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Volumn 38, Issue 2, 2006, Pages 70-78

Anti-HIV I/II activity and molecular cloning of a novel mannose/sialic acid-binding lectin from rhizome of Polygonatum cyrtonema Hua

Author keywords

3 5 rapid amplification of cDNA ends (RACE); Anti human immunodeficiency virus (HIV) I II; Docking; Mannose binding lectin; Molecular cloning; Molecular modeling; Polygonatum cyrtonema HUA; Sequence alignment

Indexed keywords

ANTIVIRUS AGENT; COMPLEMENTARY DNA; LECTIN; LECTIN RELATED PROTEIN, POLYGONATUM; LECTIN-RELATED PROTEIN, POLYGONATUM; MANNOSE BINDING LECTIN; PLANT LECTIN; SIALIC ACID BINDING IG LIKE LECTIN; SIALIC ACID BINDING IG-LIKE LECTIN;

EID: 33644838985     PISSN: 16729145     EISSN: 17457270     Source Type: Journal    
DOI: 10.1111/j.1745-7270.2006.00140.x     Document Type: Article
Times cited : (55)

References (34)
  • 2
  • 3
    • 0032422738 scopus 로고    scopus 로고
    • Plant lectins: A composite of several distinct families of structurally and evolutionary related proteins with diverse biological roles
    • Van Damme EJ Peumans WJ Barre A Rougé P. Plant lectins: A composite of several distinct families of structurally and evolutionary related proteins with diverse biological roles Crit Rev Plant Sci 1998 17 645 662
    • (1998) Crit Rev Plant Sci , vol.17 , pp. 645-662
    • Van Damme, E.J.1    Peumans, W.J.2    Barre, A.3    Rougé, P.4
  • 4
    • 0001035146 scopus 로고
    • Isolation and characterization of a lectin with exclusively specificity toward mannose from snowdrop (Galanthus nivalis) bulbs
    • Van Damme EJ Allen AK. Isolation and characterization of a lectin with exclusively specificity toward mannose from snowdrop (Galanthus nivalis) bulbs FEBS Lett 1987 215 140 144
    • (1987) FEBS Lett , vol.215 , pp. 140-144
    • Van Damme, E.J.1    Allen, A.K.2
  • 5
    • 0030452169 scopus 로고    scopus 로고
    • Structure-function relationship of monocot mannose-binding lectins
    • Barre A Van Damme EJ Peumans WJ Rougé P. Structure-function relationship of monocot mannose-binding lectins Plant Physiol 1996 112 1531 1540
    • (1996) Plant Physiol , vol.112 , pp. 1531-1540
    • Barre, A.1    Van Damme, E.J.2    Peumans, W.J.3    Rougé, P.4
  • 6
    • 0033884824 scopus 로고    scopus 로고
    • Cloning and characterization of a monocot mannose-binding lectin from Crocus vernus (family Iridaceae)
    • Van Damme EJ Astoul CH Barre A Rougé P Peumans WJ. Cloning and characterization of a monocot mannose-binding lectin from Crocus vernus (family Iridaceae) Eur J Biochem 2000 267 5067 5077
    • (2000) Eur J Biochem , vol.267 , pp. 5067-5077
    • Van Damme, E.J.1    Astoul, C.H.2    Barre, A.3    Rougé, P.4    Peumans, W.J.5
  • 7
    • 0026020005 scopus 로고
    • α-(1-3)- and β-(1-6)-D-mannose-specific plant lectins are markedly inhibitory to human immunodeficiency virus and cytomegalovirus infections in vitro.
    • Balzarini J Schols D Neyts J Van Damme E Peumans W De Clercq E. α-(1-3)- and β-(1-6)-D-mannose-specific plant lectins are markedly inhibitory to human immunodeficiency virus and cytomegalovirus infections in vitro. Antimicrob Agents Chemother 1991 35 410 416
    • (1991) Antimicrob Agents Chemother , vol.35 , pp. 410-416
    • Balzarini, J.1    Schols, D.2    Neyts, J.3    Van Damme, E.4    Peumans, W.5    De Clercq, E.6
  • 8
    • 0025125241 scopus 로고
    • Sulphoevernan, a polyanionic polysaccharide, and the narcissus lectin potently inhibit human immunodeficiency virus infection by binding to viral envelope protein
    • Weiler BE Schroder HC Stefanovich V Stewart D Forrest JM Allen LB Bowden BJ et al. Sulphoevernan, a polyanionic polysaccharide, and the narcissus lectin potently inhibit human immunodeficiency virus infection by binding to viral envelope protein J Gen Virol 1990 71 1957 1963
    • (1990) J Gen Virol , vol.71 , pp. 1957-1963
    • Weiler, B.E.1    Schroder, H.C.2    Stefanovich, V.3    Stewart, D.4    Forrest, J.M.5    Allen, L.B.6    Bowden, B.J.7
  • 10
    • 33644838825 scopus 로고    scopus 로고
    • Purification and characterization of a lectin from Polygonatum cyrtonema Hua
