborating the complex signal transduction and intracellular transport mechanisms that follow internalization. Initially, HPV16 virions bind to heparin sulfate proteoglycans(HSPG), undergo structural modifications to form endocytosis complexes for endosome entry. The complexes are subsequently transported to the Golgi apparatus by both retromer and retriever complexes, and ultimately entering the nucleus in the mitotic G2/M phase. An in-depth understanding of HPV's invasion strategies and induced immune responses is crucial for developing effective treatments against HPV infections and resultant cervical cancer. This review aims to provide essential virological insights for developing therapeutic HPV vaccines and advancing antiviral therapies for cervical cancer.
[1] Sung H, Ferlay J, Siegel RL, et al. Global cancer statistics 2020:GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries[J].CA Cancer J Clin, 2021, 71(3):209-249. DOI:10. 3322/caac. 21660.
[2] zur Hausen H. Papillomaviruses in the causation of human cancers-a brief historical account[J]. Virology,2009, 384(2):260-265. DOI:10. 1016/j.virol. 2008. 11. 046.
[3] Handler MZ, Handler NS, Majewski S, et al. Human papillomavirus vaccine trials and tribulations:clinical perspectives[J]. J Am Acad Dermatol, 2015, 73(5):743-756; quiz 757-758. DOI:10. 1016/j.jaad. 2015. 05. 040.
[4] McBride AA. Human papillomaviruses:diversity,infection and host interactions[J]. Nat Rev Microbiol,2022, 20(2):95-108. DOI:10. 1038/s41579-021-00617-5.
[5] Brianti P, De Flammineis E, Mercuri SR. Review of HPV-related diseases and cancers[J]. New Microbiol,2017, 40(2):80-85.
[6] Buck CB, Day PM, Trus BL. The papillomavirus major capsid protein L1[J]. Virology, 2013, 445(1-2):169-174. DOI:10. 1016/j. virol. 2013. 05. 038.
[7] Modis Y, Trus BL, Harrison SC. Atomic model of the papillomavirus capsid[J]. EMBO J, 2002, 21(18):4754-4762. DOI:10. 1093/emboj/cdf494.
[8] Buck CB, Cheng N, Thompson CD, et al.Arrangement of L2 within the papillomavirus capsid[J].J Virol, 2008, 82(11):5190-5197. DOI:10. 1128/JVI. 02726-07.
[9] Chen XS, Garcea RL, Goldberg I, et al. Structure of small virus-like particles assembled from the L1 protein of human papillomavirus 16[J]. Mol Cell, 2000, 5(3):557-567. DOI:10. 1016/s1097-2765(00)80449-9.
[10]Goetschius DJ, Hartmann SR, Subramanian S, et al.High resolution cryo EM analysis of HPV16 identifies minor structural protein L2 and describes capsid flexibility[J]. Sci Rep, 2021, 11(1):3498. DOI:10. 1038/s41598-021-83076-5.
[11]Wang D, Li Z, Xiao J, et al. Identification of broadgenotype HPV L2 neutralization site for pan-HPV vaccine development by a cross-neutralizing antibody[J]. PLoS One, 2015, 10(4):e0123944. DOI:10. 1371/journal. pone. 0123944.
[12]Biryukov J, Meyers C. Papillomavirus infectious pathways:a comparison of systems[J]. Viruses, 2015,7(8):4303-4325. DOI:10. 3390/v7082823.
[13]Ozbun MA, Campos SK. The long and winding road:human papillomavirus entry and subcellular trafficking[J]. Curr Opin Virol, 2021, 50:76-86. DOI:10. 1016/j. coviro. 2021. 07. 010.
[14]Biondo A, Meneses PI. The process of filopodia induction during HPV infection[J]. Viruses, 2022, 14(6):1150. DOI:10. 3390/v14061150.
[15]Knappe M, Bodevin S, Selinka HC, et al. Surfaceexposed amino acid residues of HPV16 L1 protein mediating interaction with cell surface heparan sulfate[J]. J Biol Chem, 2007, 282(38):27913-27922.DOI:10. 1074/jbc. M705127200.
[16]Dasgupta J, Bienkowska-Haba M, Ortega ME, et al.Structural basis of oligosaccharide receptor recognition by human papillomavirus[J]. J Biol Chem, 2011, 286(4):2617-2624. DOI:10. 1074/jbc. M110. 160184.
