메뉴 건너뛰기




Volumn 86, Issue 18, 2012, Pages 9843-9853

Potential electrostatic interactions in multiple regions affect human metapneumovirus F-mediated membrane fusion

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE FUSION PROTEIN;

EID: 84866174679     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00639-12     Document Type: Article
Times cited : (16)

References (42)
  • 2
    • 34249798208 scopus 로고    scopus 로고
    • Frequent frameshift and point mutations in the SH gene of human metapneumovirus passaged in vitro
    • Biacchesi S, Murphy BR, Collins PL, Buchholz UJ. 2007. Frequent frameshift and point mutations in the SH gene of human metapneumovirus passaged in vitro. J. Virol. 81:6057-6067.
    • (2007) J. Virol. , vol.81 , pp. 6057-6067
    • Biacchesi, S.1    Murphy, B.R.2    Collins, P.L.3    Buchholz, U.J.4
  • 3
    • 25144456514 scopus 로고    scopus 로고
    • Infection of nonhuman primates with recombinant human metapneumovirus lacking the SH, G, or M2-2 protein categorizes each as a nonessential accessory protein and identifies vaccine candidates
    • Biacchesi S, et al. 2005. Infection of nonhuman primates with recombinant human metapneumovirus lacking the SH, G, or M2-2 protein categorizes each as a nonessential accessory protein and identifies vaccine candidates. J. Virol. 79:12608-12613.
    • (2005) J. Virol. , vol.79 , pp. 12608-12613
    • Biacchesi, S.1
  • 4
    • 33744921361 scopus 로고    scopus 로고
    • Modification of the trypsin-dependent cleavage activation site of the human metapneumovirus fusion protein to be trypsin independent does not increase replication or spread in rodents or nonhuman primates
    • Biacchesi S, et al. 2006. Modification of the trypsin-dependent cleavage activation site of the human metapneumovirus fusion protein to be trypsin independent does not increase replication or spread in rodents or nonhuman primates. J. Virol. 80:5798-5806.
    • (2006) J. Virol. , vol.80 , pp. 5798-5806
    • Biacchesi, S.1
  • 5
    • 0242268380 scopus 로고    scopus 로고
    • Genetic diversity between human metapneumovirus subgroups
    • Biacchesi S, et al. 2003. Genetic diversity between human metapneumovirus subgroups. Virology 315:1-9.
    • (2003) Virology , vol.315 , pp. 1-9
    • Biacchesi, S.1
  • 6
    • 1642446601 scopus 로고    scopus 로고
    • Recovery of human metapneumovirus from cDNA: optimization of growth in vitro and expression of additional genes
    • Biacchesi S, et al. 2004. Recovery of human metapneumovirus from cDNA: optimization of growth in vitro and expression of additional genes. Virology 321:247-259.
    • (2004) Virology , vol.321 , pp. 247-259
    • Biacchesi, S.1
  • 7
    • 8644281996 scopus 로고    scopus 로고
    • Recombinant human metapneumovirus lacking the small hydrophobic SH and/or attachment G glycoprotein: deletion of G yields a promising vaccine candidate
    • Biacchesi S, et al. 2004. Recombinant human metapneumovirus lacking the small hydrophobic SH and/or attachment G glycoprotein: deletion of G yields a promising vaccine candidate. J. Virol. 78:12877-12887.
    • (2004) J. Virol. , vol.78 , pp. 12877-12887
    • Biacchesi, S.1
  • 8
    • 0036839273 scopus 로고    scopus 로고
    • Virological features and clinical manifestations associated with human metapneumovirus: a new paramyxovirus responsible for acute respiratory-tract infections in all age groups
    • Boivin G, et al. 2002. Virological features and clinical manifestations associated with human metapneumovirus: a new paramyxovirus responsible for acute respiratory-tract infections in all age groups. J. Infect. Dis. 186:1330-1334.
    • (2002) J. Infect. Dis. , vol.186 , pp. 1330-1334
    • Boivin, G.1
  • 9
    • 0037711386 scopus 로고    scopus 로고
    • Human metapneumovirus infections in hospitalized children
    • Boivin G, et al. 2003. Human metapneumovirus infections in hospitalized children. Emerg. Infect. Dis. 9:634-640.
