메뉴 건너뛰기




Volumn 1808, Issue 6, 2011, Pages 1567-1573

Study of the inhibition capacity of an 18-mer peptide domain of GBV-C virus on gp41-FP HIV-1 activity

Author keywords

AFM; GBV C; HIV 1; Lipid monolayer; Peptidepeptide binding

Indexed keywords

AMPHOLYTE; ARGINYLPHENYLALANYLPROLYLPHENYLALANYLHISTIDINYLARGINYLCYSTEINYLGLYCYLALANYLGLYCYLPROLYLLYSYLLEUCYLTHREONYLLYSYLASPARTYLLEUCYLGLUTAMIC ACID; GLYCOPROTEIN GP 41; LIPOSOME; PHOSPHOLIPID; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN; WATER;

EID: 79954797673     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2011.02.019     Document Type: Article
Times cited : (16)

References (35)
  • 1
    • 34848839921 scopus 로고    scopus 로고
    • Evaluation of circulating natural type 1 interferon-producing cells in HIV/GBV-C and HIV/HCV coinfected patients: A preliminary study
    • H.M.H. Mostafa, P. Ali-Akbar, M. Minoo, S. Zahra, A. Sedigheh, A. Mahnaz, S. Shahram, N. Mahin, and M. Reza Evaluation of circulating natural type 1 interferon-producing cells in HIV/GBV-C and HIV/HCV coinfected patients: a preliminary study Arch. Med. Res. 38 2007 868 875
    • (2007) Arch. Med. Res. , vol.38 , pp. 868-875
    • Mostafa, H.M.H.1    Ali-Akbar, P.2    Minoo, M.3    Zahra, S.4    Sedigheh, A.5    Mahnaz, A.6    Shahram, S.7    Mahin, N.8    Reza, M.9
  • 4
    • 69049100067 scopus 로고    scopus 로고
    • GB virus C genotype 2 predominance in a hepatitis C virus/HIV infected population associated with reduced liver disease
    • M.D. Berzsenyi, D.S. Bowden, S.K. Roberts, and P.A. Revill GB virus C genotype 2 predominance in a hepatitis C virus/HIV infected population associated with reduced liver disease J. Gastroenterol. Hepatol. 24 2009 1407 1410
    • (2009) J. Gastroenterol. Hepatol. , vol.24 , pp. 1407-1410
    • Berzsenyi, M.D.1    Bowden, D.S.2    Roberts, S.K.3    Revill, P.A.4
  • 5
    • 22144458381 scopus 로고    scopus 로고
    • GB virus C: Insights into co-infection
    • DOI 10.1016/j.jcv.2005.04.002, PII S1386653205001010
    • M.D. Berzsenyi, D.S. Bowden, and S.K. Roberts GB virus C: insights into co-infection J. Clin. Virol. 33 2005 257 266 (Pubitemid 40982513)
    • (2005) Journal of Clinical Virology , vol.33 , Issue.4 , pp. 257-266
    • Berzsenyi, M.D.1    Bowden, D.S.2    Roberts, S.K.3
  • 6
    • 34447573625 scopus 로고    scopus 로고
    • Enhanced and resumed GB virus C replication in HIV-1-infected individuals receiving HAART
    • DOI 10.1097/QAD.0b013e32823bc9b7, PII 0000203020070731000019
    • P. Björkman, L. Flamholc, V. Molnegren, A. Marshall, N. Güner, and A. Widell Enhanced and resumed GB virus C replication in HIV-1-infected individuals receiving HAART AIDS 21 2007 1641 1643 (Pubitemid 47075487)
    • (2007) AIDS , vol.21 , Issue.12 , pp. 1641-1643
    • Bjorkman, P.1    Flamholc, L.2    Molnegren, V.3    Marshall, A.4    Guner, N.5    Widell, A.6
  • 7
    • 35548993637 scopus 로고    scopus 로고
    • Application of a chimeric synthetic peptide in the development of a serologic method for the diagnosis of hepatitis G virus infection
    • DOI 10.2174/092986607782110239
    • M. Fernández-Vidal, M.D. Cubero, G. Ercilla, M.J. Gomara, and I. Haro I. Application of a chimeric synthetic peptide in the development of a serologic method for the diagnosis of hepatitis G virus infection Protein Pept. Lett. 14 2007 865 870 (Pubitemid 350013823)
    • (2007) Protein and Peptide Letters , vol.14 , Issue.9 , pp. 865-870
    • Fernandez-Vidal, M.1    Cubero, M.D.2    Ercilla, G.3    Gomara, M.J.4    Haro, I.5
  • 8
    • 33947583492 scopus 로고    scopus 로고
    • Synthetic peptides for the immunodiagnosis of human diseases