[17]Richards KF, Bienkowska-Haba M, Dasgupta J, et al.Multiple heparan sulfate binding site engagements are required for the infectious entry of human papillomavirus type 16[J]. J Virol, 2013, 87(21):11426-11437.DOI:10. 1128/JVI. 01721-13.
[18]Cerqueira C, Liu Y, Kühling L, et al. Heparin increases the infectivity of Human Papillomavirus type16 independent of cell surface proteoglycans and induces L1 epitope exposure[J]. Cell Microbiol, 2013, 15(11):1818-1836. DOI:10. 1111/cmi. 12150.
[19]Selinka HC, Florin L, Patel HD, et al. Inhibition of transfer to secondary receptors by heparan sulfatebinding drug or antibody induces noninfectious uptake of human papillomavirus[J]. J Virol, 2007, 81(20):10970-10980. DOI:10. 1128/JVI. 00998-07.
[20]Guan J, Bywaters SM, Brendle SA, et al.Cryoelectron microscopy maps of human papillomavirus16 reveal L2 densities and heparin binding site[J].Structure, 2017, 25(2):253-263. DOI:10. 1016/j.str. 2016. 12. 001.
[21]Surviladze Z, Sterkand RT, Ozbun MA. Interaction of human papillomavirus type 16 particles with heparan sulfate and syndecan-1 molecules in the keratinocyte extracellular matrix plays an active role in infection[J]. J Gen Virol, 2015, 96(8):2232-2241. DOI:10. 1099/vir. 0. 000147.
[22]吕莲秋，邓惠芳，王涵，等. SDC1在乳腺癌及其他肿瘤中作用的研究进展[J].临床医学进展，2022(12):11980-11985. DOI:10. 12677/ACM. 2022. 12121726.
[23]Aksoy P, Gottschalk EY, Meneses PI. HPV entry into cells[J]. Mutat Res Rev Mutat Res, 2017, 772:13-22. DOI:10. 1016/j. mrrev. 2016. 09. 004.
[24]Cerqueira C, Samperio Ventayol P, Vogeley C, et al.Kallikrein-8 proteolytically processes human papillomaviruses in the extracellular space to facilitate entry into host cells[J]. J Virol, 2015, 89(14):7038-7052. DOI:10. 1128/JVI. 00234-15.
[25]Broniarczyk J, Massimi P, Pim D, et al.Phosphorylation of human papillomavirus type 16 L2contributes to efficient virus infectious entry[J]. J Virol,2019, 93(13):e00128-19. DOI:10. 1128/JVI. 00128-19.
[26]Bienkowska-Haba M, Williams C, Kim SM, et al.Cyclophilins facilitate dissociation of the human papillomavirus type 16 capsid protein L1 from the L2/DNA complex following virus entry[J]. J Virol, 2012,86(18):9875-9887. DOI:10. 1128/JVI. 00980-12.
[27]Bronnimann MP, Calton CM, Chiquette SF, et al.Furin cleavage of L2 during papillomavirus infection:minimal dependence on cyclophilins[J]. J Virol, 2016,90(14):6224-6234. DOI:10. 1128/JVI. 00038-16.
[28]Becker M, Greune L, Schmidt MA, et al. Extracellular conformational changes in the capsid of human papillomaviruses contribute to asynchronous uptake into host cells[J]. J Virol, 2018, 92(11):e02106-17.DOI:10. 1128/JVI. 02106-17.
[29]Richards RM, Lowy DR, Schiller JT, et al. Cleavage of the papillomavirus minor capsid protein, L2, at a furin consensus site is necessary for infection[J]. Proc Natl Acad Sci U S A, 2006, 103(5):1522-1527.DOI:10. 1073/pnas. 0508815103.
[30]Surviladze Z, Dziduszko A, Ozbun MA. Essential roles for soluble virion-associated heparan sulfonated proteoglycans and growth factors in human papillomavirus infections[J]. PLoS Pathog, 2012, 8(2):e1002519. DOI:10. 1371/journal. ppat. 1002519.
[31]Mikuli?i?S, Finke J, Boukhallouk F, et al. ADAM17-dependent signaling is required for oncogenic human papillomavirus entry platform assembly[J]. eLife,2019, 8:e44345. DOI:10. 7554/eLife. 44345.
[32]Dziduszko A, Ozbun MA. Annexin A2 and S100A10regulate human papillomavirus type 16 entry and intracellular trafficking in human keratinocytes[J]. J Virol, 2013, 87(13):7502-7515. DOI:10. 1128/JVI. 00519-13.