    • (2003) Emerg. Infect. Dis. , vol.9 , pp. 634-640
    • Boivin, G.1
  • 10
    • 0032888955 scopus 로고    scopus 로고
    • Generation of bovine respiratory syncytial virus (BRSV) from cDNA: BRSV NS2 is not essential for virus replication in tissue culture, and the human RSV leader region acts as a functional BRSV genome promoter
    • Buchholz UJ, Finke S, Conzelmann KK. 1999. Generation of bovine respiratory syncytial virus (BRSV) from cDNA: BRSV NS2 is not essential for virus replication in tissue culture, and the human RSV leader region acts as a functional BRSV genome promoter. J. Virol. 73:251-259.
    • (1999) J. Virol. , vol.73 , pp. 251-259
    • Buchholz, U.J.1    Finke, S.2    Conzelmann, K.K.3
  • 11
    • 84857958198 scopus 로고    scopus 로고
    • Human metapneumovirus (HMPV) binding and infection are mediated by interactions between the HMPV fusion protein and heparan sulfate
    • Chang A, Masante C, Buchholz UJ, Dutch RE. 2012. Human metapneumovirus (HMPV) binding and infection are mediated by interactions between the HMPV fusion protein and heparan sulfate. J. Virol. 86:3230-3243.
    • (2012) J. Virol. , vol.86 , pp. 3230-3243
    • Chang, A.1    Masante, C.2    Buchholz, U.J.3    Dutch, R.E.4
  • 12
    • 0021910031 scopus 로고
    • Fusion mutants of the influenza virus hemagglutinin glycoprotein
    • Daniels RS, et al. 1985. Fusion mutants of the influenza virus hemagglutinin glycoprotein. Cell 40:431-439.
    • (1985) Cell , vol.40 , pp. 431-439
    • Daniels, R.S.1
  • 13
    • 0031664797 scopus 로고    scopus 로고
    • Membrane fusion promoted by increasing surface densities of the paramyxovirus F and HN proteins: comparison of fusion reactions mediated by simian virus 5 F, human parainfluenza virus type 3 F, and influenza virus HA
    • Dutch RE, Joshi SB, Lamb RA. 1998. Membrane fusion promoted by increasing surface densities of the paramyxovirus F and HN proteins: comparison of fusion reactions mediated by simian virus 5 F, human parainfluenza virus type 3 F, and influenza virus HA. J. Virol. 72:7745-7753.
    • (1998) J. Virol. , vol.72 , pp. 7745-7753
    • Dutch, R.E.1    Joshi, S.B.2    Lamb, R.A.3
  • 14
    • 0035037386 scopus 로고    scopus 로고
    • Deletion of the cytoplasmic tail of the fusion (F) protein of the paramyxovirus simian virus 5 (SV5) affects fusion pore enlargement
    • Dutch RE, Lamb RA. 2001. Deletion of the cytoplasmic tail of the fusion (F) protein of the paramyxovirus simian virus 5 (SV5) affects fusion pore enlargement. J. Virol. 75:5363-5369.
    • (2001) J. Virol. , vol.75 , pp. 5363-5369
    • Dutch, R.E.1    Lamb, R.A.2
  • 15
  • 16
    • 56149093228 scopus 로고    scopus 로고
    • Human metapneumovirus infection in adults
    • Falsey ARMD. 2008. Human metapneumovirus infection in adults. Pediatr. Infect. Dis. J. 27:S80-S83.
    • (2008) Pediatr. Infect. Dis. J. , vol.27
    • Falsey, A.R.M.D.1
  • 17
    • 34547131827 scopus 로고    scopus 로고
    • A conserved region in the F(2) subunit of paramyxovirus fusion proteins is involved in fusion regulation
    • Gardner AE, Dutch RE. 2007. A conserved region in the F(2) subunit of paramyxovirus fusion proteins is involved in fusion regulation. J. Virol. 81:8303-8314.
