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Volumn 113, Issue 20, 2009, Pages 4980-4991

The human Pk histo-blood group antigen provides protection against HIV-1 infection

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD GROUP ANTIGEN; CD4 ANTIGEN; CHEMOKINE RECEPTOR; GANGLIOSIDE GM3; GLUCOSYLCERAMIDE; PK ANTIGEN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; CERAMIDE TRIHEXOSIDE; CHEMOKINE RECEPTOR CCR5; CHEMOKINE RECEPTOR CXCR4; CXCR4 PROTEIN, HUMAN; GALACTOSYLTRANSFERASE; GLOBOTRIAOSYLCERAMIDE; UDP GALACTOSE GALBETA1 4GLCBETA1 CER ALPHA1,4 GALACTOSYLTRANSFERASE; UDP-GALACTOSE - GALBETA1-4GLCBETA1-CER ALPHA1,4-GALACTOSYLTRANSFERASE;

EID: 66549127485     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2008-03-143396     Document Type: Article
Times cited : (63)

References (52)
  • 1
    • 33749443426 scopus 로고    scopus 로고
    • Genetics of resistance to HIV infection: Role of co-receptors and co-receptor ligands
    • DOI 10.1016/j.smim.2006.07.007, PII S1044532306001011, Human Genetics of Infectious Desiases: Immunological Implications
    • Arenzana-Seisdedos F, Parmentier M. Genetics of resistance to HIV infection: role of coreceptors and coreceptor ligands. Semin Immunol. 2006;18:387-403. (Pubitemid 44511884)
    • (2006) Seminars in Immunology , vol.18 , Issue.6 , pp. 387-403
    • Arenzana-Seisdedos, F.1    Parmentier, M.2
  • 2
    • 8844245596 scopus 로고    scopus 로고
    • HIV and the CCR5-delta32 resistance allele
    • de Silva E, Stumpf MP. HIV and the CCR5-delta32 resistance allele. FEMS Microbiol Lett. 2004;241:1-12.
    • (2004) FEMS Microbiol Lett , vol.241 , pp. 1-12
    • De Silva, E.1    Stumpf, M.P.2
  • 3
    • 0032103577 scopus 로고    scopus 로고
    • Chemokine receptor allelic polymorphisms: Relationships to HIV resistance and disease progression
    • DOI 10.1006/smim.1998.0132
    • Paxton WA, Kang S. Chemokine receptor allelic polymorphisms: relationships to HIV resistance and disease progression. Semin Immunol. 1998;10:187-194. (Pubitemid 28347035)
    • (1998) Seminars in Immunology , vol.10 , Issue.3 , pp. 187-194
    • Paxton, W.A.1    Kang, S.2
  • 4
    • 0033783569 scopus 로고    scopus 로고
    • Blood group associations with parasites, bacteria, and viruses
    • Moulds JM, Moulds JJ. Blood group associations with parasites, bacteria, and viruses. Transfus Med Rev. 2000;14:302-311.
    • (2000) Transfus Med Rev , vol.14 , pp. 302-311
    • Moulds, J.M.1    Moulds, J.J.2
  • 5
    • 0028917379 scopus 로고
    • The P blood group system: Biochemical, serological, and clinical aspects
    • Spitalnik PF, Spitalnik SL. The P blood group system: biochemical, serological, and clinical aspects. Transfus Med Rev. 1995;9:110-122.
    • (1995) Transfus Med Rev , vol.9 , pp. 110-122
    • Spitalnik, P.F.1    Spitalnik, S.L.2
  • 7
    • 0029916780 scopus 로고    scopus 로고
    • Role of verotoxin receptors in pathogenesis
    • Lingwood CA. Role of verotoxin receptors in pathogenesis. Trends Microbiol. 1996;4:147-153.
