메뉴 건너뛰기




Volumn 174, Issue 1, 2011, Pages 164-172

Structural characterization and anti-HIV-1 activities of arginine/glutamate-rich polypeptide Luffin P1 from the seeds of sponge gourd (Luffa cylindrica)

Author keywords

Anti HIV 1; Luffin P1; Nuclear magnetic resonance; Ribosome inactivating peptide

Indexed keywords

GLYCOSIDASE; LUFFIN P1; RIBOSOME INACTIVATING PROTEIN; UNCLASSIFIED DRUG;

EID: 79952450056     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2010.12.007     Document Type: Article
Times cited : (53)

References (40)
  • 1
    • 0034646833 scopus 로고    scopus 로고
    • The plant ribosome inactivating proteins luffin and saporin are potent inhibitors of HIV-1 integrase
    • Au T.K., Collins R.A., Lam T.L., Ng T.B., Fong W.P., Wan D.C.C. The plant ribosome inactivating proteins luffin and saporin are potent inhibitors of HIV-1 integrase. FEBS Lett. 2000, 471:169-172.
    • (2000) FEBS Lett. , vol.471 , pp. 169-172
    • Au, T.K.1    Collins, R.A.2    Lam, T.L.3    Ng, T.B.4    Fong, W.P.5    Wan, D.C.C.6
  • 2
    • 0020261430 scopus 로고
    • Ribosome-inactivating proteins from plants: properties and possible uses
    • Barbieri L., Stirpe F. Ribosome-inactivating proteins from plants: properties and possible uses. Cancer Surv. 1982, 1:489-520.
    • (1982) Cancer Surv. , vol.1 , pp. 489-520
    • Barbieri, L.1    Stirpe, F.2
  • 3
    • 0026815648 scopus 로고
    • A maize ribosome-inactivating protein is controlled by the transcriptional activator opaque-2
    • Bass H.W., Webster C., OBrian G.R., Roberts J.K., Boston R.S. A maize ribosome-inactivating protein is controlled by the transcriptional activator opaque-2. Plant Cell 1992, 4:225-234.
    • (1992) Plant Cell , vol.4 , pp. 225-234
    • Bass, H.W.1    Webster, C.2    OBrian, G.R.3    Roberts, J.K.4    Boston, R.S.5
  • 5
    • 0023733039 scopus 로고
    • Ribosome-inactivating proteins from plants inhibit ribosome activity of Trypanosoma and Leishmania
    • Cenini P., Bolognesi A., Stirpe F. Ribosome-inactivating proteins from plants inhibit ribosome activity of Trypanosoma and Leishmania. J. Protozool. 1988, 35:384-387.
    • (1988) J. Protozool. , vol.35 , pp. 384-387
    • Cenini, P.1    Bolognesi, A.2    Stirpe, F.3
  • 6
    • 34948872162 scopus 로고    scopus 로고
    • An unusual helix-turn-helix protease inhibitory motif in a novel trypsin inhibitor from seeds of Veronica (Veronica hederifolia L.)
    • Conners R., Konarev A.V., Forsyth J., Lovegrove A., Marsh J., Joseph-Horne T., Shewry P., Brady R.L. An unusual helix-turn-helix protease inhibitory motif in a novel trypsin inhibitor from seeds of Veronica (Veronica hederifolia L.). J. Biol. Chem. 2007, 282:27760-27768.
    • (2007) J. Biol. Chem. , vol.282 , pp. 27760-27768
    • Conners, R.1    Konarev, A.V.2    Forsyth, J.3    Lovegrove, A.4    Marsh, J.5    Joseph-Horne, T.6    Shewry, P.7    Brady, R.L.8
  • 7
    • 0027981916 scopus 로고
    • Evidence that HIV-1 Rev directly promotes the nuclear export of unspliced RNA
    • Fischer U., Meyer S., Teufel M., Heckel C., Luhrmann R., Rautmann G. Evidence that HIV-1 Rev directly promotes the nuclear export of unspliced RNA. EMBO J. 1994, 13:4105-4112.
    • (1994) EMBO J. , vol.13 , pp. 4105-4112
    • Fischer, U.1    Meyer, S.2    Teufel, M.3    Heckel, C.4    Luhrmann, R.5    Rautmann, G.6
  • 8
    • 0028236694 scopus 로고
    • Luffin-S - a small novel ribosome-inactivating protein from Luffa cylindrica. Characterization and mechanism studies
    • Gao W.D., Ling J., Zhong X.M., Liu W.Y., Zhang R.P., Yang H.L., Cao H.T., Zhang Z.C. Luffin-S - a small novel ribosome-inactivating protein from Luffa cylindrica. Characterization and mechanism studies. FEBS Lett. 1994, 347:257-260.
    • (1994) FEBS Lett. , vol.347 , pp. 257-260
    • Gao, W.D.1    Ling, J.2    Zhong, X.M.3    Liu, W.Y.4    Zhang, R.P.5    Yang, H.L.6    Cao, H.T.7    Zhang, Z.C.8
  • 9
    • 3042613317 scopus 로고    scopus 로고
