Potential roles of protein disulphide isomerase in viral infections

Acta Virologica

Volumn 57, Issue 3, 2013, Pages 293-304

  Diwaker, D ^a   Mishra, K P ^a   Ganju, L ^a  

^a DEFENCE INSTITUTE OF PHYSIOLOGY AND ALLIED SCIENCES   (India)

Author keywords

Chaperone; Protein disulphide isomerase; Virus

Indexed keywords

CHAPERONE; PROTEIN DISULFIDE ISOMERASE;

ACTIN FILAMENT; AFRICAN SWINE FEVER VIRUS; ANIMAL VIRUS; ARTICLE; CATALYSIS; CELL SHAPE; DISEASE ASSOCIATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; FLAVIVIRUS INFECTION; HERPES VIRUS INFECTION; NONHUMAN; OXIDATION REDUCTION POTENTIAL; PAPILLOMAVIRUS INFECTION; PATHOGENESIS; POLYOMAVIRUS INFECTION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; RETROVIRUS INFECTION; SIGNAL TRANSDUCTION; VIRUS CELL INTERACTION; VIRUS ENTRY; VIRUS INFECTION; ANIMAL; ENZYMOLOGY; GENETICS; HUMAN; METABOLISM; VIRAL PHENOMENA AND FUNCTIONS; VIROLOGY; VIRUS DISEASES;

ANIMALS; HUMANS; PROTEIN DISULFIDE-ISOMERASES; VIRUS DISEASES; VIRUS PHYSIOLOGICAL PHENOMENA;

EID: 84891621364     PISSN: 0001723X     EISSN: None     Source Type: Journal    
DOI: 10.4149/av_2013_03_293     Document Type: Article

References (85)

