메뉴 건너뛰기




Volumn 85, Issue 4, 2011, Pages 1507-1516

A proapoptotic peptide derived from reovirus outer capsid protein μ1 has membrane-destabilizing activity

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; H1 PEPTIDE; H3 PEPTIDE; LIPOSOME; PHOSPHOLIPASE C; REOVIRUS OUTER CAPSID PROTEIN MU1; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 78951487258     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01876-10     Document Type: Article
Times cited : (9)

References (34)
  • 2
    • 58449084373 scopus 로고    scopus 로고
    • Apoptosis in animal models of virusinduced disease
    • Clarke, P., and K. L. Tyler. 2009. Apoptosis in animal models of virusinduced disease. Nat. Rev. Microbiol. 7:144-155.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 144-155
    • Clarke, P.1    Tyler, K.L.2
  • 3
    • 33748641937 scopus 로고    scopus 로고
    • Reovirus outer capsid protein μ1 induces apoptosis and associates with lipid droplets, endoplasmic reticulum, and mitochondria
    • Coffey, C. M., et al. 2006. Reovirus outer capsid protein μ1 induces apoptosis and associates with lipid droplets, endoplasmic reticulum, and mitochondria. J. Virol. 80:8422-8438.
    • (2006) J. Virol. , vol.80 , pp. 8422-8438
    • Coffey, C.M.1
  • 4
    • 0036147875 scopus 로고    scopus 로고
    • Virion disassembly is required for apoptosis induced by reovirus
    • Connolly, J. L., and T. S. Dermody. 2002. Virion disassembly is required for apoptosis induced by reovirus. J. Virol. 76:1632-1641.
    • (2002) J. Virol. , vol.76 , pp. 1632-1641
    • Connolly, J.L.1    Dermody, T.S.2
  • 5
    • 58149268150 scopus 로고    scopus 로고
    • Independent regulation of reovirus membrane penetration and apoptosis by the μ1 φ domain
    • Danthi, P., C. M. Coffey, J. S. Parker, T. W. Abel, and T. S. Dermody. 2008. Independent regulation of reovirus membrane penetration and apoptosis by the μ1 φ domain. PLoS Pathog. 4:e1000248.
    • (2008) PLoS Pathog. , vol.4
    • Danthi, P.1    Coffey, C.M.2    Parker, J.S.3    Abel, T.W.4    Dermody, T.S.5
  • 6
    • 31144446888 scopus 로고    scopus 로고
    • JAM-A-independent, antibody-mediated uptake of reovirus into cells leads to apoptosis
    • Danthi, P., M. W. Hansberger, J. A. Campbell, J. C. Forrest, and T. S. Dermody. 2006. JAM-A-independent, antibody-mediated uptake of reovirus into cells leads to apoptosis. J. Virol. 80:1261-1270.
    • (2006) J. Virol. , vol.80 , pp. 1261-1270
    • Danthi, P.1    Hansberger, M.W.2    Campbell, J.A.3    Forrest, J.C.4    Dermody, T.S.5
  • 7
    • 37349062727 scopus 로고    scopus 로고
    • Reovirus apoptosis and virulence are regulated by host cell membrane penetration efficiency
    • Danthi, P., et al. 2008. Reovirus apoptosis and virulence are regulated by host cell membrane penetration efficiency. J. Virol. 82:161-172.
    • (2008) J. Virol. , vol.82 , pp. 161-172
    • Danthi, P.1
  • 8
    • 77957677378 scopus 로고    scopus 로고
    • Bid regulates the pathogenesis of neurotropic reovirus
    • Danthi, P., et al. 2010. Bid regulates the pathogenesis of neurotropic reovirus. PLoS Pathog. 6:e1000980.
    • (2010) PLoS Pathog. , vol.6
    • Danthi, P.1
  • 9
    • 0032889283 scopus 로고    scopus 로고
    • Reovirus-induced apoptosis is preceded by increased cellular calpain activity and is blocked by calpain inhibitors
    • Debiasi, R. L., et al. 1999. Reovirus-induced apoptosis is preceded by increased cellular calpain activity and is blocked by calpain inhibitors. J. Virol. 73:695-701.
    • (1999) J. Virol. , vol.73 , pp. 695-701
    • Debiasi, R.L.1
  • 11
    • 0031039956 scopus 로고    scopus 로고
    • Peptide antibiotics
    • Hancock, R. E. 1997. Peptide antibiotics. Lancet 349:418-422.
    • (1997) Lancet , vol.349 , pp. 418-422
    • Hancock, R.E.1
  • 13
    • 42449151315 scopus 로고    scopus 로고
    • Peptides released from reovirus outer capsid form membrane pores that recruit virus particles
    • Ivanovic, T., et al. 2008. Peptides released from reovirus outer capsid form membrane pores that recruit virus particles. EMBO J. 27:1289-1298.