    • Bao JK Zeng ZK. Purification and characterization of a lectin from Polygonatum cyrtonema Hua Eur J Cell Biol 1997 74 3
    • (1997) Eur J Cell Biol , vol.74 , pp. 3
    • Bao, J.K.1    Zeng, Z.K.2
  • 11
    • 33644847020 scopus 로고    scopus 로고
    • The effect of Polygonatum cyrtonema Hua lectin II on the transmembrane fluid of calcium on mice aorta
    • Bao JK Zeng ZK. The effect of Polygonatum cyrtonema Hua lectin II on the transmembrane fluid of calcium on mice aorta Sichuan Da Xue Xue Bao 1999 36 350 356
    • (1999) Sichuan Da Xue Xue Bao , vol.36 , pp. 350-356
    • Bao, J.K.1    Zeng, Z.K.2
  • 12
    • 33644845718 scopus 로고    scopus 로고
    • Study on molecular stability and biological activity of Polygonatum cyrtonema Hua lectin II
    • Bao JK Zeng ZK. Study on molecular stability and biological activity of Polygonatum cyrtonema Hua lectin II Sheng Wu Hua Xue Za Zhi 1996 12 747 749
    • (1996) Sheng Wu Hua Xue Za Zhi , vol.12 , pp. 747-749
    • Bao, J.K.1    Zeng, Z.K.2
  • 13
    • 18644385708 scopus 로고    scopus 로고
    • Purification and characterization of Polygonatum cyrtonema.
    • Bao JK Zeng ZK Zhou H. Purification and characterization of Polygonatum cyrtonema. Sheng Wu Hua Xue Za Zhi 1996 12 165 170
    • (1996) Sheng Wu Hua Xue Za Zhi , vol.12 , pp. 165-170
    • Bao, J.K.1    Zeng, Z.K.2    Zhou, H.3
  • 14
    • 0035282855 scopus 로고    scopus 로고
    • Sepharose-unbinding ricin e as a source for ricin Achain immunotoxin
    • Woo BH Lee JT Na DH Lee KC. Sepharose-unbinding ricin E as a source for ricin Achain immunotoxin J Immunol Methods 2001 249 91 98
    • (2001) J Immunol Methods , vol.249 , pp. 91-98
    • Woo, B.H.1    Lee, J.T.2    Na, D.H.3    Lee, K.C.4
  • 16
    • 0028355084 scopus 로고
    • Characterization and molecular cloning of mannose-binding lectins from the Orchidaceae species Listera ovata, Epipactis helleborine and Cymbidium hybrid.
    • Van Damme EJ Smeets K Torrekens S Van Leuven F Peumans WJ. Characterization and molecular cloning of mannose-binding lectins from the Orchidaceae species Listera ovata, Epipactis helleborine and Cymbidium hybrid. Eur JBiochem 1994 221 769 777
    • (1994) Eur JBiochem , vol.221 , pp. 769-777
    • Van Damme, E.J.1    Smeets, K.2    Torrekens, S.3    Van Leuven, F.4    Peumans, W.J.5
  • 17
    • 0033562977 scopus 로고    scopus 로고
    • Isolation, characterization, molecular cloning and molecular modelling of two lectins of different specificities from bluebell (Scilla campanulata) bulbs
    • Wright LM Van Damme EJ Barre A Allen AK Van Leuven F Reynolds CD Rougé P et al. Isolation, characterization, molecular cloning and molecular modelling of two lectins of different specificities from bluebell (Scilla campanulata) bulbs Biochem J 1999 340 299 308
    • (1999) Biochem J , vol.340 , pp. 299-308
    • Wright, L.M.1    Van Damme, E.J.2    Barre, A.3    Allen, A.K.4    Van Leuven, F.5    Reynolds, C.D.6    Rougé, P.7
  • 18
    • 0025979184 scopus 로고
    • 9-(2-Phosphonylmethoxyethyl)adenine (PMEA) effectively inhibits retrovirus replication in vitro and simian immunodeficiency virus infection in rhesus monkeys
    • Balzarini J Naesens L Slachmuylders J Niphuis H Rosenberg I Holy A Schellekens H et al. 9-(2-Phosphonylmethoxyethyl)adenine (PMEA) effectively inhibits retrovirus replication in vitro and simian immunodeficiency virus infection in rhesus monkeys AIDS 1991 5 21 28
    • (1991) AIDS , vol.5 , pp. 21-28
    • Balzarini, J.1    Naesens, L.2    Slachmuylders, J.3    Niphuis, H.4    Rosenberg, I.5    Holy, A.6    Schellekens, H.7
  • 19
    • 0023046815 scopus 로고
    • Anew method for predicting signal sequence cleavage sites
    • Von Heijine G. Anew method for predicting signal sequence cleavage sites Nucleic Acids Res 1986 14 4683 4690
    • (1986) Nucleic Acids Res , vol.14 , pp. 4683-4690
    • Von Heijine, G.1
  • 20
    • 0002394695 scopus 로고
    • Molecular cloning and characterization of multiple isoforms of the snowdrop (Galanthus nivalis L.) lectin
    • Van Damme EJ. Molecular cloning and characterization of multiple isoforms of the snowdrop (Galanthus nivalis L.) lectin Planta 1991 186 35 43