    • Description, distribution, activity and phylogenetic relationship of ribosome-inactivating proteins in plants, fungi and bacteria
    • Girbes T., Ferreras J.M., Arias F.J., Stirpe F. Description, distribution, activity and phylogenetic relationship of ribosome-inactivating proteins in plants, fungi and bacteria. Mini-Rev. Med. Chem. 2004, 4:461-476.
    • (2004) Mini-Rev. Med. Chem. , vol.4 , pp. 461-476
    • Girbes, T.1    Ferreras, J.M.2    Arias, F.J.3    Stirpe, F.4
  • 10
    • 4344698912 scopus 로고    scopus 로고
    • Automated NMR protein structure calculation
    • Guntert P. Automated NMR protein structure calculation. Prog. Nucl. Magn. Reson. Spectrosc. 2003, 43:105-125.
    • (2003) Prog. Nucl. Magn. Reson. Spectrosc. , vol.43 , pp. 105-125
    • Guntert, P.1
  • 12
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann T., Guntert P., Wuthrich K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J. Mol. Biol. 2002, 319:209-227.
    • (2002) J. Mol. Biol. , vol.319 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 13
    • 0033824470 scopus 로고    scopus 로고
    • DALILITE workbench for protein structure comparison
    • Holm L., Park J. DALILITE workbench for protein structure comparison. Bioinformatics 2000, 16:566-567.
    • (2000) Bioinformatics , vol.16 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 15
    • 0030900582 scopus 로고    scopus 로고
    • Isolation and molecular characterization of four arginine/glutamate rich polypeptides from the seeds of sponge gourd (Luffa cylindrica)
    • Ishihara H., Sasagawa T., Sakai R., Nishikawa M., Kimura M., Funatsu G. Isolation and molecular characterization of four arginine/glutamate rich polypeptides from the seeds of sponge gourd (Luffa cylindrica). Biosci. Biotechnol. Biochim. 1997, 61:168-170.
    • (1997) Biosci. Biotechnol. Biochim. , vol.61 , pp. 168-170
    • Ishihara, H.1    Sasagawa, T.2    Sakai, R.3    Nishikawa, M.4    Kimura, M.5    Funatsu, G.6
  • 16
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure - pattern-recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure - pattern-recognition of hydrogen-bonded and geometrical features. Biopolymers 1983, 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 17
    • 0031171842 scopus 로고    scopus 로고
    • Primary structure of 6.5k-arginine/glutamate-rich polypeptide from the seeds of sponge gourd (Luffa cylindrica)
    • Kimura M., Park S.S., Sakai R., Yamasaki N., Funatsu G. Primary structure of 6.5k-arginine/glutamate-rich polypeptide from the seeds of sponge gourd (Luffa cylindrica). Biosci. Biotechnol. Biochem. 1997, 61:984-988.
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 984-988
    • Kimura, M.1    Park, S.S.2    Sakai, R.3    Yamasaki, N.4    Funatsu, G.5
  • 18
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 1996, 14(51-55):29-32.
    • (1996) J. Mol. Graphics , vol.14 , Issue.51-55 , pp. 29-32
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 19
    • 34548348189 scopus 로고    scopus 로고
    • Evidence for the importance of electrostatics in the function of two distinct families of ribosome inactivating toxins
    • Korennykh A.V., Correll C.C., Piccirilli J.A. Evidence for the importance of electrostatics in the function of two distinct families of ribosome inactivating toxins. RNA 2007, 13:1391-1396.
    • (2007) RNA , vol.13 , pp. 1391-1396
    • Korennykh, A.V.1    Correll, C.C.2    Piccirilli, J.A.3
  • 20
  • 21
    • 78049396486 scopus 로고    scopus 로고
    • A switch-on mechanism to activate maize ribosome-inactivating protein for targeting HIV-infected cells
    • Law S.K., Wang R.R., Mak A.N., Wong K.B., Zheng Y.T., Shaw P.C. A switch-on mechanism to activate maize ribosome-inactivating protein for targeting HIV-infected cells. Nucleic Acids Res. 2010, 38:6803-6812.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 6803-6812
    • Law, S.K.1    Wang, R.R.2    Mak, A.N.3    Wong, K.B.4    Zheng, Y.T.5    Shaw, P.C.6
  • 22
    • 0042978485 scopus 로고    scopus 로고