    • DOI 10.2174/092986707780059698
    • M.J. Gomara, and I. Haro Synthetic peptides for the immunodiagnosis of human diseases Cur Med. Chem. 14 2007 531 546 (Pubitemid 46477726)
    • (2007) Current Medicinal Chemistry , vol.14 , Issue.5 , pp. 531-546
    • Gomara, M.J.1    Haro, I.2
  • 11
    • 70350020284 scopus 로고    scopus 로고
    • GB virus type C interactions with HIV: The role of envelope glycoproteins
    • E.L. Mohr, and J.T. Stapleton GB virus type C interactions with HIV: the role of envelope glycoproteins J. Viral. Hepat. 16 2009 757 768
    • (2009) J. Viral. Hepat. , vol.16 , pp. 757-768
    • Mohr, E.L.1    Stapleton, J.T.2
  • 13
    • 67650080758 scopus 로고    scopus 로고
    • Synthetic peptides of hepatitis G virus (GBV-C/HGV) in the selection of putative peptide inhibitors of the HIV-1 fusion peptide
    • E. Herrera, M.J. Gomara, S. Mazzini, E. Ragg, and I. Haro Synthetic peptides of hepatitis G virus (GBV-C/HGV) in the selection of putative peptide inhibitors of the HIV-1 fusion peptide J. Phys. Chem. B 113 2009 7383 7391
    • (2009) J. Phys. Chem. B , vol.113 , pp. 7383-7391
    • Herrera, E.1    Gomara, M.J.2    Mazzini, S.3    Ragg, E.4    Haro, I.5
  • 14
    • 44149107774 scopus 로고    scopus 로고
    • Surface behavior and peptide-lipid interactions of the E1(3-17)R and E1(3-17)G peptides from E1 capsid protein of GBV-C/HGV virus
    • O. Fontvila, C. Mestres, M. Munoz, I. Haro, M.A. Alsina, and M. Pujol Surface behavior and peptide-lipid interactions of the E1(3-17)R and E1(3-17)G peptides from E1 capsid protein of GBV-C/HGV virus Coll. Surf. A Physicochemical Eng. Aspects 321 2008 175 180
    • (2008) Coll. Surf. A Physicochemical Eng. Aspects , vol.321 , pp. 175-180
    • Fontvila, O.1    Mestres, C.2    Munoz, M.3    Haro, I.4    Alsina, M.A.5    Pujol, M.6
  • 15
    • 62549106560 scopus 로고    scopus 로고
    • Behaviour of a peptide sequence from the GB virus C/hepatitis G virus E2 protein in Langmuir monolayers: Its interaction with phospholipid membrane models
    • S. Pérez-Lopez, M. Nieto-Suarez, C. Mestres, M.A. Alsina, I. Haro, and N. Vila-Romeu Behaviour of a peptide sequence from the GB virus C/hepatitis G virus E2 protein in Langmuir monolayers: its interaction with phospholipid membrane models Biophys. Chem. 141 2009 153 161
    • (2009) Biophys. Chem. , vol.141 , pp. 153-161
    • Pérez-Lopez, S.1    Nieto-Suarez, M.2    Mestres, C.3    Alsina, M.A.4    Haro, I.5    Vila-Romeu, N.6
  • 17
    • 77449144707 scopus 로고    scopus 로고
    • Nanoscale analysis of supported lipid bilayers using atomic force microscopy
    • K. El Kirat, S. Morandat, and Y.F. Dufrene Nanoscale analysis of supported lipid bilayers using atomic force microscopy Biochim. Biophys. Acta 1798 2010 750 765
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 750-765
    • El Kirat, K.1    Morandat, S.2    Dufrene, Y.F.3
  • 18
    • 68949173708 scopus 로고    scopus 로고
    • Interactions of oritavancin, a new lipoglycopeptide derived from vancomycin, with phospholipid bilayers: Effect on membrane permeability and nanoscale lipid membrane organization
    • O. Domenech, G. Francius, P.M. Tulkens, F. Van Bambeke, Y. Dufrêne, and M.P. Mingeot-Leclercq Interactions of oritavancin, a new lipoglycopeptide derived from vancomycin, with phospholipid bilayers: Effect on membrane permeability and nanoscale lipid membrane organization Biochim. Biophys. Acta 1788 2009 1832 1840
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1832-1840
    • Domenech, O.1    Francius, G.2    Tulkens, P.M.3    Van Bambeke, F.4    Dufrêne, Y.5    Mingeot-Leclercq, M.P.6