[33]Woodham AW, da Silva DM, Skeate JG, et al. The S100A10 subunit of the annexin A2 heterotetramer facilitates L2-mediated human papillomavirus infection[J]. PLoS One, 2012, 7(8):e43519. DOI:10. 1371/journal. pone. 0043519.
[34]Woodham AW, Raff AB, Raff LM, et al. Inhibition of Langerhans cell maturation by human papillomavirus type 16:a novel role for the annexin A2 heterotetramer in immune suppression[J]. J Immunol, 2014, 192(10):4748-4757. DOI:10. 4049/jimmunol. 1303190.
[35]Woodham AW, Taylor JR, Jimenez AI, et al. Small molecule inhibitors of the annexin A2 heterotetramer prevent human papillomavirus type 16 infection[J]. J Antimicrob Chemother, 2015, 70(6):1686-1690.DOI:10. 1093/jac/dkv045.
[36]Mikuli?i?S, Florin L. The endocytic trafficking pathway of oncogenic papillomaviruses[J].Papillomavirus Res, 2019, 7:135-137. DOI:10. 1016/j. pvr. 2019. 03. 004.
[37]Richards KF, Mukherjee S, Bienkowska-Haba M, et al. Human papillomavirus species-specific interaction with the basement membrane-resident non-heparan sulfate receptor[J]. Viruses, 2014, 6(12):4856-4879.DOI:10. 3390/v6124856.
[38]Finke J, Mikuli?i?S, Loster AL, et al. Anatomy of a viral entry platform differentially functionalized by integrins α3 and α6[J]. Sci Rep, 2020, 10(1):5356.DOI:10. 1038/s41598-020-62202-9.
[39]Schelhaas M, Shah B, Holzer M, et al. Entry of human papillomavirus type 16 by actin-dependent, clathrin-and lipid raft-independent endocytosis[J]. PLoS Pathog,2012, 8(4):e1002657. DOI:10. 1371/journal.ppat. 1002657.
[40]Spoden G, Freitag K, Husmann M, et al. Clathrin-and caveolin-independent entry of human papillomavirus type16—involvement of tetraspanin-enriched microdomains(TEMs)[J]. PLoS One, 2008, 3(10):e3313. DOI:10. 1371/journal. pone. 0003313.
[41]Bannach C, Brinkert P, Kühling L, et al. Epidermal growth factor receptor and Abl2 kinase regulate distinct steps of human papillomavirus 16 endocytosis[J]. J Virol, 2020, 94(11):e02143-19. DOI:10. 1128/JVI. 02143-19.
[42]Gr??el L, Fast LA, Scheffer KD, et al. The CD63-syntenin-1 complex controls post-endocytic trafficking of oncogenic human papillomaviruses[J]. Sci Rep, 2016,6:32337. DOI:10. 1038/srep32337.
[43]Spoden G, Kühling L, Cordes N, et al. Human papillomavirus types 16, 18, and 31 share similar endocytic requirements for entry[J]. J Virol, 2013, 87(13):7765-7773. DOI:10. 1128/JVI. 00370-13.
[44]Wüstenhagen E, Hampe L, Boukhallouk F, et al. The cytoskeletal adaptor obscurin-like 1 interacts with the human papillomavirus 16(HPV16)capsid protein L2and is required for HPV16 endocytosis[J]. J Virol,2016, 90(23):10629-10641. DOI:10. 1128/JVI. 01222-16.
[45]Finke J, Hitschler L, Boller K, et al. HPV caught in the tetraspanin web?[J]. Med Microbiol Immunol,2020, 209(4):447-459. DOI:10. 1007/s00430-020-00683-1.
[46]Florin L, Lang T. Tetraspanin assemblies in virus infection[J]. Front Immunol, 2018, 9:1140. DOI:10. 3389/fimmu. 2018. 01140.
[47]Fast LA, Lieber D, Lang T, et al. Tetraspanins in infections by human cytomegalo-and papillomaviruses[J]. Biochem Soc Trans, 2017, 45(2):489-497.DOI:10. 1042/BST20160295.
[48]Scheffer KD, Gawlitza A, Spoden GA, et al.Tetraspanin CD151 mediates papillomavirus type 16endocytosis[J]. J Virol, 2013, 87(6):3435-3446.DOI:10. 1128/JVI. 02906-12.
