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Volumn 6, Issue 5, 2011, Pages

Determination of the molecular basis for a limited dimorphism, N417K, in the plasmodium vivax duffy-binding protein

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; DUFFY BINDING PROTEIN; LYSINE; CELL SURFACE RECEPTOR; DUFFY ANTIGEN BINDING PROTEIN, PLASMODIUM; PARASITE ANTIGEN; PROTOZOAL PROTEIN;

EID: 79956372972     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0020192     Document Type: Article
Times cited : (20)

References (36)
  • 2
    • 7244251635 scopus 로고    scopus 로고
    • Chloroquine resistance in Plasmodium vivax
    • Baird JK, (2004) Chloroquine resistance in Plasmodium vivax. Antimicrob Agents Chemother 48: 4075-4083.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 4075-4083
    • Baird, J.K.1
  • 5
    • 46349102897 scopus 로고    scopus 로고
    • Multidrug-resistant Plasmodium vivax associated with severe and fatal malaria: a prospective study in Papua, Indonesia
    • Tjitra E, Anstey NM, Sugiarto P, Warikar N, Kenangalem E, et al. (2008) Multidrug-resistant Plasmodium vivax associated with severe and fatal malaria: a prospective study in Papua, Indonesia. PLoS Med 5: e128.
    • (2008) PLoS Med , vol.5
    • Tjitra, E.1    Anstey, N.M.2    Sugiarto, P.3    Warikar, N.4    Kenangalem, E.5
  • 6
    • 0025011054 scopus 로고
    • The Duffy receptor family of Plasmodium knowlesi is located within the micronemes of invasive malaria merozoites
    • Adams JH, Hudson DE, Torii M, Ward GE, Wellems TE, et al. (1990) The Duffy receptor family of Plasmodium knowlesi is located within the micronemes of invasive malaria merozoites. Cell 63: 141-153.
    • (1990) Cell , vol.63 , pp. 141-153
    • Adams, J.H.1    Hudson, D.E.2    Torii, M.3    Ward, G.E.4    Wellems, T.E.5
  • 8
    • 0017077503 scopus 로고
    • The resistance factor to Plasmodium vivax in blacks. The Duffy-blood-group genotype, FyFy
    • Miller LH, Mason SJ, Clyde DF, McGinniss MH, (1976) The resistance factor to Plasmodium vivax in blacks. The Duffy-blood-group genotype, FyFy. N Engl J Med 295: 302-304.
    • (1976) N Engl J Med , vol.295 , pp. 302-304
    • Miller, L.H.1    Mason, S.J.2    Clyde, D.F.3    McGinniss, M.H.4
  • 9
    • 0024416519 scopus 로고
    • Plasmodium vivax interaction with the human Duffy blood group glycoprotein: identification of a parasite receptor-like protein
    • Wertheimer SP, Barnwell JW, (1989) Plasmodium vivax interaction with the human Duffy blood group glycoprotein: identification of a parasite receptor-like protein. Exp Parasitol 69: 340-350.
    • (1989) Exp Parasitol , vol.69 , pp. 340-350
    • Wertheimer, S.P.1    Barnwell, J.W.2
  • 10
    • 46149123863 scopus 로고    scopus 로고
    • Naturally acquired Duffy-binding protein-specific binding inhibitory antibodies confer protection from blood-stage Plasmodium vivax infection
    • King CL, Michon P, Shakri AR, Marcotty A, Stanisic D, et al. (2008) Naturally acquired Duffy-binding protein-specific binding inhibitory antibodies confer protection from blood-stage Plasmodium vivax infection. Proc Natl Acad Sci U S A 105: 8363-8368.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 8363-8368
    • King, C.L.1    Michon, P.2    Shakri, A.R.3    Marcotty, A.4    Stanisic, D.5
  • 11
    • 0033598744 scopus 로고    scopus 로고
    • Mapping regions containing binding residues within functional domains of Plasmodium vivax and Plasmodium knowlesi erythrocyte-binding proteins
    • Ranjan A, Chitnis CE, (1999) Mapping regions containing binding residues within functional domains of Plasmodium vivax and Plasmodium knowlesi erythrocyte-binding proteins. Proc Natl Acad Sci U S A 96: 14067-14072.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 14067-14072
    • Ranjan, A.1    Chitnis, C.E.2
  • 12
    • 8144222982 scopus 로고    scopus 로고
    • Conserved residues in the Plasmodium vivax Duffy-binding protein ligand domain are critical for erythrocyte receptor recognition
    • VanBuskirk KM, Sevova E, Adams JH, (2004) Conserved residues in the Plasmodium vivax Duffy-binding protein ligand domain are critical for erythrocyte receptor recognition. Proc Natl Acad Sci U S A 101: 15754-15759.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 15754-15759
    • VanBuskirk, K.M.1    Sevova, E.2    Adams, J.H.3
  • 13
    • 0042326726 scopus 로고    scopus 로고
    • Definition of structural elements in Plasmodium vivax and P. knowlesi Duffy-binding domains necessary for erythrocyte invasion
    • Singh SK, Singh AP, Pandey S, Yazdani SS, Chitnis CE, et al. (2003) Definition of structural elements in Plasmodium vivax and P. knowlesi Duffy-binding domains necessary for erythrocyte invasion. Biochem J 374: 193-198.