    • (2008) EMBO J. , vol.27 , pp. 1289-1298
    • Ivanovic, T.1
  • 14
    • 0036718385 scopus 로고    scopus 로고
    • Reovirus-induced apoptosis requires both death receptor- and mitochondrial-mediated caspase-dependent pathways of cell death
    • Kominsky, D. J., R. J. Bickel, and K. L. Tyler. 2002. Reovirus-induced apoptosis requires both death receptor- and mitochondrial-mediated caspase-dependent pathways of cell death. Cell Death Differ. 9:926-933.
    • (2002) Cell Death Differ. , vol.9 , pp. 926-933
    • Kominsky, D.J.1    Bickel, R.J.2    Tyler, K.L.3
  • 15
    • 0036827535 scopus 로고    scopus 로고
    • Reovirus-induced apoptosis requires mitochondrial release of Smac/DIABLO and involves reduction of cellular inhibitor of apoptosis protein levels
    • Kominsky, D. J., R. J. Bickel, and K. L. Tyler. 2002. Reovirus-induced apoptosis requires mitochondrial release of Smac/DIABLO and involves reduction of cellular inhibitor of apoptosis protein levels. J. Virol. 76:11414-11424.
    • (2002) J. Virol. , vol.76 , pp. 11414-11424
    • Kominsky, D.J.1    Bickel, R.J.2    Tyler, K.L.3
  • 16
    • 0036850312 scopus 로고    scopus 로고
    • Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane
    • Kuwana, T., et al. 2002. Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane. Cell 111:331-342.
    • (2002) Cell , vol.111 , pp. 331-342
    • Kuwana, T.1
  • 18
    • 3042737827 scopus 로고    scopus 로고
    • Membrane disrupting lytic peptides for cancer treatments
    • Leuschner, C., and W. Hansel. 2004. Membrane disrupting lytic peptides for cancer treatments. Curr. Pharm. Des. 10:2299-2310.
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 2299-2310
    • Leuschner, C.1    Hansel, W.2
  • 19
    • 0037169362 scopus 로고    scopus 로고
    • Structure of the reovirus membrane-penetration protein, μ1, in a complex with is protector protein, σ3
    • Liemann, S., K. Chandran, T. S. Baker, M. L. Nibert, and S. C. Harrison. 2002. Structure of the reovirus membrane-penetration protein, μ1, in a complex with is protector protein, σ3. Cell 108:283-295.
    • (2002) Cell , vol.108 , pp. 283-295
    • Liemann, S.1    Chandran, K.2    Baker, T.S.3    Nibert, M.L.4    Harrison, S.C.5
  • 20
    • 0026733619 scopus 로고
    • A carboxy-terminal fragment of protein μ1/μ1C is present in infectious subvirion particles of mammalian reoviruses and is proposed to have a role in penetration
    • Nibert, M. L., and B. N. Fields. 1992. A carboxy-terminal fragment of protein μ1/μ1C is present in infectious subvirion particles of mammalian reoviruses and is proposed to have a role in penetration. J. Virol. 66:6408-6418.
    • (1992) J. Virol. , vol.66 , pp. 6408-6418
    • Nibert, M.L.1    Fields, B.N.2
  • 21
    • 3543115472 scopus 로고    scopus 로고
    • Putative autocleavage of outer capsid protein μ1, allowing release of myristoylated peptide μ1N during particle uncoating, is critical for cell entry by reovirus
    • Odegard, A. L., et al. 2004. Putative autocleavage of outer capsid protein μ1, allowing release of myristoylated peptide μ1N during particle uncoating, is critical for cell entry by reovirus. J. Virol. 78:8732-8745.
    • (2004) J. Virol. , vol.78 , pp. 8732-8745
    • Odegard, A.L.1
  • 22
    • 28444450556 scopus 로고    scopus 로고
    • Coexistence of a two-states organization for a cell-penetrating peptide in lipid bilayer
    • Plenat, T., S. Boichot, P. Dosset, P. E. Milhiet, and C. Le Grimellec. 2005. Coexistence of a two-states organization for a cell-penetrating peptide in lipid bilayer. Biophys. J. 89:4300-4309.
    • (2005) Biophys. J. , vol.89 , pp. 4300-4309
    • Plenat, T.1    Boichot, S.2    Dosset, P.3    Milhiet, P.E.4    Le Grimellec, C.5
  • 23
    • 6444236956 scopus 로고    scopus 로고
    • Interaction of primary amphipathic cell-penetrating peptides with phospholipid-supported monolayers
    • Plenat, T., et al. 2004. Interaction of primary amphipathic cell-penetrating peptides with phospholipid-supported monolayers. Langmuir 20:9255-9261.
    • (2004) Langmuir , vol.20 , pp. 9255-9261
    • Plenat, T.1
  • 24
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and antibacterial activity
    • Powers, J. P., and R. E. Hancock. 2003. The relationship between peptide structure and antibacterial activity. Peptides 24:1681-1691.