    • (1996) Trends Microbiol , vol.4 , pp. 147-153
    • Lingwood, C.A.1
  • 8
    • 0025653730 scopus 로고
    • Neutral glycosphingolipids of the globo-series characterize activation stages corresponding to germinal center B cells
    • Schwartz-Albiez R, Dorken B, Moller P, Brodin NT, Monner DA, Kniep B. Neutral glycosphingolipids of the globo-series characterize activation stages corresponding to germinal center B cells. Int Immunol. 1990;2:929-936. (Pubitemid 20330542)
    • (1990) International Immunology , vol.2 , Issue.10 , pp. 928-936
    • Schwartz-Albiez, R.1    Dorken, B.2    Moller, P.3    Brodin, N.T.4    Monner, D.A.5    Kniep, B.6
  • 9
    • 0037119419 scopus 로고    scopus 로고
    • k blood group phenotype: Identification of four inactivating mutations in the UDP-N-acetylgalactosamine: Globotriaosylceramide 3-beta-N- Acetylgalactosaminyltransferase gene
    • DOI 10.1074/jbc.M203047200
    • Hellberg A, Poole J, Olsson ML. Molecular basis of the globoside-deficient P(k) blood group phenotype. Identification of four inactivating mutations in the UDP-N-acetylgalactosamine: globotriaosylceramide 3-beta-N-acetylgalactosaminyltransferase gene. J Biol Chem. 2002;277:29455- 29459. (Pubitemid 41079230)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.33 , pp. 29455-29459
    • Hellberg, A.1    Poole, J.2    Olsson, M.L.3
  • 10
    • 27644594291 scopus 로고    scopus 로고
    • k) locus do not correlate with the presence of the P1 blood group antigen
    • DOI 10.1186/1471-2156-6-49
    • Hellberg A, Chester MA, Olsson ML. Two previously proposed P1/P2-differentiating and nine novel polymorphisms at the A4GALT (Pk) locus do not correlate with the presence of the P1 blood group antigen. BMC Genet. 2005;6:49. (Pubitemid 41554905)
    • (2005) BMC Genetics , vol.6 , pp. 49
    • Hellberg, A.1    Chester, M.A.2    Olsson, M.L.3
  • 11
    • 3142683273 scopus 로고    scopus 로고
    • Genetic heterogeneity at the glycosyltransferase loci underlying the GLOB blood group and collection
    • DOI 10.1111/j.1365-2141.2004.04930.x
    • Hellberg A, Ringressi A, Yahalom V, Safwenberg J, Reid ME, Olsson ML. Genetic heterogeneity at the glycosyltransferase loci underlying the GLOB blood group system and collection. Br J Haematol. 2004;125:528-536. (Pubitemid 38916199)
    • (2004) British Journal of Haematology , vol.125 , Issue.4 , pp. 528-536
    • Hellberg, A.1    Ringressi, A.2    Yahalom, V.3    Safwenberg, J.4    Reid, M.E.5    Olsson, M.L.6
  • 12
    • 0034529161 scopus 로고    scopus 로고
    • Molecular basis for the p phenotype. Identification of distinct and multiple mutations in the alpha1,4-galactosyltransferase gene in Swedish and Japanese individuals
    • DOI 10.1074/jbc.C000625200
    • Furukawa K, Iwamura K, Uchikawa M, et al. Molecular basis for the p phenotype: identification of distinct and multiple mutations in the alpha 1,4-galactosyltransferase gene in Swedish and Japanese individuals. J Biol Chem. 2000;275:37752-37756. (Pubitemid 32004890)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.48 , pp. 37752-37756
    • Furukawa, K.1    Iwamura, K.2    Uchikawa, M.3    Sojka, B.N.4    Wiels, J.5    Okajima, T.6    Urano, T.7    Furukawa, K.8
  • 15
    • 0033575192 scopus 로고    scopus 로고
    • A convenient oxidation of natural glycosphingolipids to their "ceramide acids" for neoglycoconjugation: Bovine serum albumin-glycosylceramide acid conjugates as investigative probes for HIV gp120 coat protein-glycosphingolipid interactions
    • Mylvaganam M, Lingwood CA. A convenient oxidation of natural glycosphingolipids to their "ceramide acids" for neoglycoconjugation: bovine serum albumin-glycosylceramide acid conjugates as investigative probes for HIV gp120 coat protein-glycosphingolipid interactions. J Biol Chem. 1999;274:20725-20732.