    • (2003) Biochem J , vol.374 , pp. 193-198
    • Singh, S.K.1    Singh, A.P.2    Pandey, S.3    Yazdani, S.S.4    Chitnis, C.E.5
  • 14
    • 0037417213 scopus 로고    scopus 로고
    • Diversity and natural selection in Plasmodium vivax Duffy binding protein gene
    • Cole-Tobian J, King CL, (2003) Diversity and natural selection in Plasmodium vivax Duffy binding protein gene. Mol Biochem Parasitol 127: 121-132.
    • (2003) Mol Biochem Parasitol , vol.127 , pp. 121-132
    • Cole-Tobian, J.1    King, C.L.2
  • 15
    • 0035374823 scopus 로고    scopus 로고
    • Analysis of polymorphic regions of Plasmodium vivax Duffy binding protein of Korean isolates
    • Kho WG, Chung JY, Sim EJ, Kim DW, Chung WC, (2001) Analysis of polymorphic regions of Plasmodium vivax Duffy binding protein of Korean isolates. Korean J Parasitol 39: 143-150.
    • (2001) Korean J Parasitol , vol.39 , pp. 143-150
    • Kho, W.G.1    Chung, J.Y.2    Sim, E.J.3    Kim, D.W.4    Chung, W.C.5
  • 16
    • 0027960198 scopus 로고
    • Natural variation within the principal adhesion domain of the Plasmodium vivax duffy binding protein
    • Tsuboi T, Kappe SH, al-Yaman F, Prickett MD, Alpers M, et al. (1994) Natural variation within the principal adhesion domain of the Plasmodium vivax duffy binding protein. Infect Immun 62: 5581-5586.
    • (1994) Infect Immun , vol.62 , pp. 5581-5586
    • Tsuboi, T.1    Kappe, S.H.2    al-Yaman, F.3    Prickett, M.D.4    Alpers, M.5
  • 17
    • 24644523245 scopus 로고    scopus 로고
    • Structure of AMA1 from Plasmodium falciparum reveals a clustering of polymorphisms that surround a conserved hydrophobic pocket
    • Bai T, Becker M, Gupta A, Strike P, Murphy VJ, et al. (2005) Structure of AMA1 from Plasmodium falciparum reveals a clustering of polymorphisms that surround a conserved hydrophobic pocket. Proc Natl Acad Sci U S A 102: 12736-12741.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 12736-12741
    • Bai, T.1    Becker, M.2    Gupta, A.3    Strike, P.4    Murphy, V.J.5
  • 18
    • 33646342967 scopus 로고    scopus 로고
    • The most polymorphic residue on Plasmodium falciparum apical membrane antigen 1 determines binding of an invasion-inhibitory antibody
    • Coley AM, Parisi K, Masciantonio R, Hoeck J, Casey JL, et al. (2006) The most polymorphic residue on Plasmodium falciparum apical membrane antigen 1 determines binding of an invasion-inhibitory antibody. Infect Immun 74: 2628-2636.
    • (2006) Infect Immun , vol.74 , pp. 2628-2636
    • Coley, A.M.1    Parisi, K.2    Masciantonio, R.3    Hoeck, J.4    Casey, J.L.5
  • 19
    • 0030017335 scopus 로고    scopus 로고
    • Protective immune responses to apical membrane antigen 1 of Plasmodium chabaudi involve recognition of strain-specific epitopes
    • Crewther PE, Matthew ML, Flegg RH, Anders RF, (1996) Protective immune responses to apical membrane antigen 1 of Plasmodium chabaudi involve recognition of strain-specific epitopes. Infect Immun 64: 3310-3317.