[49]Fast LA, Mikuli?i?S, Fritzen A, et al. Inhibition of tetraspanin functions impairs human papillomavirus and cytomegalovirus infections[J]. Int J Mol Sci, 2018, 19(10):3007. DOI:10. 3390/ijms19103007.
[50]Mikuli?i?S, Fritzen A, Scheffer K, et al. Tetraspanin CD9 affects HPV16 infection by modulating ADAM17activity and the ERK signalling pathway[J]. Med Microbiol Immunol, 2020, 209(4):461-471. DOI:10. 1007/s00430-020-00671-5.
[51]Ishii Y, Nakahara T, Kataoka M, et al. Identification of TRAPPC8 as a host factor required for human papillomavirus cell entry[J]. PLoS One, 2013, 8(11):e80297. DOI:10. 1371/journal. pone. 0080297.
[52]Balaji K, Mooser C, Janson CM, et al. RIN1orchestrates the activation of RAB5 GTPases and ABL tyrosine kinases to determine the fate of EGFR[J]. J Cell Sci, 2012, 125(Pt 23):5887-5896. DOI:10. 1242/jcs. 113688.
[53]Taylor JR, Fernandez DJ, Thornton SM, et al.Heterotetrameric annexin A2/S100A10(A2t)is essential for oncogenic human papillomavirus trafficking and capsid disassembly, and protects virions from lysosomal degradation[J]. Sci Rep, 2018, 8(1):11642. DOI:10. 1038/s41598-018-30051-2.
[54]Bharadwaj A, Bydoun M, Holloway R, et al. Annexin A2 heterotetramer:structure and function[J]. Int J Mol Sci, 2013, 14(3):6259-6305. DOI:10. 3390/ijms14036259.
[55]Lipovsky A, Popa A, Pimienta G, et al. Genome-wide siRNA screen identifies the retromer as a cellular entry factor for human papillomavirus[J]. Proc Natl Acad Sci U S A, 2013, 110(18):7452-7457. DOI:10. 1073/pnas. 1302164110.
[56]Müller KH, Spoden GA, Scheffer KD, et al. Inhibition by cellular vacuolar ATPase impairs human papillomavirus uncoating and infection[J]. Antimicrob Agents Chemother, 2014, 58(5):2905-2911. DOI:10. 1128/AAC. 02284-13.
[57]DiGiuseppe S, Keiffer TR, Bienkowska-Haba M, et al. Topography of the human papillomavirus minor capsid protein L2 during vesicular trafficking of infectious entry[J]. J Virol, 2015, 89(20):10442-10452. DOI:10. 1128/JVI. 01588-15.
[58]Bugnon Valdano M, Massimi P, Broniarczyk J, et al.Human Papillomavirus infection requires the CCT Chaperonin Complex[J]. J Virol, 2021, 95(11):e01943-20. DOI:10. 1128/JVI. 01943-20.
[59]Broniarczyk J, Bergant M, Go?dzicka-Józefiak A, et al.Human papillomavirus infection requires the TSG101component of the ESCRT machinery[J]. Virology,2014, 460-461:83-90. DOI:10. 1016/j.virol. 2014. 05. 005.
[60]Broniarczyk J, Pim D, Massimi P, et al. The VPS4component of the ESCRT machinery plays an essential role in HPV infectious entry and capsid disassembly[J].Sci Rep, 2017, 7:45159. DOI:10. 1038/srep45159.
[61]Bergant M, Peternel?，Pim D, et al. Characterizing the spatio-temporal role of sorting nexin 17 in human papillomavirus trafficking[J]. J Gen Virol, 2017, 98(4):715-725. DOI:10. 1099/jgv. 0. 000734.
[62]Bergant Maru?i?M, Ozbun MA, Campos SK, et al.Human papillomavirus L2 facilitates viral escape from late endosomes via sorting nexin 17[J]. Traffic, 2012,13(3):455-467. DOI:10. 1111/j. 1600-0854. 2011. 01320. x.
[63]McNally KE, Faulkner R, Steinberg F, et al. Retriever is a multiprotein complex for retromer-independent endosomal cargo recycling[J]. Nat Cell Biol, 2017, 19(10):1214-1225. DOI:10. 1038/ncb3610.
[64]Uhlorn BL, Jackson R, Li S, et al. Vesicular trafficking permits evasion of cGAS/STING surveillance during initial human papillomavirus infection[J]. PLoS Pathog, 2020, 16(11):e1009028. DOI:10. 1371/journal. ppat. 1009028.