    • Purification and characterization of Luffin P1, a ribosome-inactivating peptide from the seeds of Luffa cylindrica
    • Li F., Yang X.X., Xia H.C., Zeng R., Hu W.G., Li Z., Zhang Z.C. Purification and characterization of Luffin P1, a ribosome-inactivating peptide from the seeds of Luffa cylindrica. Peptides 2003, 24:799-805.
    • (2003) Peptides , vol.24 , pp. 799-805
    • Li, F.1    Yang, X.X.2    Xia, H.C.3    Zeng, R.4    Hu, W.G.5    Li, Z.6    Zhang, Z.C.7
  • 23
    • 35548984395 scopus 로고    scopus 로고
    • Structure-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active site
    • Mak A.N.S., Wong Y.T., An Y.J., Cha S.S., Sze K.H., Au S.W.N., Wong K.B., Shaw P.C. Structure-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active site. Nucleic Acids Res. 2007, 35:6259-6267.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 6259-6267
    • Mak, A.N.S.1    Wong, Y.T.2    An, Y.J.3    Cha, S.S.4    Sze, K.H.5    Au, S.W.N.6    Wong, K.B.7    Shaw, P.C.8
  • 24
    • 0025190644 scopus 로고
    • HIV-1 structural gene-expression requires binding of the Rev trans-activator to its RNA target sequence
    • Malim M.H., Tiley L.S., Mccarn D.F., Rusche J.R., Hauber J., Cullen B.R. HIV-1 structural gene-expression requires binding of the Rev trans-activator to its RNA target sequence. Cell 1990, 60:675-683.
    • (1990) Cell , vol.60 , pp. 675-683
    • Malim, M.H.1    Tiley, L.S.2    Mccarn, D.F.3    Rusche, J.R.4    Hauber, J.5    Cullen, B.R.6
  • 25
    • 0036422777 scopus 로고    scopus 로고
    • Purification and characterization of moschins, arginine-glutamate-rich proteins with translation-inhibiting activity from brown pumpkin (Cucurbita moschata) seeds
    • Ng T.B., Parkash A., Tso W.W. Purification and characterization of moschins, arginine-glutamate-rich proteins with translation-inhibiting activity from brown pumpkin (Cucurbita moschata) seeds. Protein Express. Purif. 2002, 26:9-13.
    • (2002) Protein Express. Purif. , vol.26 , pp. 9-13
    • Ng, T.B.1    Parkash, A.2    Tso, W.W.3
  • 26
    • 0022529307 scopus 로고
    • Reduced turnover of the elongation-factor EF-1 ribosome complex after treatment with the protein-synthesis inhibitor II from barley-seeds
    • Nilsson L., Asano K., Svensson B., Poulsen F.M., Nygard O. Reduced turnover of the elongation-factor EF-1 ribosome complex after treatment with the protein-synthesis inhibitor II from barley-seeds. Biochim. Biophys. Acta 1986, 868:62-70.
    • (1986) Biochim. Biophys. Acta , vol.868 , pp. 62-70
    • Nilsson, L.1    Asano, K.2    Svensson, B.3    Poulsen, F.M.4    Nygard, O.5
  • 28
    • 0035996833 scopus 로고    scopus 로고
    • Isolation and characterization of luffacylin, a ribosome inactivating peptide with anti-fungal activity from sponge gourd (Luffa cylindrica) seeds
    • Parkash A., Ng T.B., Tso W.W. Isolation and characterization of luffacylin, a ribosome inactivating peptide with anti-fungal activity from sponge gourd (Luffa cylindrica) seeds. Peptides 2002, 23:1019-1024.
    • (2002) Peptides , vol.23 , pp. 1019-1024
    • Parkash, A.1    Ng, T.B.2    Tso, W.W.3
  • 29
    • 0030569510 scopus 로고    scopus 로고
    • Characterization of the enzymatic mechanism of gamma-momorcharin, a novel ribosome-inactivating protein with lower molecular weight of 11,500 purified from the seeds of bitter gourd (Momordica charantia)
    • Pu Z., Lu B.Y., Liu W.Y., Jin S.W. Characterization of the enzymatic mechanism of gamma-momorcharin, a novel ribosome-inactivating protein with lower molecular weight of 11,500 purified from the seeds of bitter gourd (Momordica charantia). Biochem. Biophys. Res. Commun. 1996, 229:287-294.
    • (1996) Biochem. Biophys. Res. Commun. , vol.229 , pp. 287-294
    • Pu, Z.1    Lu, B.Y.2    Liu, W.Y.3    Jin, S.W.4
  • 30
    • 3042658236 scopus 로고    scopus 로고
    • The structure of ribosome inactivating proteins
    • Robertus J.D., Monzingo A.F. The structure of ribosome inactivating proteins. Mini-Rev. Med. Chem. 2004, 4:477-486.