1. Akagi S, Yamamoto A, Yoshimori T, Masaki R, Ogawa R, Tashiro Y (1988): Distribution of protein disulfide isomerase in rat hepatocytes. J. Histochem. Cytochem. 36,1533-1542. http://dx.doi.org/10.1177/36.12.3192937
2. Alanen HI, Salo KEH, Pekkala M, Siekkinen HM, Pirneskoski A, Ruddock LW (2003): Defining the domain boundaries of the human protein disulfide isomerases. Antioxid. Redox Signal. 5, 367-374. http://dx.doi.org/10.1089/152308603768295096
3. Alejo A, Andrés G, Vi-uela E, Salas ML (1999): The African swine fever virus prenyltransferase is an integral membrane trans-geranylgeranyl-diphosphate synthase. J. Biol. Chem. 274, 18033-18039. http://dx.doi.org/10.1074/jbc.274.25.18033
4. Anelli T, Alessio M, Bachi A, Bergamelli L, Bertoli G, Camerini S, Mezghrani A, Ruffato E, Simmen T, Sitia R (2003): Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44. EMBO J. 22, 5015-5022. http://dx.doi.org/10.1093/emboj/cdg491
5. Anelli T, Alessio M, Mezghrani A, Simmen T, Talamo F, Bachi A, Sitia R (2002): ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family. EMBO J. 21, 835-844. http://dx.doi.org/10.1093/emboj/21.4.835
6. Bahbouhi B, Landay A, Al-Harthi L (2004): Dynamics of cytokine expression in HIV productively infected primary CD4+ T cells. Blood 103, 4581-4587. http://dx.doi.org/10.1182/blood-2003-12-4172
7. Bennett TA, Edwards BS, Sklar LA, Rogelj S (2000): Sulfhydryl regulation of l-selectin shedding: Phenylarsine oxide promotes activation-independent l-selectin shedding from leukocytes. J. Immunol. 164, 4120-4129.
8. Bi, S, Earl, L, Jacobs, L, Baum, LG (2008): Structural features of galectin-9 and galectin-1 that determine distinct T cell death pathways. J. Biol. Chem. 283, 12248-12258. http://dx.doi.org/10.1074/jbc.M800523200
9. Bi S, Hong PW, Lee B, Baum LG (2011): Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry. Proc. Natl. Acad. Sci. USA 108, 10650-10655. http://dx.doi.org/10.1073/pnas.1017954108
10. Cabibbo A, Pagani M, Fabbri M, Rocchi M, Farmery MR, Bulleid NJ, Sitia R (2000): ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum. J. Biol. Chem. 275, 4827-4833. http://dx.doi.org/10.1074/jbc.275.7.4827
11. Campos SK, Chapman J, Deymier MJ, Bronnimann M.P, Ozbun MA (2012): Opposing effects of bacitracin on human papillomavirus type 16 infection: enhancement of binding and entry and inhibition of endosomal penetration. J. Virol. 86, 4169-4181. http://dx.doi.org/10.1128/JVI.05493-11
12. Chen MC, Lin CF, Lei HY, Lin SC, Liu HS, Yeh TM, Anderson R, Lin YS (2009): Deletion of the C-terminal region of dengue virus nonstructural protein 1 (NS1) abolishes anti-NS1-mediated platelet dysfunction and bleeding tendency. J. Immunol. 183, 1797-1803. http://dx.doi.org/10.4049/jimmunol.0800672
13. Cheng HJ, Lin CF, Lei HY, Liu HS, Yeh TM, Luo YH, Lin YS (2009): Proteomic analysis of endothelial cell autoantigens recognized by anti-dengue virus nonstructural protein 1 antibodies. Exp. Biol. Med. 234, 63-73. http://dx.doi.org/10.3181/0805-RM-147
14. Choo QL, Richman KH, Han JH, Berger K, Lee C, Dong C, Gallegos C, Coit D, Medina-Selby R, Barr PJ (1991): Genetic organization and diversity of the hepatitis C virus. Proc. Natl. Acad. Sci. 88, 2451-2455. http://dx.doi.org/10.1073/pnas.88.6.2451
15. Chua JJE, Ng MML, Chow VTK (2004): The non-structural 3 (NS3) protein of Dengue virus type 2 interacts with human nuclear receptor binding protein and is associated with alterations in membrane structure. Virus Res. 102, 151-163. http://dx.doi.org/10.1016/j.virusres.2004.01.025
16. Depuydt M, Messens J, Collet J-F (2011): How proteins form disulfide bonds. Antioxid. Redox Signal. 15, 49-66. http://dx.doi.org/10.1089/ars.2010.3575