[65]Xie J, Zhang P, Crite M, et al. Papillomaviruses go retro[J]. Pathogens, 2020, 9(4):E267. DOI:10. 3390/pathogens9040267.
[66]Popa A, Zhang W, Harrison MS, et al. Direct binding of retromer to human papillomavirus type 16 minor capsid protein L2 mediates endosome exit during viral infection[J]. PLoS Pathog, 2015, 11(2):e1004699.DOI:10. 1371/journal. ppat. 1004699.
[67]Pim D, Broniarczyk J, Siddiqa A, et al. Human papillomavirus 16 L2 recruits both retromer and retriever complexes during retrograde trafficking of the viral genome to the cell nucleus[J]. J Virol, 2021, 95(3):e02068-20. DOI:10. 1128/JVI. 02068-20.
[68]Zhang P, Moreno R, Lambert PF, et al. Cellpenetrating peptide inhibits retromer-mediated human papillomavirus trafficking during virus entry[J]. Proc Natl Acad Sci U S A, 2020, 117(11):6121-6128.DOI:10. 1073/pnas. 1917748117.
[69]Zhang P, Monteiro da Silva G, Deatherage C, et al.Cell-penetrating peptide mediates intracellular membrane passage of human papillomavirus L2 protein to trigger retrograde trafficking[J]. Cell, 2018, 174(6):1465-1476. e13. DOI:10. 1016/j. cell. 2018. 07. 031.
[70]Carosi JM, Denton D, Kumar S, et al. Receptor recycling by retromer[J]. Mol Cell Biol, 2023, 43(7):317-334. DOI:10. 1080/10985549. 2023. 2222053.
[71]Harwood MC, Dupzyk AJ, Inoue T, et al. p120catenin recruits HPV to γ-secretase to promote virus infection[J]. PLoS Pathog, 2020, 16(10):e1008946.DOI:10. 1371/journal. ppat. 1008946.
[72]Inoue T, Zhang P, Zhang W, et al. γ-Secretase promotes membrane insertion of the human papillomavirus L2 capsid protein during virus infection[J]. J Cell Biol, 2018, 217(10):3545-3559. DOI:10. 1083/jcb. 201804171.
[73]Zhang W, Kazakov T, Popa A, et al. Vesicular trafficking of incoming human papillomavirus 16 to the Golgi apparatus and endoplasmic reticulum requires γ-secretase activity[J]. mBio, 2014, 5(5):e01777-14.DOI:10. 1128/mBio. 01777-14.
[74]Karanam B, Peng S, Li T, et al. Papillomavirus infection requires gamma secretase[J]. J Virol, 2010,84(20):10661-10670. DOI:10. 1128/JVI. 01081-10.
[75]Young JM, Zine El Abidine A, Gómez-Martinez RA,et al. The known and potential intersections of rabGTPases in human papillomavirus infections[J]. Front Cell Dev Biol, 2019, 7:139. DOI:10. 3389/fcell. 2019. 00139.
[76]Siddiqa A, Massimi P, Pim D, et al. Human papillomavirus 16 infection induces VAP-dependent endosomal tubulation[J]. J Virol, 2018, 92(6):e01514-17. DOI:10. 1128/JVI. 01514-17.
[77]Xie J, Heim EN, Crite M, et al. TBC1D5-catalyzed cycling of Rab7 is required for retromer-mediated human papillomavirus trafficking during virus entry[J]. Cell Rep, 2020, 31(10):107750. DOI:10. 1016/j.celrep. 2020. 107750.
[78]Day PM, Thompson CD, Schowalter RM, et al.Identification of a role for the trans-Golgi network in human papillomavirus 16 pseudovirus infection[J]. J Virol, 2013, 87(7):3862-3870. DOI:10. 1128/JVI. 03222-12.
[79]Li S, Bronnimann MP, Williams SJ, et al. Glutathione contributes to efficient post-Golgi trafficking of incoming HPV16 genome[J]. PLoS One, 2019, 14(11):e0225496. DOI:10. 1371/journal. pone. 0225496.
[80]Gottschalk EY, Meneses PI. A dual role for the nonreceptor tyrosine kinase Pyk2 during the intracellular trafficking of human papillomavirus 16[J]. J Virol,2015, 89(17):9103-9114. DOI:10. 1128/JVI. 01183-15.