    • (2004) Mini-Rev. Med. Chem. , vol.4 , pp. 477-486
    • Robertus, J.D.1    Monzingo, A.F.2
  • 31
    • 15944368960 scopus 로고    scopus 로고
    • Recent advances in trichosanthin, a ribosome-inactivating protein with multiple pharmacological properties
    • Shaw P.C., Lee K.M., Wong K.B. Recent advances in trichosanthin, a ribosome-inactivating protein with multiple pharmacological properties. Toxicon 2005, 45:683-689.
    • (2005) Toxicon , vol.45 , pp. 683-689
    • Shaw, P.C.1    Lee, K.M.2    Wong, K.B.3
  • 32
    • 0033042935 scopus 로고    scopus 로고
    • Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy
    • Sreerama N., Venyaminov S.Y., Woody R.W. Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy. Protein Sci. 1999, 8:370-380.
    • (1999) Protein Sci. , vol.8 , pp. 370-380
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 34
    • 1942484412 scopus 로고    scopus 로고
    • Site-directed PEGylation of trichosanthin retained its anti-HIV activity with reduced potency in vitro
    • Wang J.H., Tam S.C., Huang H., Ouyang D.Y., Wang Y.Y., Zheng Y.T. Site-directed PEGylation of trichosanthin retained its anti-HIV activity with reduced potency in vitro. Biochem. Biophys. Res. Commun. 2004, 317:965-971.
    • (2004) Biochem. Biophys. Res. Commun. , vol.317 , pp. 965-971
    • Wang, J.H.1    Tam, S.C.2    Huang, H.3    Ouyang, D.Y.4    Wang, Y.Y.5    Zheng, Y.T.6
  • 35
    • 77953487616 scopus 로고    scopus 로고
    • A novel recombinant immunotoxin with the smallest ribosome-inactivating protein luffin p1: T-cell cytotoxicity and prolongation of allograft survival
    • Wang R.P., Gan C.J., Gao W.D., He W.F., Wang X.J., Peng Y.M., Zhuo J.Y., Tan J.L., Peng X., Wu J., Luo G.X. A novel recombinant immunotoxin with the smallest ribosome-inactivating protein luffin p1: T-cell cytotoxicity and prolongation of allograft survival. J. Cell Mol. Med. 2010, 14:578-586.
    • (2010) J. Cell Mol. Med. , vol.14 , pp. 578-586
    • Wang, R.P.1    Gan, C.J.2    Gao, W.D.3    He, W.F.4    Wang, X.J.5    Peng, Y.M.6    Zhuo, J.Y.7    Tan, J.L.8    Peng, X.9    Wu, J.10    Luo, G.X.11
  • 36
    • 0025473661 scopus 로고
    • Isolation and partial characterization of 3 protein-synthesis inhibitory proteins from the seeds of Luffa cylindrica
    • Watanabe K., Minami Y., Funatsu G. Isolation and partial characterization of 3 protein-synthesis inhibitory proteins from the seeds of Luffa cylindrica. Agric. Biol. Chem. Tokyo 1990, 54:2085-2092.
    • (1990) Agric. Biol. Chem. Tokyo , vol.54 , pp. 2085-2092
    • Watanabe, K.1    Minami, Y.2    Funatsu, G.3
  • 37
    • 0030571043 scopus 로고    scopus 로고
    • Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions
    • Wen J., Arakawa T., Philo J.S. Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions. Anal. Biochem. 1996, 240:155-166.
    • (1996) Anal. Biochem. , vol.240 , pp. 155-166
    • Wen, J.1    Arakawa, T.2    Philo, J.S.3
  • 39
    • 73649148999 scopus 로고    scopus 로고
    • Solution structure of an active mutant of maize ribosome-inactivating protein (MOD) and its interaction with the ribosomal stalk protein P2
    • Yang Y.H., Mak A.N.S., Shaw P.C., Sze K.H. Solution structure of an active mutant of maize ribosome-inactivating protein (MOD) and its interaction with the ribosomal stalk protein P2. J. Mol. Biol. 2010, 395:897-907.
    • (2010) J. Mol. Biol. , vol.395 , pp. 897-907
    • Yang, Y.H.1    Mak, A.N.S.2    Shaw, P.C.3    Sze, K.H.4
  • 40
    • 77953155887 scopus 로고    scopus 로고
    • Trichosanthin inhibits integration of human immunodeficiency virus type 1 through depurinating the long-terminal repeats
    • Zhao W.L., Feng D., Wu J., Sui S.F. Trichosanthin inhibits integration of human immunodeficiency virus type 1 through depurinating the long-terminal repeats. Mol. Biol. Rep. 2010, 37:2093-2098.
    • (2010) Mol. Biol. Rep. , vol.37 , pp. 2093-2098
    • Zhao, W.L.1    Feng, D.2    Wu, J.3    Sui, S.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.