Structure and mechanism of a transmission blocking vaccine candidate protein Pfs25 from P. falciparum: A molecular modeling and docking study

In Silico Biology

Volumn 8, Issue 3-4, 2008, Pages 193-206

  Sharma, Babita ^a  

^a JAWAHARLAL NEHRU UNIVERSITY   (India)

Author keywords

Docking; EGF domain; GPI anchor; Homology modeling; Pfs25

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR 3; LAMININ; MEMBRANE PROTEIN; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 4B7; PROTEIN P25; PROTEIN PFS25; PROTEIN PVS25; PROTOZOAL PROTEIN; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; HEAVY CHAIN; HOST PARASITE INTERACTION; HYDROGEN BOND; MALARIA; MOLECULAR DOCKING; MOLECULAR MODEL; NONHUMAN; PARASITE TRANSMISSION; PLASMODIUM FALCIPARUM; PLASMODIUM VIVAX; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES, MONOCLONAL; ANTIBODIES, PROTOZOAN; COMPUTATIONAL BIOLOGY; COMPUTER SIMULATION; IMMUNOGLOBULIN VARIABLE REGION; MALARIA VACCINES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTOZOAN PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 53249090374     PISSN: 13866338     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (50)

1. World Malaria Report (2005). Geneva. RBM/WHO/UNICEF.
2. UN Millennium Project. Coming to Grips with Malaria in the New Millennium (2005). Task Force on HIV/AIDS, Malaria, TB, and Access to Essential Medicines, Working Group on Malaria.
3. Kumar. N. and Carter, R. (1985). Biosynthesis of two stage-specific membrane proteins during transformation of Plasmodium gallinaceum zygotes into ookinetes. Mol. Biocbem. Parasitol. 14, 127-139.
4. Vermeulen, A. N., Ponnudurai, T., Beckers, P. J. A., Verhave, J. P., Smits, M. A. and Meuwissen, J. H. E. T. (1985). Sequential expression of antigens on sexual stages of Plasmodium falciparum accessible to transmission blocking antibodies in the mosquito. J. Exp. Med. 162 1460-1476.
5. Paton, M. G., Barker, G. C., Matsuoka, H., Ramesar, J., Janse C. J., Waters, A. P. and Sinden, R. E. (1993). Structure and expression of a post-transcriptionally regulated malaria gene encoding a surface protein from the sexual stages of Plasmodium berghei. Mol. Biochem. Parasitol. 59, 263-275.
6. Fries, H. C., Lamers, M. B., Van Deursen, J., Ponnudurai, T. and Meuwissen, J. H. (1990). Biosynthesis of the 25-kDa protein in the macrogametes/zygotes of Plasmodium falciparum. Exp. Parasitol. 71, 229-235.
7. Winger, L. A., Tirawanchai, N., Nicholas, N. J., Carter, H. E., Smith, J. E. and Sinden, R. E. (1988). Ookinete antigens of Plasmodium berghei. Appearance on the zygote surface of an Mr 21 kD determinant identified by transmission-blocking monoclonal antibodies. Parasite Immunol. 10 193-207.
8. Sinden, R. E.,Winger, L., Carter, E. H., Hartley, R. H., Tirawanchai, N., Davies, C. S., Moore, J. and Sluiters J. F. (1987). Ookinete antigens of Plasmodium berghei: A light and electron-microscope immunogold study of expression of the 21 kDa determinant recognized by a transmission-blocking antibody. Proc. R. Soc. Lond. B. Biol. Sci. 230 443-458.
9. Duffy, P. E., Pimenta, P. and Kaslow, D. C. (1993). Pgs28 belongs to a family of epidermal growth factor-like antigens that are targets of malaria transmission-blocking antibodies. J. Exp. Med. 177, 505-510.
10. Tomas, A. M., Margos, G., Dimopoulos, G., Van Lin, L. H., de Koning-Ward, T. F., Sinha, R., Lupetti, P., Beetsma, A. L., Rodriguez, M. C., Karras, M., Hager, A., Mendoza, J., Butcher, G. A., Kafatos, F., Janse, C. J., Waters, A. P. and Sinden, R. E. (2001). P25 and P28 proteins of the malaria ookinete surface have multiple and partially redundant functions. EMBO J. 20, 3975-3983.
11. Kaslow, D. C., Quakyi, I. A., Syin, C., Raum, M. G., Keister, D. B., Coligan, J. E., McCutchan, T. F. and Miller, L. H. (1988). A vaccine candidate from the sexual stage of human malaria that contains EGF-like domains. Nature 333, 74-76.
