Toxoplasma gondii ingests and digests host Cytosolic proteins

mBio

Volumn 5, Issue 4, 2014, Pages

  Dou, Zhicheng ^a   McGovern, Olivia L ^a   Di Cristina, Manlio ^b   Carruthers, Vern B ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^b UNIVERSITY OF PERUGIA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN L; CELL PROTEIN; CYTOSOLIC PROTEIN; PROTEINASE; UNCLASSIFIED DRUG; PROTEIN;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CELL MEMBRANE; CELL VACUOLE; CONTROLLED STUDY; CYTOSOL; ENDOSOME; FEMALE; HOST CELL; HUMAN; HUMAN CELL; INTERNALIZATION; LYSOSOME; MOUSE; NONHUMAN; PARASITE DEVELOPMENT; PARASITE VIRULENCE; PROTEIN METABOLISM; TOXOPLASMA GONDII; ANIMAL; METABOLISM; PARASITOLOGY; PATHOGENICITY; TOXOPLASMA; TOXOPLASMOSIS;

TOXOPLASMA GONDII;

ANIMALS; CYTOSOL; FEMALE; MICE; PROTEINS; TOXOPLASMA; TOXOPLASMOSIS;

EID: 84907972304     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.01188-14     Document Type: Article

References (29)

1. Lindsay DS, Dubey JP. 2011. Toxoplasma gondii: the changing paradigm of congenital toxoplasmosis. Parasitology 138:1-3. http://dx.doi.org/10.1017/S003118201000096X.
2. Black MW, Boothroyd JC. 2000. Lytic cycle of Toxoplasma gondii. Microbiol. Mol. Biol. Rev. 64:607-623. http://dx.doi.org/10.1128/MMBR.64.3.607-623.2000.
3. Carruthers VB. 2002. Host cell invasion by the opportunistic pathogen Toxoplasma gondii. Acta Trop. 81:111-122. http://dx.doi.org/10.1016/S0001-706X(01)00201-7.
4. Mercier C, Dubremetz JF, Rauscher B, Lecordier L, Sibley LD, Cesbron-Delauw MF. 2002. Biogenesis of nanotubular network in Toxoplasma parasitophorous vacuole induced by parasite proteins. Mol. Biol. Cell 13:2397-2409. http://dx.doi.org/10.1091/mbc.E02-01-0021.
5. Mercier C, Adjogble KD, Däubener W, Delauw MF. 2005. Dense granules: are they key organelles to help understand the parasitophorous vacuole of all Apicomplexa parasites? Int. J. Parasitol. 35:829-849. http://dx.doi.org/10.1016/j.ijpara.2005.03.011.
6. Caffaro CE, Boothroyd JC. 2011. Evidence for host cells as the major contributor of lipids in the intravacuolar network of Toxoplasma-infected cells. Eukaryot. Cell 10:1095-1099. http://dx.doi.org/10.1128/EC.00002-11.
7. Sibley LD. 2004. Intracellular parasite invasion strategies. Science 304: 248-253. http://dx.doi.org/10.1126/science.1094717.
8. Schwab JC, Beckers CJ, Joiner KA. 1994. The parasitophorous vacuole membrane surrounding intracellular Toxoplasma gondii functions as a molecular sieve. Proc. Natl. Acad. Sci. U. S. A. 91:509-513. http://dx.doi.org/10.1073/pnas.91.2.509.
9. Goldszmid RS, Coppens I, Lev A, Caspar P, Mellman I, Sher A. 2009. Host ER-parasitophorous vacuole interaction provides a route of entry for antigen cross-presentation in Toxoplasma gondii-infected dendritic cells. J. Exp. Med. 206:399-410. http://dx.doi.org/10.1084/jem.20082108.
10. Nichols BA, Chiappino ML, Pavesio CE. 1994. Endocytosis at the micropore of Toxoplasma gondii. Parasitol. Res. 80:91-98. http://dx.doi.org/10.1007/BF00933773.
11. Botero-Kleiven S, Fernández V, Lindh J, Richter-Dahlfors A, von Euler A, Wahlgren M. 2001. Receptor-mediated endocytosis in an apicomplexan parasite (Toxoplasma gondii). Exp. Parasitol. 98:134-144. http://dx.doi.org/10.1006/expr.2001.4624.
12. Parussini F, Coppens I, Shah PP, Diamond SL, Carruthers VB. 2010. Cathepsin L occupies a vacuolar compartment and is a protein maturase within the endo/exocytic system of Toxoplasma gondii. Mol. Microbiol. 76:1340-1357. http://dx.doi.org/10.1111/j.1365-2958.2010.07181.x.
13. Robibaro B, Stedman TT, Coppens I, Ngô HM, Pypaert M, Bivona T, Nam HW, Joiner KA. 2002. Toxoplasma gondii Rab5 enhances cholesterol acquisition from host cells. Cell. Microbiol. 4:139-152. http://dx.doi.org/10.1046/j.1462-5822.2002.00178.x.
14. Dou Z, Carruthers VB. 2011. Cathepsin proteases in Toxoplasma gondii. Adv. Exp. Med. Biol. 712:49-61. http://dx.doi.org/10.1007/978-1-4419-8414-2_4.