    • (2007) J. Virol. , vol.81 , pp. 8303-8314
    • Gardner, A.E.1    Dutch, R.E.2
  • 19
    • 50149093248 scopus 로고    scopus 로고
    • Low-pH-induced membrane fusion mediated by human metapneumovirus F protein is a rare, strain-dependent phenomenon
    • Herfst S, et al. 2008. Low-pH-induced membrane fusion mediated by human metapneumovirus F protein is a rare, strain-dependent phenomenon. J. Virol. 82:8891-8895.
    • (2008) J. Virol. , vol.82 , pp. 8891-8895
    • Herfst, S.1
  • 20
    • 0036151820 scopus 로고    scopus 로고
    • Protonation and stability of the globular domain of influenza virus hemagglutinin
    • Huang Q, Opitz R, Knapp E-W, Herrmann A. 2002. Protonation and stability of the globular domain of influenza virus hemagglutinin. Biophys. J. 82:1050-1058.
    • (2002) Biophys. J. , vol.82 , pp. 1050-1058
    • Huang, Q.1    Opitz, R.2    Knapp, E-W.3    Herrmann, A.4
  • 21
    • 0037811025 scopus 로고    scopus 로고
    • Early steps of the conformational change of influenza virus hemagglutinin to a fusion active state: stability and energetics of the hemagglutinin
    • Huang Q, et al. 2003. Early steps of the conformational change of influenza virus hemagglutinin to a fusion active state: stability and energetics of the hemagglutinin. Biochim. Biophys. Acta 1614:3-13.
    • (2003) Biochim. Biophys. Acta , vol.1614 , pp. 3-13
    • Huang, Q.1
  • 22
    • 33749266195 scopus 로고    scopus 로고
    • The role of histidine residues in low-pH-mediated viral membrane fusion
    • Kampmann T, Mueller DS, Mark AE, Young PR, Kobe B. 2006. The role of histidine residues in low-pH-mediated viral membrane fusion. Structure 14:1481-1487.
    • (2006) Structure , vol.14 , pp. 1481-1487
    • Kampmann, T.1    Mueller, D.S.2    Mark, A.E.3    Young, P.R.4    Kobe, B.5
  • 23
    • 0031457568 scopus 로고    scopus 로고
    • Respiratory syncytial virus (RSV) SH and G proteins are not essential for viral replication in vitro: clinical evaluation and molecular characterization of a cold-passaged, attenuated RSV sub-group B-mutant
    • Karron RA, et al. 1997. Respiratory syncytial virus (RSV) SH and G proteins are not essential for viral replication in vitro: clinical evaluation and molecular characterization of a cold-passaged, attenuated RSV sub-group B-mutant. Proc. Natl. Acad. Sci. U. S. A. 94:13961-13966.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 13961-13966
    • Karron, R.A.1
  • 24
    • 0036902235 scopus 로고    scopus 로고
    • Close-range electrostatic interactions in proteins
    • Kumar S, Nussinov R. 2002. Close-range electrostatic interactions in proteins. ChemBioChem 3:604-617.
    • (2002) ChemBioChem , vol.3 , pp. 604-617
    • Kumar, S.1    Nussinov, R.2
  • 25
    • 34547601896 scopus 로고    scopus 로고
    • Paramyxoviridae: the viruses and their replication
    • Knipe DM, et al (ed), 5th ed, Lippincott Williams & Wilkins, Philadelphia, PA.
    • Lamb RA, Parks GD. 2007. Paramyxoviridae: the viruses and their replication, p 1449-1646. In Knipe DM, et al (ed), Fields virology, 5th ed, vol 1. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2007) Fields virology , vol.1 , pp. 1449-1646
    • Lamb, R.A.1    Parks, G.D.2
  • 26
    • 60349093083 scopus 로고    scopus 로고
    • Infection and maturation of monocyte-derived human dendritic cells by human respiratory syncytial virus, human metapneumovirus, and human parainfluenza virus type 3
    • Le Nouën C, et al. 2009. Infection and maturation of monocyte-derived human dendritic cells by human respiratory syncytial virus, human metapneumovirus, and human parainfluenza virus type 3. Virology 385:169-182.