    • (1991) Planta , vol.186 , pp. 35-43
    • Van Damme, E.J.1
  • 21
    • 0030568976 scopus 로고    scopus 로고
    • The mannose-specific bulb lectin from Galanthus nivalis (snowdrop) binds mono and dimannosides at distinct sites. Structure analysis of refined complexes at 2.3 Å and 3.0 Å resolution
    • Hester G Wright CS. The mannose-specific bulb lectin from Galanthus nivalis (snowdrop) binds mono and dimannosides at distinct sites. Structure analysis of refined complexes at 2.3 Å and 3.0 Å resolution J Mol Biol 1996 262 516 531
    • (1996) J Mol Biol , vol.262 , pp. 516-531
    • Hester, G.1    Wright, C.S.2
  • 22
    • 0023657949 scopus 로고
    • Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences
    • Gaboriaud C Bissery V Benchetrit T Mornon JP. Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences FEBS Lett 1987 224 149 155
    • (1987) FEBS Lett , vol.224 , pp. 149-155
    • Gaboriaud, C.1    Bissery, V.2    Benchetrit, T.3    Mornon, J.P.4
  • 23
    • 0025129872 scopus 로고
    • Hydrophobic cluster analysis: Procedures to derive structural and functional information from 2-D-representation of protein sequences
    • Lemesle-Varloot L Henrissat B Gaboriaud C Bissery V Morgat A Mornon JP. Hydrophobic cluster analysis: procedures to derive structural and functional information from 2-D-representation of protein sequences Biochimie 1990 72 555 574
    • (1990) Biochimie , vol.72 , pp. 555-574
    • Lemesle-Varloot, L.1    Henrissat, B.2    Gaboriaud, C.3    Bissery, V.4    Morgat, A.5    Mornon, J.P.6
  • 24
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede T Kopp J Guex N Peitsch MC. SWISS-MODEL: An automated protein homology-modeling server Nucleic Acids Res 2003 31 3381 3385
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 25
    • 0029008975 scopus 로고
    • Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family
    • Hester G Kaku H Goldstein IJ Wright CS. Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family Nat Struct Biol 1995 2 472 479
    • (1995) Nat Struct Biol , vol.2 , pp. 472-479
    • Hester, G.1    Kaku, H.2    Goldstein, I.J.3    Wright, C.S.4
  • 27
    • 0023133752 scopus 로고
    • Potential secondary structure at translation-initiation sites
    • Ganoza MC Kofoid EC Marliere P. Potential secondary structure at translation-initiation sites Nucleic Acids Res 1987 15 345 360
    • (1987) Nucleic Acids Res , vol.15 , pp. 345-360
    • Ganoza, M.C.1    Kofoid, E.C.2    Marliere, P.3
  • 29
    • 4644227155 scopus 로고    scopus 로고
    • Mannose-specific plant lectins from the Amaryllidaceae family qualify as efficient microbicides for prevention of human immunodeficiency virus infection
    • Balzarini J Hatse S Vermeire K Princen K Aquaro S Perno CF Clercq ED et al. Mannose-specific plant lectins from the Amaryllidaceae family qualify as efficient microbicides for prevention of human immunodeficiency virus infection Antimicrob Agents Chemother 2004 48 3858 3870
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 3858-3870
    • Balzarini, J.1    Hatse, S.2    Vermeire, K.3    Princen, K.4    Aquaro, S.5    Perno, C.F.6    Clercq, E.D.7
  • 30
    • 5444248711 scopus 로고    scopus 로고
    • Mannose binding lectin (MBL) and HIV
    • Ji X Gewurz H Spear GT. Mannose binding lectin (MBL) and HIV Mol Immunol 2005 42 145 152
    • (2005) Mol Immunol , vol.42 , pp. 145-152
    • Ji, X.1    Gewurz, H.2    Spear, G.T.3
  • 31
    • 0028095106 scopus 로고
    • Lectins in AIDS research
    • Favero J. Lectins in AIDS research Glycobiology 1994 4 387 396
    • (1994) Glycobiology , vol.4 , pp. 387-396
    • Favero, J.1
  • 32
    • 0025292252 scopus 로고
    • Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells
    • Leonard CK Spellman MW Riddle L Harris RJ Thomas JN Gregory TJ. Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells J Biol Chem 1990 265 10373 10382
    • (1990) J Biol Chem , vol.265 , pp. 10373-10382
    • Leonard, C.K.1    Spellman, M.W.2    Riddle, L.3    Harris, R.J.4    Thomas, J.N.5    Gregory, T.J.6


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