17. Desjardins M (2003): ER-mediated phagocytosis: a new membrane for new functions. Nature reviews. Immunology 3, 280-291. http://dx.doi.org/10.1038/nri1053
18. Ellgaard L, Ruddock LW (2005): The human protein disulphide isomerase family: substrate interactions and functional properties. EMBO Rep. 6, 28-32. http://dx.doi.org/10.1038/sj.embor.7400311
19. Elliott JG, Oliver JD, High S (1997): The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral mem brane proteins. J. Biol. Chem. 272, 13849-13855. http://dx.doi.org/10.1074/jbc.272.21.13849
20. Essex DW, Li M, Miller A, Feinman RD (2001): Protein disulfide isomerase and sulfhydryl-dependent pathways in platelet activation. Biochemistry. 40, 6070-6075. http://dx.doi.org/10.1021/bi002454e
21. Fenouillet E, Barbouche R, Courageot J, Miquelis R (2001): The catalytic activity of protein disulfide isomerase is involved in human immunodeficiency virus envelope-mediated membrane fusion after CD4 cell binding. J. Infect. Dis. 183, 744-752. http://dx.doi.org/10.1086/318823
22. Fenouillet E, Barbouche R, Jones IM (2007): Cell entry by enveloped viruses: redox considerations for HIV and SARS-coronavirus. Antioxid. Redox Signal. 9, 1009-1034. http://dx.doi.org/10.1089/ars.2007.1639
23. Freedman RB, Gane PJ, Hawkins HC, Hlodan R, McLaughlin SH, Parry JW (1998): Experimental and theoretical analyses of the domain architecture of mammalian protein disulphide-isomerase. Biol. Chem. 379, 321-328. http://dx.doi.org/10.1515/bchm.1998.379.3.321
24. Gallina A, Hanley TM, Mandel R, Trahey M, Broder CC, Viglianti GA, Ryser HJ-P (2002): Inhibitors of protein-disulfide isomerase prevent cleavage of disulfide bonds in receptor-bound gp120 and prevent HIV-1 entry. J. Biol. Chem. 277, 50579-50588. http://dx.doi.org/10.1074/jbc.M204547200
25. Garner OB, Baum LG (2008): Galectin-glycan lattices regulate cell-surface glycoprotein organization and signalling. Biochem. Soc. T. 36, 1472-1477. http://dx.doi.org/10.1042/BST0361472
26. Gilbert J, Ou W, Silver J, Benjamin T (2006): Downregulation of protein disulfide isomerase inhibits infection by the mouse polyomavirus. J. Virol. 80, 10868-10970. http://dx.doi.org/10.1128/JVI.01117-06
27. Goodwin EC, Lipovsky A, Inoue T, Magaldi TG, Edwards APB, Van Goor KEY, Paton AW, Paton JC, Atwood WJ, Tsai B, DiMaio D (2011): BiP and multiple DNAJ molecular chaperones in the endoplasmic reticulum are required for efficient simian virus 40 infection. mBio 2(3), e00101-11.
28. Hatahet F, Ruddock LW (2009): Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation. Antioxid. Redox Signal. 11, 2807-2850. http://dx.doi.org/10.1089/ars.2009.2466
29. Horváth I, Multhoff G, Sonnleitner A, Vígh L (2008): Membrane-associated stress proteins: more than simply chaperones. Biochim. Biophys. Acta 1778, 1653-1664. http://dx.doi.org/10.1016/j.bbamem.2008.02.012
30. Hwang C, Sinskey AJ, Lodish HF (1992): Oxidized redox state of glutathione in the endoplasmic reticulum. Science (New York, N.Y.) 257, 1496-1502. http://dx.doi.org/10.1126/science.1523409
31. Imaizumi T, Kumagai M, Sasaki N, Kurotaki H, Mori F, Seki M, Nishi N, Fujimoto K, Tanji K, Shibata T, Tamo W, Matsumiya T, Yoshida H, Cui X-F, Takanashi S, Hanada K, Okumura K, Yagihashi S, Wakabayashi K, Nakamura T, Hirashima M, Satoh K (2002): Interferon-gamma stimulates the expression of galectin-9 in cultured human endothelial cells. J. Leukocyte Biol. 72, 486-491.
32. Inoue T, Tsai B (2011): A large and intact viral particle penetrates the endoplasmic reticulum membrane to reach the cytosol. PLoS Pathog. 7(5), e1002037. http://dx.doi.org/10.1371/journal.ppat.1002037
