EXO70 protein influences dengue virus secretion

Microbes and Infection

Volumn 13, Issue 2, 2011, Pages 143-150

  Chen, Zhaoni ^a   Lin, Xing ^a   Zhang, Zhiwei ^a   Huang, Jianchun ^a   Fu, Shujie ^a   Huang, Renbin ^a  

^a Department of Pharmacology   (Netherlands)

Author keywords

Dengue virus; EXO70; Virus egression

Indexed keywords

ENVELOPE PROTEIN; EXOCYST; PROTEIN EXO 70; UNCLASSIFIED DRUG;

ARTICLE; DENGUE; DENGUE VIRUS; EXOCYTOSIS; HUMAN; HUMAN CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; UPREGULATION; VIRUS PARTICLE;

BLOTTING, WESTERN; CELL LINE; DENGUE; DENGUE VIRUS; FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT; GENE EXPRESSION REGULATION; GENE KNOCKDOWN TECHNIQUES; HEP G2 CELLS; HUMANS; MICROSCOPY, ELECTRON, TRANSMISSION; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; RNA; VESICULAR TRANSPORT PROTEINS; VIRAL PROTEINS; VIRUS REPLICATION;

DENGUE VIRUS;

EID: 78651492816     PISSN: 12864579     EISSN: 1769714X     Source Type: Journal    
DOI: 10.1016/j.micinf.2010.10.011     Document Type: Article

References (33)