    • (1996) Infect Immun , vol.64 , pp. 3310-3317
    • Crewther, P.E.1    Matthew, M.L.2    Flegg, R.H.3    Anders, R.F.4
  • 20
    • 1942519904 scopus 로고    scopus 로고
    • Allelic polymorphisms in apical membrane antigen-1 are responsible for evasion of antibody-mediated inhibition in Plasmodium falciparum
    • Healer J, Murphy V, Hodder AN, Masciantonio R, Gemmill AW, et al. (2004) Allelic polymorphisms in apical membrane antigen-1 are responsible for evasion of antibody-mediated inhibition in Plasmodium falciparum. Mol Microbiol 52: 159-168.
    • (2004) Mol Microbiol , vol.52 , pp. 159-168
    • Healer, J.1    Murphy, V.2    Hodder, A.N.3    Masciantonio, R.4    Gemmill, A.W.5
  • 23
    • 6944255286 scopus 로고    scopus 로고
    • Antigenic drift in the ligand domain of Plasmodium vivax duffy binding protein confers resistance to inhibitory antibodies
    • VanBuskirk KM, Cole-Tobian JL, Baisor M, Sevova ES, Bockarie M, et al. (2004) Antigenic drift in the ligand domain of Plasmodium vivax duffy binding protein confers resistance to inhibitory antibodies. J Infect Dis 190: 1556-1562.
    • (2004) J Infect Dis , vol.190 , pp. 1556-1562
    • VanBuskirk, K.M.1    Cole-Tobian, J.L.2    Baisor, M.3    Sevova, E.S.4    Bockarie, M.5
  • 24
    • 20044390745 scopus 로고    scopus 로고
    • Sulphated tyrosines mediate association of chemokines and Plasmodium vivax Duffy binding protein with the Duffy antigen/receptor for chemokines (DARC)
    • Choe H, Moore MJ, Owens CM, Wright PL, Vasilieva N, et al. (2005) Sulphated tyrosines mediate association of chemokines and Plasmodium vivax Duffy binding protein with the Duffy antigen/receptor for chemokines (DARC). Mol Microbiol 55: 1413-1422.
    • (2005) Mol Microbiol , vol.55 , pp. 1413-1422
    • Choe, H.1    Moore, M.J.2    Owens, C.M.3    Wright, P.L.4    Vasilieva, N.5
  • 25
    • 32544440337 scopus 로고    scopus 로고
    • Structural basis for Duffy recognition by the malaria parasite Duffy-binding-like domain
    • Singh SK, Hora R, Belrhali H, Chitnis CE, Sharma A, (2006) Structural basis for Duffy recognition by the malaria parasite Duffy-binding-like domain. Nature 439: 741-744.
    • (2006) Nature , vol.439 , pp. 741-744
    • Singh, S.K.1    Hora, R.2    Belrhali, H.3    Chitnis, C.E.4    Sharma, A.5
  • 26
    • 38049050264 scopus 로고    scopus 로고
    • Plasmodium vivax invasion of human erythrocytes inhibited by antibodies directed against the Duffy binding protein
    • Grimberg BT, Udomsangpetch R, Xainli J, McHenry A, Panichakul T, et al. (2007) Plasmodium vivax invasion of human erythrocytes inhibited by antibodies directed against the Duffy binding protein. PLoS Med 4: e337.
    • (2007) PLoS Med , vol.4
    • Grimberg, B.T.1    Udomsangpetch, R.2    Xainli, J.3    McHenry, A.4    Panichakul, T.5
  • 27
    • 0342614926 scopus 로고    scopus 로고
    • Codon usage tabulated from international DNA sequence databases: status for the year 2000
    • Nakamura Y, Gojobori T, Ikemura T, (2000) Codon usage tabulated from international DNA sequence databases: status for the year 2000. Nucleic Acids Res 28: 292.
    • (2000) Nucleic Acids Res , vol.28 , pp. 292
    • Nakamura, Y.1    Gojobori, T.2    Ikemura, T.3
  • 28
    • 0346364657 scopus 로고    scopus 로고
    • Amino acid properties and consequences of substitutions
    • In: Barnes MR, Gray IC, editors, West Sussex, Wiley
    • Betts MJ, Russell RB, (2003) Amino acid properties and consequences of substitutions. In: Barnes MR, Gray IC, editors. Bioinformatics for Geneticists West Sussex Wiley.