    • (2009) Virology , vol.385 , pp. 169-182
    • Le Nouën, C.1
  • 27
    • 81255163734 scopus 로고    scopus 로고
    • Residues of the human metapneumovirus fusion (F) protein critical for its strain-related fusion phenotype: implications for the virus replication cycle
    • Mas V, Herfst S, Osterhaus ADME, Fouchier RAM, Melero JA. 2011. Residues of the human metapneumovirus fusion (F) protein critical for its strain-related fusion phenotype: implications for the virus replication cycle. J. Virol. 85:12650-12661.
    • (2011) J. Virol. , vol.85 , pp. 12650-12661
    • Mas, V.1    Herfst, S.2    Osterhaus, A.D.M.E.3    Fouchier, R.A.M.4    Melero, J.A.5
  • 28
    • 77954153198 scopus 로고    scopus 로고
    • The distinguishing features of human metapneumovirus and respiratory syncytial virus
    • Papenburg J, Boivin G. 2010. The distinguishing features of human metapneumovirus and respiratory syncytial virus. Rev. Med. Virol. 20:245-260.
    • (2010) Rev. Med. Virol. , vol.20 , pp. 245-260
    • Papenburg, J.1    Boivin, G.2
  • 29
    • 0002285832 scopus 로고
    • The molecular biology of influenza viruses and paramyxoviruses
    • Davidson A, Elliott RM (ed), IRL Oxford University Press, Oxford, United Kingdom
    • Paterson RG, Lamb RA. 1993. The molecular biology of influenza viruses and paramyxoviruses, p 35-73. In Davidson A, ElliottRM(ed), Molecular virology: a practical approach. IRL Oxford University Press, Oxford, United Kingdom.
    • (1993) Molecular virology: a practical approach , pp. 35-73
    • Paterson, R.G.1    Lamb, R.A.2
  • 30
    • 33947661927 scopus 로고    scopus 로고
    • The relevance of salt bridges for the stability of the influenza virus hemagglutinin
    • Rachakonda PS, et al. 2007. The relevance of salt bridges for the stability of the influenza virus hemagglutinin. FASEB J. 21:995-1002.
    • (2007) FASEB J. , vol.21 , pp. 995-1002
    • Rachakonda, P.S.1
  • 31
    • 0242298583 scopus 로고    scopus 로고
    • A dual-functional paramyxovirus F protein regulatory switch segment: activation and membrane fusion
    • Russell CJ, Kantor KL, Jardetzky TS, Lamb RA. 2003. A dual-functional paramyxovirus F protein regulatory switch segment: activation and membrane fusion. J. Cell Biol. 163:363-374.
    • (2003) J. Cell Biol. , vol.163 , pp. 363-374
    • Russell, C.J.1    Kantor, K.L.2    Jardetzky, T.S.3    Lamb, R.A.4
  • 32
    • 3142574848 scopus 로고    scopus 로고
    • H1 and H7 influenza haemagglutinin structures extend a structural classification of haemagglutinin subtypes
    • Russell RJ, et al. 2004. H1 and H7 influenza haemagglutinin structures extend a structural classification of haemagglutinin subtypes. Virology 325:287-296.
    • (2004) Virology , vol.325 , pp. 287-296
    • Russell, R.J.1
  • 33
    • 23244433087 scopus 로고    scopus 로고
    • An S101P substitution in the putative cleavage motif of the human metapneumovirus fusion protein is a major determinant for trypsin-independent growth in Vero cells and does not alter tissue tropism in hamsters
    • Schickli JH, Kaur J, Ulbrandt N, Spaete RR, Tang RS. 2005. An S101P substitution in the putative cleavage motif of the human metapneumovirus fusion protein is a major determinant for trypsin-independent growth in Vero cells and does not alter tissue tropism in hamsters. J. Virol. 79:10678-10689.