[81]DiGiuseppe S, Luszczek W, Keiffer TR, et al.Incoming human papillomavirus type 16 genome resides in a vesicular compartment throughout mitosis[J]. Proc Natl Acad Sci U S A, 2016, 113(22):6289-6294.DOI:10. 1073/pnas. 1600638113.
[82]Calton CM, Bronnimann MP, Manson AR, et al.Translocation of the papillomavirus L2/vDNA complex across the limiting membrane requires the onset of mitosis[J]. PLoS Pathog, 2017, 13(5):e1006200.DOI:10. 1371/journal. ppat. 1006200.
[83]Pyeon D, Pearce SM, Lank SM, et al. Establishment of human papillomavirus infection requires cell cycle progression[J]. PLoS Pathog, 2009, 5(2):e1000318.DOI:10. 1371/journal. ppat. 1000318.
[84]Florin L, Becker KA, Lambert C, et al. Identification of a dynein interacting domain in the papillomavirus minor capsid protein l2[J]. J Virol, 2006, 80(13):6691-6696. DOI:10. 1128/JVI. 00057-06.
[85]Schneider MA, Spoden GA, Florin L, et al.Identification of the dynein light chains required for human papillomavirus infection[J]. Cell Microbiol,2011, 13(1):32-46. DOI:10. 1111/j. 1462-5822. 2010. 01515. x.
[86]Florin L, Becker KA, Sapp C, et al. Nuclear translocation of papillomavirus minor capsid protein L2requires Hsc70[J]. J Virol, 2004, 78(11):5546-5553.DOI:10. 1128/JVI. 78. 11. 5546-5553. 2004.
[87]Aydin I, Weber S, Snijder B, et al. Large scale RNAi reveals the requirement of nuclear envelope breakdown for nuclear import of human papillomaviruses[J]. PLoS Pathog, 2014, 10(5):e1004162. DOI:10. 1371/journal. ppat. 1004162.
[88]Aydin I, Villalonga-Planells R, Greune L, et al. A central region in the minor capsid protein of papillomaviruses facilitates viral genome tethering and membrane penetration for mitotic nuclear entry[J].PLoS Pathog, 2017, 13(5):e1006308. DOI:10. 1371/journal. ppat. 1006308.
[89]Lai KY, Rizzato M, Aydin I, et al. A Ran-binding protein facilitates nuclear import of human papillomavirus type 16[J]. PLoS Pathog, 2021, 17(5):e1009580. DOI:10. 1371/journal. ppat. 1009580.
[90]Bund T, Spoden GA, Koynov K, et al. An L2 SUMO interacting motif is important for PML localization and infection of human papillomavirus type 16[J]. Cell Microbiol, 2014, 16(8):1179-1200. DOI:10. 1111/cmi. 12271.
[91]Guion L, Bienkowska-Haba M, DiGiuseppe S, et al.PML nuclear body-residing proteins sequentially associate with HPV genome after infectious nuclear delivery[J]. PLoS Pathog, 2019, 15(2):e1007590.DOI:10. 1371/journal. ppat. 1007590.
[92]Marusic MB, Mencin N, Licen, et al. Modification of human papillomavirus minor capsid protein L2 by sumoylation[J]. J Virol, 2010, 84(21):11585-11589.DOI:10. 1128/JVI. 01269-10.
[93]Day PM, Baker CC, Lowy DR, et al. Establishment of papillomavirus infection is enhanced by promyelocytic leukemia protein(PML)expression[J]. Proc Natl Acad Sci U S A, 2004, 101(39):14252-14257. DOI:10. 1073/pnas. 0404229101.
[94]Bienkowska-Haba M, Luszczek W, Keiffer TR, et al.Incoming human papillomavirus 16 genome is lost in PML protein-deficient HaCaT keratinocytes[J]. Cell Microbiol, 2017, 19(5). DOI:10. 1111/cmi. 12708.
[95]Stepp WH, Meyers JM, McBride AA. Sp100 provides intrinsic immunity against human papillomavirus infection[J]. mBio, 2013, 4(6):e00845-13. DOI:10. 1128/mBio. 00845-13.
[96]Schneider MA, Scheffer KD, Bund T, et al. The transcription factors TBX2 and TBX3 interact with human papillomavirus 16(HPV16)L2 and repress the long control region of HPVs[J]. J Virol, 2013, 87(8):4461-4474. DOI:10. 1128/JVI. 01803-12.