12. Tsuboi, T., Kaslow, D. C., Gozar, M. M., Tachibana, M., Cao, Y. M. and Torii, M. (1998). Sequence polymorphism in two novel Plasmodium vivax ookinete surface proteins, Pvs25 and Pvs28 that are malaria transmission-blocking vaccine candidates. Mol. Med. 4, 772-782.
13. Appella, E., Weber, I. T. and Blasi, F. (1988). Structure and function of epidermal growth factor like regions in proteins. FEBS Lett. 231 1-4.
14. Carter, R., Graves, P. M., Quakyi, I. A. and Good, M. F. (1989). Restricted or absent immune responses in human populations to Plasmodium falciparum gamete antigens that are targets of malaria transmission blocking antibodies. J. Exp. Med. 169, 135-147.
15. Coban, C., Philipp, M. T., Purcell, J. E., Keister, D. B., Okulate, M., Martin, D. S. and Kumar, N. (2004). Induction of Plasmodium falciparum transmission-blocking antibodies in nonhuman primates by a combination of DNA and protein immunizations. Infect. Immun. 72, 253-259.
16. Kaslow, D. C. (1996). Transmission-Blocking Vaccine. In: Hoffman, S. L. (Ed.), Malaria Vaccine Development: A Multi-Immune Response Approach. American Society for Microbiology, Washington, DC. 181-227.
17. Malkin, E. M., Durbin, A. P., Diemert, D. J., Sattabongkot, J., Wu, Y., Miura, K., Long, C. A., Lambert, L., Miles, A. P., Wang, J., Stowers, A., Miller, L. H. and Saul, A. (2005). Phase 1 vaccine trial of Pvs25: A transmission blocking vaccine for Plasmodium vivax malaria. Vaccine 23, 3131-3138.
18. Han, Y. S., Thompson, J., Kafatos, F. C. and Barillas-Mury, C. (2000). Molecular interactions between Anopheles stephensi midgut cells and Plasmodium berghei: The time bomb theory of ookinete invasion of mosquitos. EMBO J. 19, 6030-6040.
19. Tsuboi, T., Cao, Y. M., Hitsumoto, Y., Yanagi, T., Kanbara, H. and Torii, M. (1997). Two antigens on zygotes and ookinetes of Plasmodium yoelii and Plasmodium berghei that are distinct targets of transmission blocking immunity. Infect. Immun. 65, 2260-2264.
20. Yoshida, S., Matsuoka, H., Luo, E., Iwai, K., Arai, M., Sinden, R. E. and Ishii, A. (1999). A single-chain antibody fragment specific for the Plasmodium berghei ookinete protein Pbs21 confers transmission blockade in the mosquito midgut. Mol. Biochem. Parasitol. 104, 195-204.
21. Sivasubramanian, A., Chao, G., Pressler, H. M., Wittrup, K. D. and Gray, J. J. (2006). Structural model of the mAb 806-EGFR complex using computational docking followed by computational and experimental mutagenesis. Structure 14, 401-414.
22. Gray, J. J. (2006). High resolution protein-protein docking. Curr. Opin. Struct. Biol. 16, 183-193.
23. Wiehe, K., Pierce, B., Mintseris, J., Tong, W. W., Anderson, R., Chen, R. and Weng, Z. (2005). ZDOCK and RDOCK performance in CAPRI rounds 3, 4, and 5. Proteins 60, 207-213.
24. Gasteiger, E., Gattiker, A., Hoogland, C., Ivanyi, I., Appel, R. D. and Bairoch, A. (2003). ExPASy: The proteomics server for in-depth protein knowledge and analysis. Nucleic Acids Res. 31, 3784-3788.
25. Altschul, S. F., Gish, W., Miller, W., Myers, E. W. and Lipman, D. J. (1990). Basic local alignment search tool. J. Mol. Biol. 215, 403-410.
26. Berman, H. M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T. N., Weissig, H., Shindyalov, I. N. and Bourne, P. E. (2000). The Protein Data Bank. Nucleic Acids Res. 28, 235-242.
27. Chenna, R., Sugawara, H., Koike, T., Lopez, R., Gibson, T. J., Higgins, D. G. and Thompson, J. D. (2003). Multiple sequence alignment with the Clustal series of programs. Nucleic Acids Res. 31, 3497-3500.
28. Sali, A. and Blundell, T. L. (1993). Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815.