15. Dou Z, Coppens I, Carruthers VB. 2013. Non-canonical maturation of two papain-family proteases in Toxoplasma gondii. J. Biol. Chem. 288: 3523-3534. http://dx.doi.org/10.1074/jbc.M112.443697.
16. Miranda K, Pace DA, Cintron R, Rodrigues JC, Fang J, Smith A, Rohloff P, Coelho E, de Haas F, de Souza W, Coppens I, Sibley LD, Moreno SN. 2010. Characterization of a novel organelle in Toxoplasma gondii with similar composition and function to the plant vacuole. Mol. Microbiol. 76:1358-1375. http://dx.doi.org/10.1111/j.1365-2958.2010.07165.x.
17. Fox BA, Falla A, Rommereim LM, Tomita T, Gigley JP, Mercier C, Cesbron-Delauw MF, Weiss LM, Bzik DJ. 2011. Type II Toxoplasma gondii KU80 knockout strains enable functional analysis of genes required for cyst development and latent infection. Eukaryot. Cell 10:1193-1206. http://dx.doi.org/10.1128/EC.00297-10.
18. Franke-Fayard B, Djokovic D, Dooren MW, Ramesar J, Waters AP, Falade MO, Kranendonk M, Martinelli A, Cravo P, Janse CJ. 2008. Simple and sensitive antimalarial drug screening in vitro and in vivo using transgenic luciferase expressing Plasmodium berghei parasites. Int. J. Parasitol. 38:1651-1662. http://dx.doi.org/10.1016/j.ijpara.2008.05.012.
19. Larson ET, Parussini F, Huynh MH, Giebel JD, Kelley AM, Zhang L, Bogyo M, Merritt EA, Carruthers VB. 2009. Toxoplasma gondii cathepsin L is the primary target of the invasion-inhibitory compound morpholinurea-leucyl-homophenyl-vinyl sulfone phenyl. J. Biol. Chem. 284:26839-26850. http://dx.doi.org/10.1074/jbc.M109.003780.
20. Sibley LD, Krahenbuhl JL, Adams GM, Weidner E. 1986. Toxoplasma modifies macrophage phagosomes by secretion of a vesicular network rich in surface proteins. J. Cell Biol. 103:867-874. http://dx.doi.org/10.1083/jcb.103.3.867.
21. Labruyere E, Lingnau M, Mercier C, Sibley LD. 1999. Differential membrane targeting of the secretory proteins GRA4 and GRA6 within the parasitophorous vacuole formed by Toxoplasma gondii. Mol. Biochem. Parasitol. 102:311-324. http://dx.doi.org/10.1016/S0166-6851(99)00092-4.
22. Coppens I, Dunn JD, Romano JD, Pypaert M, Zhang H, Boothroyd JC, Joiner KA. 2006. Toxoplasma gondii sequesters lysosomes from mammalian hosts in the vacuolar space. Cell 125:261-274. http://dx.doi.org/10.1016/j.cell.2006.01.056.
23. Magno RC, Lemgruber L, Vommaro RC, De Souza W, Attias M. 2005. Intravacuolar network may act as a mechanical support for Toxoplasma gondii inside the parasitophorous vacuole. Microsc. Res. Tech. 67:45-52. http://dx.doi.org/10.1002/jemt.20182.
24. Breinich MS, Ferguson DJ, Foth BJ, van Dooren GG, Lebrun M, Quon DV, Striepen B, Bradley PJ, Frischknecht F, Carruthers VB, Meissner M. 2009. A dynamin is required for the biogenesis of secretory organelles in Toxoplasma gondii. Curr. Biol. 19:277-286. http://dx.doi.org/10.1016/j.cub.2009.01.039.
25. Slomianny C. 1990. Three-dimensional reconstruction of the feeding process of the malaria parasite. Blood Cells 16:369-378.
26. Rosenthal PJ. 2011. Falcipains and other cysteine proteases of malaria parasites. Adv. Exp. Med. Biol. 712:30-48. http://dx.doi.org/10.1007/978-1-4419-8414-2_3.
27. Harper JM, Huynh MH, Coppens I, Parussini F, Moreno S, Carruthers VB. 2006. A cleavable propeptide influences Toxoplasma infection by facilitating the trafficking and secretion of the TgMIC2-M2AP invasion complex. Mol. Biol. Cell 17:4551-4563. http://dx.doi.org/10.1091/mbc.E06-01-0064.
28. Donald RG, Roos DS. 1998. Gene knock-outs and allelic replacements in Toxoplasma gondii: HXGPRT as a selectable marker for hit-and-run mutagenesis. Mol. Biochem. Parasitol. 91:295-305. http://dx.doi.org/10.1016/S0166-6851(97)00210-7.
29. Brydges SD, Carruthers VB. 2003. Mutation of an unusual mitochondrial targeting sequence of SODB2 produces multiple targeting fates in Toxoplasma gondii. J. Cell Sci. 116:4675-4685. http://dx.doi.org/10.1242/jcs.00750.