1. Halstead S.B. Dengue. Lancet 2007, 370:1644-1652.
2. Leong A.S., Wong K.T., Leong T.Y., Tan P.H., Wannakrairot P. The pathology of dengue hemorrhagic fever. Semin. Diagn. Pathol 2007, 24:227-236.
3. Acosta E.G., Castilla V., Damonte E.B. Functional entry of dengue virus into aedes albopictus mosquito cells is dependent on clathrin-mediated endocytosis. J. Gen. Virol 2008, 89:474-484.
4. Peng T., Wang J.L., Chen W., Zhang J.L., Gao N., Chen Z.T., Xu X.F., Fan D.Y., An J. Entry of dengue virus serotype 2 into ECV304 cells depends on clathrin-dependent endocytosis, but not on caveolae-dependent endocytosis. Can. J. Microbiol. 2009, 55:139-145.
5. Bressanelli S., Stiasny K., Allison S.L., Stura E.A., Duquerroy S., Lescar J., Heinz F.X., Rey F.A. Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation. EMBO J 2004, 23:728-738.
6. Heinz F.X., Allison S.L. Flavivirus structure and membrane fusion. Adv. Virus. Res. 2003, 59:63-97.
7. Allison S.L., Schalich J., Stiasny K., Mandl C.W., Heinz F.X. Mutational evidence for an internal fusion peptide in flavivirus envelope protein E. J. Virol. 2001, 75:4268-4275.
8. Heinz F.X., Allison S.L. Structures and mechanisms in flavivirus fusion. Adv. Virus Res. 2000, 55:231-269.
9. Koschinski A., Wengler G., Repp H. The membrane proteins of flaviviruses form ion-permeable pores in the target membrane after fusion: identification of the pores and analysis of their possible role in virus infection. J. Gen. Virol 2003, 84:1711-1721.
10. Chambers T.J., Hahn C.S., Galler R., Rice C.M. Flavivirus genome organization, expression, and replication. Annu. Rev. Microbiol. 1990, 44:649-688.
11. Mackenzie J.M., Westaway E.G. Assembly and maturation of the flavivirus Kunjin virus appear to occur in the rough endoplasmic reticulum and along the secretory pathway, respectively. J. Virol 2001, 75:10787-10799.
12. Ma L., Jones C.T., Groesch T.D., Kuhn R.J., Post C.B. Solution structure of dengue virus capsid protein reveals another fold. Proc. Natl. Acad. Sci. U S A 2004, 101:3414-3419.
13. Wang S.H., Syu W.J., Hu S.T. Identification of the homotypic interaction domain of the core protein of dengue virus type 2. J. Gen. Virol 2004, 85:2307-2314.
14. Lobigs M., Lee E. Inefficient signalase cleavage promotes efficient nucleocapsid incorporation into budding flavivirus membranes. J. Virol 2004, 78:178-186.
15. Murray J.M., Aaskov J.G., Wright P.J. Processing of the dengue virus type 2 proteins prM and C-prM. J. Gen. Virol 1993, 74(Pt 2):175-182.
16. Yu I.M., Zhang W., Holdaway H.A., Li L., Kostyuchenko V.A., Chipman P.R., Kuhn R.J., Rossmann M.G., Chen J. Structure of the immature dengue virus at low pH primes proteolytic maturation. Science 2008, 319:1834-1837.
17. TerBush D.R., Maurice T., Roth D., Novick P. The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae. EMBO J 1996, 15:6483-6494.
18. Hsu S., Hazuka C., Foletti D., Scheller R. Targeting vesicles to specific sites on the plasma membrane: the role of the sec6/8 complex. Trends Cell. Biol. 1999, 9:150-153.
19. Zhang X., Orlando K., He B., Xi F., Zhang J., Zajac A., Guo W. Membrane association and functional regulation of Sec3 by phospholipids and Cdc42. J. Cell. Biol. 2008, 180:145-158.
20. Finger F.P., Novick P. Sec3p is involved in secretion and morphogenesis in Saccharomyces cerevisiae. Mol. Biol. Cell. 1997, 8:647-662.
21. Finger F.P., Hughes T., Novick P. Sec3p is a spatial landmark for polarized secretion in budding yeast. Cell 1998, 92:559-571.
22. Hsu S.C., TerBush D., Abraham M., Guo W. The exocyst complex in polarized exocytosis. Int. Rev. Cytol 2004, 233:243-265.
23. Guo W., Tamanoi F., Novick P. Spatial regulation of the exocyst complex by Rho1 GTPase. Nat. Cell. Biol. 2001, 3:353-360.
24. Zhang X., Bi E., Novick P., Du L., Kozminski K.G., Lipschutz J.H., Guo W. Cdc42 interacts with the exocyst and regulates polarized secretion. J. Biol. Chem. 2001, 276:46745-46750.
25. Baek K., Knodler A., Lee S.H., Zhang X., Orlando K., Zhang J., Foskett T.J., Guo W., Dominguez R. Structure-function study of the N-terminal domain of exocyst subunit Sec3. J. Biol. Chem. 2010, 285:10424-10433.
26. Aronov S., Gerst J. Involvement of the late secretory pathway in actin regulation and mRNA transport in yeast. J. Biol. Chem. 2004, 279:36962-36971.
27. Bhuvanakantham R., Li J., Tan T.T., Ng M.L. Human Sec3 protein is a novel transcriptional and translational repressor of flavivirus. Cell. Microbiol. 2010, 12:453-472.
28. Gao F., Duan X., Lu X., Liu Y., Zheng L., Ding Z., Li J. Novel binding between pre-membrane protein and claudin-1 is required for efficient dengue virus entry. Biochem. Biophys. Res. Commun 2010, 391:952-957.
29. Duan X., Lu X., Li J., Liu Y. Novel binding between pre-membrane protein and vacuolar ATPase is required for efficient dengue virus secretion. Biochem. Biophys. Res. Commun 2008, 373:319-324.
30. Boyd C., Hughes T., Pypaert M., Novick P. Vesicles carry most exocyst subunits to exocytic sites marked by the remaining two subunits, Sec3p and Exo70p. J. Cell. Biol. 2004, 167:889-901.
31. He B., Xi F., Zhang X., Zhang J., Guo W. Exo70 interacts with phospholipids and mediates the targeting of the exocyst to the plasma membrane. EMBO J 2007, 26:4053-4065.
32. Wu H., Turner C., Gardner J., Temple B., Brennwald P. The Exo70 subunit of the exocyst is an effector for both Cdc42 and Rho3 function in polarized exocytosis. Mol. Biol. Cell. 2010, 21:430-442.
33. He B., Guo W. The exocyst complex in polarized exocytosis. Curr. Opin. Cell. Biol. 2009, 21:537-542.