The Novel Fold of Scytovirin Reveals a New Twist For Antiviral Entry Inhibitors

Journal of Molecular Biology

Volumn 369, Issue 2, 2007, Pages 451-461

  McFeeters, Robert L ^a   Xiong, Changyun ^a   O'Keefe, Barry R ^a   Bokesch, Heidi R ^a,b   McMahon, James B ^a   Ratner, Daniel M ^c   Castelli, Riccardo ^d   Seeberger, Peter H ^d   Byrd, R Andrew ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

^b SAIC FREDERICK INC   (United States)

^c MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^d ETH ZURICH   (Switzerland)

Author keywords

antiviral; carbohydrate; hevein; HIV; scytovirin

Indexed keywords

AMINO ACID; BINDING PROTEIN; CARBOHYDRATE BINDING PROTEIN; CHITIN; PROTEIN DERIVATIVE; SCYTOVIRIN; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; CYANOBACTERIUM; DISULFIDE BOND; HUMAN IMMUNODEFICIENCY VIRUS 1 INFECTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; VIRUS INHIBITION;

SCYTONEMA;

EID: 34247563359     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.03.030     Document Type: Article

References (27)

1. Boraston A.B., Bolam D.N., Gilbert H.J., and Davies G.J. Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem. J. 382 (2004) 769-781
2. Rodriguez-Romero A., Ravichandran K.G., and Soriano-Garcia M. Crystal structure of hevein at 2.8 A resolution. FEBS Letters 291 (1991) 307-309
3. Charan R.D., Munro M.H., O'Keefe B.R., Sowder R., McKee T.C., Currens M.J., et al. Isolation and characterization of Myrianthus holstii lectin, a potent HIV-1 inhibitory protein from the plant Myrianthus holstii(1). J. Nat. Products 63 (2000) 1170-1174
4. Bokesch H.R., O'keefe B.R., McKee T.C., Pannell L.K., Patterson G.M., Gardella R.S., et al. A potent novel anti-HIV protein from the cultured cyanobacterium Scytonema varium. Biochemistry 42 (2003) 2578-2584
5. Peumans W.J., Rouge P., and Van Damme E.J. The tomato lectin consists of two homologous chitin-binding modules separated by an extensin-like linker. Biochem. J. 376 (2003) 717-724
6. Stoeva S., Franz M., Wacker R., Krauspenhaar R., Guthohrlein E., Mikhailov A., et al. Primary structure, isoforms, and molecular modeling of a chitin-binding mistletoe lectin. Arch. Biochem. Biophys. 392 (2001) 23-31
7. Adams E.W., Ratner D.M., Bokesch H.R., McMahon J.B., O'Keefe B.R., and Seeberger P.H. Oligosaccharide and glycoprotein microarrays as tools in HIV glycobiology; glycan-dependent gp120/protein interactions. [see comment]. Chem. Biol. 11 (2004) 875-881
8. Asensio J.L., Canada F.J., Siebert H.C., Laynez J., Poveda A., Nieto P.M., et al. Structural basis for chitin recognition by defense proteins: GlcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domains. Chem. Biol. 7 (2000) 529-543
9. Ikura M., Bax A., Clore G.M., and Gronenborn A.M. Detection of nuclear Overhauser effects between degenerate amid proton resonances by heteronuclear three-dimensional NMR spectroscopy. J. Am. Chem. Soc. 112 (1990) 9020-9022
10. 15N-correlations to link sequential neighbors of prolines. J. Biomol. NMR 17 (2000) 331-335
11. 13C chemical-shift data. J. Biomol. NMR 4 (1994) 171-180
12. Wishart D.S., Sykes B.D., and Richards F.M. The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31 (1992) 1647-1651
13. McFeeters R.L., Fowler C.A., Gaponenko V.V., and Byrd R.A. Efficient and precise measurement of H(alpha)-C(alpha), C(alpha)-C′, C(alpha)-C(beta) and H(N)-N residual dipolar couplings from 2D H(N)-N correlation spectra. J. Biomol. NMR 31 (2005) 35-47
14. Cierpicki T., Zhukov I., Byrd R.A., and Otlewski J. Hydrogen bonds in human ubiquitin reflected in temperature coefficients of amide protons. J. Magn. Reson. 157 (2002) 178-180
15. Holm L., and Sander C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233 (1993) 123-138
16. 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry 28 (1991) 8972-8979
17. Xiong C., O'Keefe B.R., Byrd R.A., and McMahon J.B. Potent anti-HIV activity of scytovirin domain 1 peptide. Peptides 27 (2006) 1668-1675
18. Chavez M.I., Andreu C., Vidal P., Aboitiz N., Freire F., Canada F.J., and Jimenez-Barbero J. On the importance of carbohydrate-aromatic interaction for the molecular recognition of oligosaccharides by proteins: NMR studies of the structure and binding affinity of AcAMP2-like peptides with non-natural naphtyyl and fluoroaromatic residues. Chem. Eur. J. 11 (2005) 7060-7074
19. Barrientos L.G., Matei E., Lasala F., Delgado R., and Gronenborn A.M. Dissecting carbohydrate-Cyanovirin-N binding by structure-guided mutagenesis: functional implications for viral entry inhibition. Protein Eng. Des. Select. 19 (2006) 525-535
20. Bewley C.A., and Otero-Quintero S. The potent anti-HIV protein cyanovirin-N contains two novel carbohydrate binding sites that selectively bind to Man(8) D1D3 and Man(9) with nanomolar affinity: implications for binding to the HIV envelope protein gp120. J. Am. Chem. Soc. 123 (2001) 3892-3902
21. Botos I., O'Keefe B.R., Shenoy S.R., Cartner L.K., Ratner D.M., Seeberger P.H., et al. Structures of the complexes of a potent anti-HIV protein cyanovirin-N and high mannose oligosaccharides. J. Biol. Chem. 277 (2002) 34336-34342
22. Xiong C., O'keefe B.R., Botos I., Wlodawer A., and McMahon J.B. Overexpression and purification of scytovirin, a potent, novel anti-HIV protein from the cultured cyanobacterium Scytonema varium. Protein Expr. Purif. 46 (2006) 233-239
23. Delaglio F., Grzesiek S., Vuister G.W., Zhu G., Pfeifer J., and Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. [see comment]. J. Biomol. NMR 6 (1995) 277-293
24. Goddard T.D., and Kneller D.G. SPARKY 3 (0000), University of California, San Francisco
25. Schwieters C.D., Kuszewski J.J., Tjandra N., and Clore G.M. The Xplor-NIH NMR molecular structure determination package. J. Magn. Reson. 160 (2003) 65-73
26. Plante O.J., Buchwald S.L., and Seeberger P.H. Halobenzyl ethers as protecting groups for organic synthesis. J. Am. Chem. Soc. 122 (2000) 7148-7149
27. Ratner D.M., Plante O.J., and Seeberger P.H. A linear synthesis of branched high-mannose oligosaccharides from the HIV-1 viral surface envelope glycoprotein gp120. Eur. J. Org. Chem. 5 (2002) 826-833