  • 19
    • 75649107201 scopus 로고    scopus 로고
    • Time-lapse atomic force microscopy observations of the morphology, growth rate, and spontaneous alignment of nanofibers containing a peptide-amphiphile from the hepatitis G virus (NS3 Protein)
    • K.J. Weronski, P. Cea, I. Diez-Pérez, M.A. Busquets, J. Prat, and V. Girona Time-lapse atomic force microscopy observations of the morphology, growth rate, and spontaneous alignment of nanofibers containing a peptide-amphiphile from the hepatitis G virus (NS3 Protein) J. Phys. Chem. B 114 2010 620 625
    • (2010) J. Phys. Chem. B , vol.114 , pp. 620-625
    • Weronski, K.J.1    Cea, P.2    Diez-Pérez, I.3    Busquets, M.A.4    Prat, J.5    Girona, V.6
  • 20
    • 0025050505 scopus 로고
    • Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41
    • DOI 10.1021/bi00486a020
    • M. Rafalski, J.D. Lear, and W.F. DeGrado Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41 Biochemistry 29 1990 7917 7922 (Pubitemid 20281241)
    • (1990) Biochemistry , vol.29 , Issue.34 , pp. 7917-7922
    • Rafalski, M.1    Lear, J.D.2    DeGrado, W.F.3
  • 21
    • 0037701321 scopus 로고    scopus 로고
    • Interaction of E2 and NS3 synthetic peptides of GB virus C with model lipid membranes
    • N. Rojo, M.J. Gómara, M.A. Busquets, M.A. Alsina, and I. Haro Interaction of E2 and NS3 synthetic peptides of GB virus C with model lipid membranes Talanta 60 2003 395 404
    • (2003) Talanta , vol.60 , pp. 395-404
    • Rojo, N.1    Gómara, M.J.2    Busquets, M.A.3    Alsina, M.A.4    Haro, I.5
  • 22
    • 0034681908 scopus 로고    scopus 로고
    • Designing transmembrane α-helices that insert spontaneously
    • DOI 10.1021/bi992746j
    • W.C. Wimley, and S.H. White Designing transmembrane alpha-helices that insert spontaneously Biochemistry 39 2000 4432 4442 (Pubitemid 30212660)
    • (2000) Biochemistry , vol.39 , Issue.15 , pp. 4432-4442
    • Wimley, W.C.1    White, S.H.2
  • 23
    • 33745577944 scopus 로고    scopus 로고
    • Hexapeptides that interfere with HIV-1 fusion peptide activity in liposomes block GP41-mediated membrane fusion
    • DOI 10.1016/j.febslet.2006.04.003, PII S0014579306004224
    • M.J. Gomara, M. Lorizate, N. Huarte, I. Mingarro, E. Perez-Paya, and J.L. Nieva Hexapeptides that interfere with HIV-1 fusion peptide activity in liposomes block GP41-mediated membrane fusion FEBS Lett. 580 2006 2561 2566 (Pubitemid 44294500)
    • (2006) FEBS Letters , vol.580 , Issue.11 , pp. 2561-2566
    • Gomara, M.J.1    Lorizate, M.2    Huarte, N.3    Mingarro, I.4    Perez-Paya, E.5    Nieva, J.L.6
  • 24
    • 75649122919 scopus 로고    scopus 로고
    • A Langmuir monolayer study of the interaction of E1(145-162) Hepatitis G virus peptide with phospholipid membranes
    • M.J. Sanchez-Martin, I. Haro, M.A. Alsina, M.A. Busquets, and M. Pujol A Langmuir monolayer study of the interaction of E1(145-162) Hepatitis G virus peptide with phospholipid membranes J. Phys. Chem. B 114 2010 448 456
    • (2010) J. Phys. Chem. B , vol.114 , pp. 448-456
    • Sanchez-Martin, M.J.1    Haro, I.2    Alsina, M.A.3    Busquets, M.A.4    Pujol, M.5
  • 27
    • 53849093041 scopus 로고    scopus 로고
    • Role of HIV gp41 mediated fusion/hemifusion in bystander apoptosi
    • H. Garg, and R. Blumenthal Role of HIV gp41 mediated fusion/hemifusion in bystander apoptosi Cell. Mol. Life Sci. 65 2008 3134 3144
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 3134-3144
    • Garg, H.1    Blumenthal, R.2
  • 28
    • 65249139402 scopus 로고    scopus 로고
    • Conformational stability and membrane interaction of the full-length ectodomain of HIV-1 gp41: Implication for mode of action