33. Jansen G, Määttänen P, Denisov AY, Scarffe L, Schade B, Balghi H, Dejgaard K, Chen LY, Muller WJ, Gehring K, Thomas DY (2012): An interaction map of ER chaperones and foldases. Mol. Cell. Proteomics 11 (9), 710-723. http://dx.doi.org/10.1074/mcp.M111.016550
34. Jessop CE, Chakravarthi S, Garbi N, Hammerling GJ, Lovell S, Bulleid NJ (2007): ERp57 is essential for efficient folding of glycoproteins sharing common structural domains. EMBO J. 26, 28-40. http://dx.doi.org/10.1038/sj.emboj.7601505
35. Jiang M, Abend JR, Tsai B, Imperiale MJ (2009): Early events during BK virus entry and disassembly. J. Virol. 83,1350-1358. http://dx.doi.org/10.1128/JVI.02169-08
36. Kim Y, Kang K, Kim I, Lee YJ, Oh C, Ryoo J, Jeong E, Ahn K (2009): Molecular mechanisms of MHC class I-antigen processing: redox considerations. Antioxid. Redox Signal. 11, 907-936. http://dx.doi.org/10.1089/ars.2008.2316
37. Klappa P, Ruddock LW, Darby NJ, Freedman RB (1998): The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins. EMBO J. 17, 927-935. http://dx.doi.org/10.1093/emboj/17.4.927
38. Kozlov G, Maattanen P, Schrag JD, Hura GL, Gabrielli L, Cygler M, Thomas DY, Gehring K (2009): Structure of the noncatalytic domains and global fold of the protein disulfide isomerase ERp72. Structure 17, 651-659. http://dx.doi.org/10.1016/j.str.2009.02.016
39. Kozlov G, Maattanen P, Schrag JD, Pollock S, Cygler M, Nagar B, Thomas DY, Gehring K (2006): Crystal structure of the bb' domains of the protein disulfide isomerase ERp57. Structure 14, 1331-1339. http://dx.doi.org/10.1016/j.str.2006.06.019
40. Kozlov G, Määttänen P, Thomas DY, Gehring K (2010): A structural overview of the PDI family of proteins. FEBS J. 277, 3924-3936. http://dx.doi.org/10.1111/j.1742-4658.2010.07793.x
41. Krey T, Thiel HJ, Rümenapf T (2005): Acid-resistant bovine pestivirus requires activation for pH-triggered fusion during entry. J. Virol. 79, 4191-4200. http://dx.doi.org/10.1128/JVI.79.7.4191-4200.2005
42. Lee S, Park B, Kang K, Ahn K (2009): Redox-regulated export of the major histocompatibility complex class I-peptide complexes from the endoplasmic reticulum Mol. Biol. Cell 20, 3285-3294. http://dx.doi.org/10.1091/mbc.E09-03-0238
43. Lee S-O, Cho K, Cho S, Kim I, Oh C, Ahn K (2010): Protein disulphide isomerase is required for signal peptide peptidase-mediated protein degradation. EMBO J. 29, 363-375. http://dx.doi.org/10.1038/emboj.2009.359
44. Liu F-T, Rabinovich G (2010): Galectins: regulators of acute and chronic inflammation. Ann. NY. Acad. Sci. USA 1183, 158-182. http://dx.doi.org/10.1111/j.1749-6632.2009.05131.x
45. Loesing J-B, Fiore SD, Ritter K, Fischer R, Kleines M (2009): Epstein-Barr virus BDLF2-BMRF2 complex affects cellular morphology. J. Gen. Virol. 90, 1440-1449. http://dx.doi.org/10.1099/vir.0.009571-0
46. Macer DR, Koch GL (1988): Identification of a set of calcium-binding proteins in reticuloplasm, the luminal content of the endoplasmic reticulum. J. Cell Sci. 91, 61-70.
47. Markovic I, Stantchev TS, Fields KH, Tiffany LJ, Tomiç M, Weiss CD, Broder CC, Strebel K, Clouse KA (2004): Thiol/disulfide exchange is a prerequisite for CXCR4-tropic HIV-1 envelope-mediated T-cell fusion during viral entry. Blood 103, 1586-1594. http://dx.doi.org/10.1182/blood-2003-05-1390
48. Mezghrani A, Fassio A, Benham A, Simmen T, Braakman I, Sitia R (2001): Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO J. 20, 6288-6296. http://dx.doi.org/10.1093/emboj/20.22.6288
49. Mishra KP, Shweta, Diwaker D, Ganju L (2012): Dengue virus infection induces upregulation of hn RNP-H and PDIA3 for its multiplication in the host cell. Virus Res. 163, 573-579. http://dx.doi.org/10.1016/j.virusres.2011.12.010