    • (2003) Peptides , vol.24 , pp. 1681-1691
    • Powers, J.P.1    Hancock, R.E.2
  • 25
    • 67650375869 scopus 로고    scopus 로고
    • Immune-mediated antitumor activity of reovirus is required for therapy and is independent of direct viral oncolysis and replication
    • Prestwich, R. J., et al. 2009. Immune-mediated antitumor activity of reovirus is required for therapy and is independent of direct viral oncolysis and replication. Clin. Cancer Res. 15:4374-4381.
    • (2009) Clin. Cancer Res. , vol.15 , pp. 4374-4381
    • Prestwich, R.J.1
  • 26
    • 0032526693 scopus 로고    scopus 로고
    • The molecular basis of viral oncolysis: Usurpation of the Ras signaling pathway by reovirus
    • Strong, J. E., M. C. Coffey, D. Tang, P. Sabinin, and P. W. Lee. 1998. The molecular basis of viral oncolysis: usurpation of the Ras signaling pathway by reovirus. EMBO J. 17:3351-3362.
    • (1998) EMBO J. , vol.17 , pp. 3351-3362
    • Strong, J.E.1    Coffey, M.C.2    Tang, D.3    Sabinin, P.4    Lee, P.W.5
  • 27
    • 0030722714 scopus 로고    scopus 로고
    • Novel antimicrobial peptides derived from human immunodeficiency virus type 1 and other lentivirus transmembrane proteins
    • Tencza, S. B., J. P. Douglass, D. J. Creighton, Jr., R. C. Montelaro, and T. A. Mietzner. 1997. Novel antimicrobial peptides derived from human immunodeficiency virus type 1 and other lentivirus transmembrane proteins. Antimicrob. Agents Chemother. 41:2394-2398.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 2394-2398
    • Tencza, S.B.1    Douglass, J.P.2    Creighton Jr., D.J.3    Montelaro, R.C.4    Mietzner, T.A.5
  • 28
    • 67650296739 scopus 로고    scopus 로고
    • Oncolytic viral therapy using reovirus
    • Thirukkumaran, C., and D. G. Morris. 2009. Oncolytic viral therapy using reovirus. Methods Mol. Biol. 542:607-634.
    • (2009) Methods Mol. Biol. , vol.542 , pp. 607-634
    • Thirukkumaran, C.1    Morris, D.G.2
  • 29
    • 0029085955 scopus 로고
    • 2+from the endoplasmic reticulum
    • 2+ from the endoplasmic reticulum. J. Virol. 69:5763-5772.
    • (1995) J. Virol. , vol.69 , pp. 5763-5772
    • Tian, P.1
  • 30
    • 0028826078 scopus 로고
    • Differences in the capacity of reovirus strains to induce apoptosis are determined by the viral attachment protein σ1
    • Tyler, K. L., et al. 1995. Differences in the capacity of reovirus strains to induce apoptosis are determined by the viral attachment protein σ1. J. Virol. 69:6972-6979.
    • (1995) J. Virol. , vol.69 , pp. 6972-6979
    • Tyler, K.L.1
  • 31
    • 78650041205 scopus 로고    scopus 로고
    • Reovirus infection or ectopic expression of outer-capsid protein μ1 induces apoptosis independently of the cellular proapoptotic proteins Bax and Bak
    • 27 October [Epub ahead of print.] doi:10.1128/JVI.01982-10
    • Wisniewski, M. L., et al. 27 October 2010. Reovirus infection or ectopic expression of outer-capsid protein μ1 induces apoptosis independently of the cellular proapoptotic proteins Bax and Bak. J. Virol. [Epub ahead of print.] doi:10.1128/JVI.01982-10.
    • (2010) J. Virol.
    • Wisniewski, M.L.1
  • 32
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochrome C from mitochondria blocked
    • Yang, J., et al. 1997. Prevention of apoptosis by Bcl-2: release of cytochrome C from mitochondria blocked. Science 275:1129-1132.
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1
  • 33
    • 33748933561 scopus 로고    scopus 로고
    • Alpha-helical antimicrobial peptides - Using a sequence template to guide structure-activity relationship studies
    • Zelezetsky, I., and A. Tossi. 2006. Alpha-helical antimicrobial peptides - using a sequence template to guide structure-activity relationship studies. Biochim. Biophys. Acta 1758:1436-1449.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1436-1449
    • Zelezetsky, I.1    Tossi, A.2
  • 34
    • 67650444363 scopus 로고    scopus 로고
    • Requirements for the formation of membrane pores by the reovirus myristoylated μ1N peptide
    • Zhang, L., et al. 2009. Requirements for the formation of membrane pores by the reovirus myristoylated μ1N peptide. J. Virol. 83:7004-7014.
    • (2009) J. Virol. , vol.83 , pp. 7004-7014
    • Zhang, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.