    • N. Lev, Y. Fridmann-Sirkis, L. Blank, A. Bitler, R.F. Epand, R.M. Epand, and Y. Shai Conformational stability and membrane interaction of the full-length ectodomain of HIV-1 gp41: implication for mode of action Biochemistry 48 2009 3166 3175
    • (2009) Biochemistry , vol.48 , pp. 3166-3175
    • Lev, N.1    Fridmann-Sirkis, Y.2    Blank, L.3    Bitler, A.4    Epand, R.F.5    Epand, R.M.6    Shai, Y.7
  • 29
    • 67349258550 scopus 로고    scopus 로고
    • Parameters modulating the maximum insertion pressure of proteins and peptides in lipid monolayers
    • P. Calvez, S. Bussières, E. Demers, and C. Salesse Parameters modulating the maximum insertion pressure of proteins and peptides in lipid monolayers Biochimie 91 2009 718 733
    • (2009) Biochimie , vol.91 , pp. 718-733
    • Calvez, P.1    Bussières, S.2    Demers, E.3    Salesse, C.4
  • 30
    • 0030606012 scopus 로고    scopus 로고
    • Lateral pressure in membranes
    • D. Marsh Lateral pressure in membranes Biochim Biophys. Acta 1286 1996 183 193
    • (1996) Biochim Biophys. Acta , vol.1286 , pp. 183-193
    • Marsh, D.1
  • 31
    • 27444434548 scopus 로고    scopus 로고
    • Interaction of a peptide derived from the N-heptad repeat region of gp41 Env ectodomain with model membranes. Modulation of phospholipid phase behavior
    • DOI 10.1021/bi050928+
    • R. Pascual, M. Contreras, A. Fedorov, M. Prieto, and J. Villalain Interaction of a peptide derived from the N-heptated repeat region of gp41 Env ectodomain with model membranes. Modulation phospholipid phase behavior Biochemistry 44 2005 14275 14288 (Pubitemid 41533052)
    • (2005) Biochemistry , vol.44 , Issue.43 , pp. 14275-14288
    • Pascual, R.1    Contreras, M.2    Fedorov, A.3    Prieto, M.4    Villalain, J.5
  • 32
    • 33646672410 scopus 로고    scopus 로고
    • The membranotropic regions of the endo and ecto domains of HIV gp41 envelope glycoprotein
    • DOI 10.1016/j.bbamem.2006.01.007, PII S0005273606000046
    • M.R. Moreno, M. Giudici, and J. Villalain The mebranotropic regions of the endo and ecto domains of HIV gp41 envelope glycoprotein Biochim. Biophys. Acta 1758 2006 111 123 (Pubitemid 44262107)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.1 , pp. 111-123
    • Moreno, M.R.1    Giudici, M.2    Villalain, J.3
  • 34
    • 77953544933 scopus 로고    scopus 로고
    • Kinetics of interaction of HIV fusion protein (gp41) with lipid membranes studied by real-time AFM imaging
    • A. Bitler, N. Lev, Y. Fridmann-Sirkis, L. Blank, S.R. Cohen, Y. Shai, and S. Yechiel Kinetics of interaction of HIV fusion protein (gp41) with lipid membranes studied by real-time AFM imaging Ultramicroscopy 110 2010 694 700
    • (2010) Ultramicroscopy , vol.110 , pp. 694-700
    • Bitler, A.1    Lev, N.2    Fridmann-Sirkis, Y.3    Blank, L.4    Cohen, S.R.5    Shai, Y.6    Yechiel, S.7
  • 35
    • 77249112159 scopus 로고    scopus 로고
    • Comparative analysis of membrane-associated fusion peptide secondary structure of HIV gp41 constructs that model the early pre-hairpin intermediate and final hairpin conformations
    • K. Sackett, M.J. Nethercott, R.F. Epand, R.M. Epand, D.R. Kindra, Y. Shai, and D.P. Keliky Comparative analysis of membrane-associated fusion peptide secondary structure of HIV gp41 constructs that model the early pre-hairpin intermediate and final hairpin conformations J. Mol. Biol. 397 2010 301 315
    • (2010) J. Mol. Biol. , vol.397 , pp. 301-315
    • Sackett, K.1    Nethercott, M.J.2    Epand, R.F.3    Epand, R.M.4    Kindra, D.R.5    Shai, Y.6    Keliky, D.P.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.