50. Ndubuisi MI, Guo GG, Fried VA, Etlinger JD, Sehgal PB (1999): Cellular physiology of STAT3: Where's the cytoplasmic monomer? J. Biol. Chem. 274, 25499-25509. http://dx.doi.org/10.1074/jbc.274.36.25499
51. Nigam SK, Goldberg AL, Ho S, Rohde MF, Bush KT, Sherman MY (1994): A set of endoplasmic reticulum proteins possessing properties of molecular chaperones includes Ca(2{thorn})-binding proteins and members of the thioredoxin superfamily. J. Biol. Chem. 269, 1744-1749.
52. Oliver JD, Roderick HL, Llewellyn DH, High S (1999): ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin. Mol. Biol. Cell. 10, 2573-2582. http://dx.doi.org/10.1091/mbc.10.8.2573
53. Padwad YS, Mishra KP, Jain M, Chanda S, Ganju L (2010): Dengue virus infection activates cellular chaperone Hsp70 in THP-1 cells: downregulation of Hsp70 by siRNA revealed decreased viral replication. Viral Immunol. 23, 557-565. http://dx.doi.org/10.1089/vim.2010.0052
54. Padwad YS, Mishra KP, Jain M, Chanda S, Karan D, Ganju L (2009): RNA interference mediated silencing of Hsp60 gene in human monocytic myeloma cell line U937 revealed decreased dengue virus multiplication. Immunobiology 214, 422-429. http://dx.doi.org/10.1016/j.imbio.2008.11.010
55. Papandréou M-J, Barbouche R, Guieu R, Rivera S, Fantini J, Khrestchatisky M, Jones IM, Fenouillet E, (2010): Mapping of domains on HIV envelope protein mediating association with calnexin and protein-disulfide isomerase. J. Biol. Chem. 285, 13788-13796. http://dx.doi.org/10.1074/jbc.M109.066670
56. Park B, Lee S, Kim E, Cho K, Riddell SR, Cho S, Ahn K (2006): Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing. Cell 127, 369-382. http://dx.doi.org/10.1016/j.cell.2006.08.041
57. Pihlajaniemi T, Helaakoski T, Tasanen K, Myllylä R, Huhtala M.-L, Koivu J, Kivirikko KI (1987): Molecular cloning of the subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. EMBO J. 6, 643-649.
58. Powers ET, Balch WE (2011): Protein folding: Protection from the outside. Nature 471, 42-43. http://dx.doi.org/10.1038/471042a
59. Quemeneur E, Guthapfel R, Gueguen P (1994): A major phosphoprotein of the endoplasmic reticulum is protein disulfide isomerase. J. Biol. Chem. 269, 5485-5488.
60. Rainey-Barger EK, Magnuson B, Tsai B (2007): A chaperone-activated nonenveloped virus perforates the physiologically relevant endoplasmic reticulum membrane. J. Virol. 81, 12996-13004. http://dx.doi.org/10.1128/JVI.01037-07
61. Reed, KE, Rice, CM (2000): Overview of hepatitis C virus genome structure, polyprotein processing, and protein properties. Curr. Top. Microbiol. Immunol. 242, 55-84. http://dx.doi.org/10.1007/978-3-642-59605-6_4
62. Rigobello MP, Donella-Deana A, Cesaro L, Bindoli A (2001): Distribution of protein disulphide isomerase in rat liver mitochondria. Biochem. J. 356, 567-570. http://dx.doi.org/10.1042/0264-6021:3560567
63. Sato Y, Nadanaka S, Okada T, Okawa K, Mori K (2011): Luminal domain of ATF6 alone is sufficient for sensing endoplasmic reticulum stress and subsequent transport to the Golgi apparatus. Cell Struct. Funct. 36, 35-47. http://dx.doi.org/10.1247/csf.10010
64. Schelhaas M, Malmström J, Pelkmans L, Haugstetter J, Ellgaard L, Grünewald K, Helenius A (2007): Simian Virus 40 depends on ER protein folding and quality control factors for entry into host cells. Cell 131, 516-529. http://dx.doi.org/10.1016/j.cell.2007.09.038
65. Sehgal PB (2003): Plasma membrane rafts and chaperones in cytokine/STAT signaling. Acta Biochim. Pol. 50, 583-594.
66. Sevier CS, Qu H, Heldman N, Gross E, Fass D, Kaiser CA (2007): Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1. Cell 129, 333-344. http://dx.doi.org/10.1016/j.cell.2007.02.039