29. Saxena, A. K., Singh, K., Long, C. A. and Garboczi, D. N. (2004). Preparation, crystallization and preliminary X-ray analysis of complex between antibody and Plasmodium vivax sexual stage 25kDa protein Pvs25 and malaria transmission-blocking antibody Fab fragment. Acta Crystallogr. D Biol. Crystallogr. D60, 2054-2057.
30. Saxena, A. K., Saul, A. and Garboczi, D. N. (2004). Crystallization and preliminary X-ray analysis of the Plasmodium vivax sexual stage 25kD protein, Pvs25, a transmission-blocking vaccine candidate for malaria. Acta Crystallogr. D Biol. Crystallogr. D60, 706-708.
31. Saxena, A. K., Singh, K., Su, H. P., Klein, M. M., Stower, A. W., Saul, A. J., Long, C. A. and Garboczi, D. N. (2006). Plasmodium P25 and P28, essential proteins for survival of the malaria parasite in the mosquito, are tile-like triangular prism. The essential mosquito-stage P25 and P28 proteins from Plasmodium form tile-like triangular prisms.? Nat. Struct. Mol. Biol. 13, 90-91.
32. Fiser,A. and Sali, A. (2003). ModLoop: Automated modeling of loops in protein structures. Bioinformatics 19, 2500-2501.
33. Fiser, A., Do, R. K. and Sali, A. (2000). Modeling of loops in protein structures. Protein Sci. 9, 1753-1773.
34. Whitelegg, N. and Rees, A. R. (2000).WAM: An improved algorithm for modelling antibodies on the WEB. Protein Eng. 13, 819-824.
35. Whitelegg, N. and Rees, A. R. (2004). Antibody variable regions: Toward a unified modeling method. Methods Mol. Biol. 248, 51-91.
36. Wiederstein, M. and Sippl, M. J. (2007). ProSA-web: Interactive web service for the recognition of errors in three-dimensional structures of proteins. Nucleic Acids Res. 35, W407-W410.
37. Sippl, M. J. (1993). Recognition of errors in three-dimensional structures of proteins. Proteins 17, 355-362.
38. Laskowski, R. A, MacArthur, M. W., Moss, D. S. and Thornton, J. M. (1993). PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
39. Vriend, G. (1990). WHAT IF: A molecular modeling and drug design program. J. Mol. Graph. 8, 52-56.
40. Hooft, R. W., Vriend, G., Sander, C. and Abola, E. E. (1996). Errors in protein structures. Nature 381, 272-272.
41. Morris, A. L., MacArthur, M. W., Hutchinson, E. G. and Thornton, J. M. (1992). Stereochemical quality of protein structure coordinates. Proteins 12, 345-364.
42. Humphrey, W., Dalke, A. and Schulten, K. (1996). VMD - Visual Molecular Dynamics. J. Mol. Graph. 14, 33-38.
43. Chen, R. and Weng, Z. (2003). A novel shape complementarirty scoring function for protein-Protein Docking. Proteins 51, 397-408.
44. The Open Babel Package, version 2.0.0. http://openbabel.sourceforge.net/.
45. Li, L., Chen, R. and Weng, Z. (2003). RDOCK: Refinement of rigid-body protein docking predictions. Proteins 53, 693-707.
46. Brooks, B. R., Bruccoleri, R. E., Olafson, B. D., States, D. J., Swaminathan, S. and Karplus, M. (1983). CHARMM: A program for macromolecular energy minimization and dynamics calculations. J. Comp. Chem. 4, 187-217.
47. Cavallo, L., Kleinjung, J. and Fraternali, F. (2003). POPS: A fast algorithm for solvent accessible surface areas at atomic and residue level. Nucleic Acids Res. 3, 3364-3366.
48. Laskowski, R. A. (2001). PDBsum: Summaries and analyses of PDB structures. Nucleic Acids Res. 29, 221-222.
49. Kaslow, D. C., Syin, C., McCutchan, T. F. and Miller L. H. (1989). Comparison of the primary structure of the 25 kDa ookinete surface antigens of Plasmodium falciparum and Plasmodium gallinaceum reveal six conserved regions. Mol. Biochem. Parasitol. 33, 283-287.
50. Stura, E. A., Kang, A. S., Stefanko, R. S., Calvo, J. C., Kaslow, D. C. and Satterthwait, A. C. (1994). Crystallization, sequence and preliminary crystallographic data for transmission-blocking anti-malaria Fab 4B7 with cyclic peptides from the Pfs25 protein of P. falciparum Acta Crystallogr. D. Biol. Crystallogr. D50, 535-542.