[97]Wüstenhagen E, Boukhallouk F, Negwer I, et al. The Myb-related protein MYPOP is a novel intrinsic host restriction factor of oncogenic human papillomaviruses[J]. Oncogene, 2018, 37(48):6275-6284. DOI:10. 1038/s41388-018-0398-6.
[98]Sch?fer G, Graham LM, Lang DM, et al. Vimentin modulates infectious internalization of human papillomavirus 16 pseudovirions[J]. J Virol, 2017, 91(16):e00307-17. DOI:10. 1128/JVI. 00307-17.
[99]Carse S, Lang D, Katz AA, et al. Exogenous vimentin supplementation transiently affects early steps during HPV16 pseudovirus infection[J]. Viruses, 2021, 13(12):2471. DOI:10. 3390/v13122471.
[100]Wiens ME, Smith JG. Alpha-defensin HD5 inhibits furin cleavage of human papillomavirus 16 L2 to block infection[J]. J Virol, 2015, 89(5):2866-2874. DOI:10. 1128/JVI. 02901-14.
[101]Wiens ME, Smith JG. α-defensin HD5 inhibits human papillomavirus 16 infection via capsid stabilization and redirection to the lysosome[J]. mBio, 2017, 8(1):e02304-16. DOI:10. 1128/mBio. 02304-16.
[102]Wang S, Lu Z, Wang S, et al. The inhibitory effects and mechanisms of polymannuroguluronate sulfate against human papillomavirus infection in vitro and in vivo[J]. Carbohydr Polym, 2020, 241:116365. DOI:10. 1016/j. carbpol. 2020. 116365.
[103] Griffin LM, Cicchini L, Pyeon D. Human papillomavirus infection is inhibited by host autophagy in primary human keratinocytes[J]. Virology, 2013, 437(1):12-19. DOI:10. 1016/j. virol. 2012. 12. 004.
[104] Ishii Y. Electron microscopic visualization of autophagosomes induced by infection of human papillomavirus pseudovirions[J]. Biochem Biophys Res Commun, 2013, 433(4):385-389. DOI:10. 1016/j.bbrc. 2013. 02. 130.
[105]Besemer AS, Maus J, Ax MDA, et al. Receptormediated endocytosis 8(RME-8)/DNAJC13 is a novel positive modulator of autophagy and stabilizes cellular protein homeostasis[J]. Cell Mol Life Sci, 2021, 78(2):645-660. DOI:10. 1007/s00018-020-03521-y.
[106]Surviladze Z, Sterk RT, DeHaro SA, et al. Cellular entry of human papillomavirus type 16 involves activation of the phosphatidylinositol 3-kinase/Akt/mTOR pathway and inhibition of autophagy[J]. J Virol, 2013, 87(5):2508-2517. DOI:10. 1128/JVI. 02319-12.
[107]Day PM, Thompson CD, Lowy DR, et al. Interferon gamma prevents infectious entry of human papillomavirus 16 via an L2-dependent mechanism[J]. J Virol, 2017, 91(10):e00168-17. DOI:10. 1128/JVI. 00168-17.
[108]Lipovsky A, Erden A, Kanaya E, et al. The cellular endosomal protein stannin inhibits intracellular trafficking of human papillomavirus during virus entry[J]. J Gen Virol, 2017, 98(11):2821-2836. DOI:10. 1099/jgv. 0. 000954.
[109] Calton CM, Schlegel AM, Chapman JA, et al.Human papillomavirus type 16 does not require cathepsin L or B for infection[J]. J Gen Virol, 2013, 94(Pt 8):1865-1869. DOI:10. 1099/vir. 0. 053694-0.
基本信息:
DOI：10.13242/j.cnki.bingduxuebao.004649
中图分类号:R737.33
引用信息:
[1]曹琳,池鑫,韩峰,等.人乳头瘤病毒16型感染上皮细胞过程的研究进展[J].病毒学报,2025,41(01):232-244.DOI:10.13242/j.cnki.bingduxuebao.004649.
基金信息:
国家自然科学基金（项目号82271873）,题目：以T=7人乳头瘤类病毒颗粒为基座可化学缀合多种对称性寡聚抗原的通用纳米颗粒疫苗分子; 厦门市自然科学基金（项目号3502Z20227165）,题目：基于组学的大肠杆菌可溶性外源表达的调控机制研究~~
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2025-01-03
2025-01-03
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