67. Tsai B, Gilbert JM, Stehle T, Lencer W, Benjamin TL, Rapoport TA (2003): Gangliosides are receptors for murine polyoma virus and SV40. EMBO J. 22, 4346-4355. http://dx.doi.org/10.1093/emboj/cdg439
68. Tsai B, Qian M (2010): Cellular entry of polyomaviruses. Curr. Top. Microbiol. Immunol. 343, 177-194. http://dx.doi.org/10.1007/82_2010_38
69. Tsibris JC, Hunt LT, Ballejo G, Barker WC, Toney LJ, Spellacy WN (1989): Selective inhibition of protein disulfide isomerase by estrogens. J. Biol. Chem. 264, 13967-13970.
70. Tugizov SM, Berline JW, Palefsky JM (2003): Epstein-Barr virus infection of polarized tongue and nasopharyngeal epithelial cells. Nat. Med. 9, 307-314. http://dx.doi.org/10.1038/nm830
71. Turano C, Coppari S, Altieri F, Ferraro A (2002): Proteins of the PDI family: unpredicted non-ER locations and functions. J. Cell. Physiol. 193, 154-163. http://dx.doi.org/10.1002/jcp.10172
72. Valle JR, Salvador C-S, Medina F, del Angel RM (2005): Heat shock protein 90 and Heat shock protein 70 are components of dengue virus receptor complex in human cells. J. Virol. 79, 4557-4567. http://dx.doi.org/10.1128/JVI.79.8.4557-4567.2005
73. Vasta, GR (2009): Roles of galectins in infection. Nat. Rev. Microbiol. 7, 424-438. http://dx.doi.org/10.1038/nrmicro2146
74. Walczak CP, Bernardi KM, Tsai B (2012): Endoplasmic reticulum-dependent redox reactions control endoplasmic reticulum-associated degradation and pathogen entry. Antioxid. Redox Signal. 16, 809-818. http://dx.doi.org/10.1089/ars.2011.4425
75. Walczak CP, Tsai B (2011): A PDI family network acts distinctly and coordinately with ERp29 to facilitate polyomavirus infection. J. Virol. 85, 2386-2396. http://dx.doi.org/10.1128/JVI.01855-10
76. Wan S-W, Lin C-F, Lu Y-T, Lei H-Y, Anderson R, Lin Y-S (2012): Endothelial cell surface expression of protein disulfide isomerase activates β1 and β3 integrins and facilitates dengue virus infection. J. Cell. Biochem. 113, 1681-1691.
77. Wang C, Yu J, Huo L, Wang L, Feng W, Wang C (2012): Human protein-disulfide isomerase is a redox-regulated chaperone activated by oxidation of domain a'. J. Biol. Chem. 287, 1139-1149. http://dx.doi.org/10.1074/jbc.M111.303149
78. Wang CC, Tsou CL (1993): Protein disulfide isomerase is both an enzyme and a chaperone. FASEB J. 7, 1515-1517.
79. Wang J, Tong W, Zhang X, Chen L, Yi Z, Pan T, Hu Y, Xiang L, Yuan Z (2006): Hepatitis C virus non-structural protein NS5A interacts with FKBP38 and inhibits apoptosis in Huh7 hepatoma cells. FEBS Lett. 580, 4392-4400. http://dx.doi.org/10.1016/j.febslet.2006.07.002
80. Weiss RA (1993): How does HIV cause AIDS? Science 260, 1273-1279. http://dx.doi.org/10.1126/science.8493571
81. Wetterau JR, Combs KA, Spinner SN, Joiner BJ (1990): Protein disulfide isomerase as a component of the microsomal triglyceride transfer protein complex. J. Biol. Chem. 265, 9800-9807.
82. Wilkinson B, Gilbert HF (2004): Protein disulfide isomerase. Biochim. Biophys. Acta 1699, 35-44.
83. Yocupicio-Monroy RME, Medina F, del Valle RJ, del Angel RM (2003): Cellular proteins from human monocytes bind to dengue 4 virus minus-strand 3' untranslated region RNA. J. Virol. 77, 3067-3076. http://dx.doi.org/10.1128/JVI.77.5.3067-3076.2003
84. Zapun A, Darby NJ, Tessier DC, Michalak M, Bergeron JJ, Thomas DY (1998): Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57. J. Biol. Chem. 273, 6009-6012. http://dx.doi.org/10.1074/jbc.273.11.6009
85. Zhang J, Wang J, Gao N, Chen Z, Tian Y, An J (2007): Up-regulated expression of beta3 integrin induced by dengue virus serotype 2 infection associated with virus entry into human dermal microvascular endothelial cells. Biochem. Bioph. Res. Co. 356, 763-768. http://dx.doi.org/10.1016/j.bbrc.2007.03.051