    • (2005) J. Virol. , vol.79 , pp. 10678-10689
    • Schickli, J.H.1    Kaur, J.2    Ulbrandt, N.3    Spaete, R.R.4    Tang, R.S.5
  • 34
    • 59749100734 scopus 로고    scopus 로고
    • Low-pH triggering of human metapneumovirus fusion: essential residues and importance in entry
    • Schowalter RM, Chang A, Robach JG, Buchholz UJ, Dutch RE. 2009. Low-pH triggering of human metapneumovirus fusion: essential residues and importance in entry. J. Virol. 83:1511-1522.
    • (2009) J. Virol. , vol.83 , pp. 1511-1522
    • Schowalter, R.M.1    Chang, A.2    Robach, J.G.3    Buchholz, U.J.4    Dutch, R.E.5
  • 35
    • 33750698660 scopus 로고    scopus 로고
    • Characterization of human metapneumovirus F protein-promoted membrane fusion: critical roles for proteolytic processing and low pH
    • Schowalter RM, Smith SE, Dutch RE. 2006. Characterization of human metapneumovirus F protein-promoted membrane fusion: critical roles for proteolytic processing and low pH. J. Virol. 80:10931-10941.
    • (2006) J. Virol. , vol.80 , pp. 10931-10941
    • Schowalter, R.M.1    Smith, S.E.2    Dutch, R.E.3
  • 36
    • 77957196709 scopus 로고    scopus 로고
    • Side chain packing below the fusion peptide strongly modulates triggering of the Hendra virus F protein
    • Smith EC, Dutch RE. 2010. Side chain packing below the fusion peptide strongly modulates triggering of the Hendra virus F protein. J. Virol. 84:10928-10932.
    • (2010) J. Virol. , vol.84 , pp. 10928-10932
    • Smith, E.C.1    Dutch, R.E.2
  • 37
    • 71949123985 scopus 로고    scopus 로고
    • Viral entry mechanisms: the increasing diversity of paramyxovirus entry
    • Smith EC, Popa A, Chang A, Masante C, Dutch RE. 2009. Viral entry mechanisms: the increasing diversity of paramyxovirus entry. FEBS J. 276:7217-7227.
    • (2009) FEBS J. , vol.276 , pp. 7217-7227
    • Smith, E.C.1    Popa, A.2    Chang, A.3    Masante, C.4    Dutch, R.E.5
  • 38
    • 80052499006 scopus 로고    scopus 로고
    • Identification of nucleolin as a cellular receptor for human respiratory syncytial virus
    • Tayyari F, et al. 2011. Identification of nucleolin as a cellular receptor for human respiratory syncytial virus. Nat. Med. 17:1132-1135.
    • (2011) Nat. Med. , vol.17 , pp. 1132-1135
    • Tayyari, F.1
  • 39
    • 36749003222 scopus 로고    scopus 로고
    • Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion
    • Thoennes S, et al. 2008. Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion. Virology 370:403-414.
    • (2008) Virology , vol.370 , pp. 403-414
    • Thoennes, S.1
  • 40
    • 0034953901 scopus 로고    scopus 로고
    • A newly discovered human pneumovirus isolated from young children with respiratory tract disease
    • van den Hoogen BG, et al. 2001. A newly discovered human pneumovirus isolated from young children with respiratory tract disease. Nat. Med. 7:719-724.
    • (2001) Nat. Med. , vol.7 , pp. 719-724
    • van den Hoogen, B.G.1
  • 41
    • 58149098611 scopus 로고    scopus 로고
    • Human metapneumovirus infections in adults: another piece of the puzzle
    • Walsh EE, Peterson DR, Falsey AR. 2008. Human metapneumovirus infections in adults: another piece of the puzzle. Arch. Intern. Med. 168:2489-2496.
    • (2008) Arch. Intern. Med. , vol.168 , pp. 2489-2496
    • Walsh, E.E.1    Peterson, D.R.2    Falsey, A.R.3
  • 42
    • 30144436116 scopus 로고    scopus 로고
    • Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation
    • Yin HS, Wen X, Paterson RG, Lamb RA, Jardetzky TS. 2006. Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation. Nature 439:38-44.
    • (2006) Nature , vol.439 , pp. 38-44
    • Yin, H.S.1    Wen, X.2    Paterson, R.G.3    Lamb, R.A.4    Jardetzky, T.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.