    • (2003) Bioinformatics for Geneticists
    • Betts, M.J.1    Russell, R.B.2
  • 29
    • 0029657785 scopus 로고    scopus 로고
    • Genetic polymorphism of the Duffy receptor binding domain of Plasmodium vivax in Colombian wild isolates
    • Ampudia E, Patarroyo MA, Patarroyo ME, Murillo LA, (1996) Genetic polymorphism of the Duffy receptor binding domain of Plasmodium vivax in Colombian wild isolates. Mol Biochem Parasitol 78: 269-272.
    • (1996) Mol Biochem Parasitol , vol.78 , pp. 269-272
    • Ampudia, E.1    Patarroyo, M.A.2    Patarroyo, M.E.3    Murillo, L.A.4
  • 30
    • 0037103399 scopus 로고    scopus 로고
    • Age-acquired immunity to a Plasmodium vivax invasion ligand, the duffy binding protein
    • Cole-Tobian JL, Cortes A, Baisor M, Kastens W, Xainli J, et al. (2002) Age-acquired immunity to a Plasmodium vivax invasion ligand, the duffy binding protein. J Infect Dis 186: 531-539.
    • (2002) J Infect Dis , vol.186 , pp. 531-539
    • Cole-Tobian, J.L.1    Cortes, A.2    Baisor, M.3    Kastens, W.4    Xainli, J.5
  • 31
    • 0034495920 scopus 로고    scopus 로고
    • The erythrocyte binding motif of plasmodium vivax duffy binding protein is highly polymorphic and functionally conserved in isolates from Papua New Guinea
    • Xainli J, Adams JH, King CL, (2000) The erythrocyte binding motif of plasmodium vivax duffy binding protein is highly polymorphic and functionally conserved in isolates from Papua New Guinea. Mol Biochem Parasitol 111: 253-260.
    • (2000) Mol Biochem Parasitol , vol.111 , pp. 253-260
    • Xainli, J.1    Adams, J.H.2    King, C.L.3
  • 32
    • 14844282817 scopus 로고    scopus 로고
    • Mapping binding residues in the Plasmodium vivax domain that binds Duffy antigen during red cell invasion
    • Hans D, Pattnaik P, Bhattacharyya A, Shakri AR, Yazdani SS, et al. (2005) Mapping binding residues in the Plasmodium vivax domain that binds Duffy antigen during red cell invasion. Mol Microbiol 55: 1423-1434.
    • (2005) Mol Microbiol , vol.55 , pp. 1423-1434
    • Hans, D.1    Pattnaik, P.2    Bhattacharyya, A.3    Shakri, A.R.4    Yazdani, S.S.5
  • 33
    • 0034115851 scopus 로고    scopus 로고
    • Naturally acquired and vaccine-elicited antibodies block erythrocyte cytoadherence of the Plasmodium vivax Duffy binding protein
    • Michon P, Fraser T, Adams JH, (2000) Naturally acquired and vaccine-elicited antibodies block erythrocyte cytoadherence of the Plasmodium vivax Duffy binding protein. Infect Immun 68: 3164-3171.
    • (2000) Infect Immun , vol.68 , pp. 3164-3171
    • Michon, P.1    Fraser, T.2    Adams, J.H.3
  • 34
    • 0035917883 scopus 로고    scopus 로고
    • Duffy-null promoter heterozygosity reduces DARC expression and abrogates adhesion of the P. vivax ligand required for blood-stage infection
    • Michon P, Woolley I, Wood EM, Kastens W, Zimmerman PA, et al. (2001) Duffy-null promoter heterozygosity reduces DARC expression and abrogates adhesion of the P. vivax ligand required for blood-stage infection. FEBS Lett 495: 111-114.
    • (2001) FEBS Lett , vol.495 , pp. 111-114
    • Michon, P.1    Woolley, I.2    Wood, E.M.3    Kastens, W.4    Zimmerman, P.A.5
  • 35
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • Arnold K, Bordoli L, Kopp J, Schwede T, (2006) The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22: 195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 36
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede T, Kopp J, Guex N, Peitsch MC, (2003) SWISS-MODEL: An automated protein homology-modeling server. Nucleic Acids Res 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.