    • (1999) J Biol Chem , vol.274 , pp. 20725-20732
    • Mylvaganam, M.1    Lingwood, C.A.2
  • 18
    • 0037192816 scopus 로고    scopus 로고
    • Identification of a common sphingolipid-binding domain in Alzheimer, prion, and HIV-1 proteins
    • DOI 10.1074/jbc.M111679200
    • Mahfoud R, Garmy N, Maresca M, Yahi N, Puigserver A, Fantini J. Identification of a common sphingolipid-binding domain in Alzheimer, prion, and HIV-1 proteins. J Biol Chem. 2002;277:11292-11296. (Pubitemid 34952893)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.13 , pp. 11292-11296
    • Mahfoud, R.1    Garmy, N.2    Maresca, M.3    Yahi, N.4    Puigserver, A.5    Fantini, J.6
  • 20
  • 21
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry cofactor: Functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor
    • Feng Y, Broder CC, Kennedy PE, Berger EA. HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor. Science. 1996;272:872-877.
    • (1996) Science , vol.272 , pp. 872-877
    • Feng, Y.1    Broder, C.C.2    Kennedy, P.E.3    Berger, E.A.4
  • 22
    • 0036888490 scopus 로고    scopus 로고
    • A post-CD4-binding step involving interaction of the V3 region of viral gp120 with host cell surface glycosphingolipids is common to entry and infection by diverse HIV-1 strains
    • Nehete PN, Vela EM, Hossain MM, et al. A post-CD4-binding step involving interaction of the V3 region of viral gp120 with host cell surface glycosphingolipids is common to entry and infection by diverse HIV-1 strains. Antiviral Res. 2002;56:233-251.
    • (2002) Antiviral Res , vol.56 , pp. 233-251
    • Nehete, P.N.1    Vela, E.M.2    Hossain, M.M.3
  • 23
    • 0041877636 scopus 로고    scopus 로고
    • Modulation of entry of enveloped viruses by cholesterol and sphingolipids
    • DOI 10.1080/0968768031000104944
    • Rawat SS, Viard M, Gallo SA, Rein A, Blumenthal R, Puri A. Modulation of entry of enveloped viruses by cholesterol and sphingolipids [Review]. Mol Membr Biol. 2003;20:243-254. (Pubitemid 37046249)
    • (2003) Molecular Membrane Biology , vol.20 , Issue.3 , pp. 243-254
    • Rawat, S.S.1    Viard, M.2    Gallo, S.A.3    Rein, A.4    Blumenthal, R.5    Puri, A.6
  • 24
    • 0032743108 scopus 로고    scopus 로고
    • Role of glycosphingolipids in HIV-1 entry: Requirement of globotriosylceramide (Gb3) in CD4/CXCR4-dependent fusion
    • Puri A, Hug P, Jernigan K, Rose P, Blumenthal R. Role of glycosphingolipids in HIV-1 entry: requirement of globotriosylceramide (Gb3) in CD4/CXCR4-dependent fusion. Biosci Rep. 1999;19:317-325.
    • (1999) Biosci Rep , vol.19 , pp. 317-325
    • Puri, A.1    Hug, P.2    Jernigan, K.3    Rose, P.4    Blumenthal, R.5
  • 26
    • 25844482999 scopus 로고    scopus 로고
    • Lack of susceptibility of cells from patients with Fabry disease to productive infection with R5 human immunodeficiency virus
    • Lund N, Branch DR, Sakac D, et al. Lack of susceptibility of cells from patients with Fabry disease to productive infection with R5 human immunodeficiency virus. AIDS. 2005;19:1543-1546. (Pubitemid 41400702)
    • (2005) AIDS , vol.19 , Issue.14 , pp. 1543-1546
    • Lund, N.1    Branch, D.R.2    Sakac, D.3    Lingwood, C.A.4    Siatskas, C.5    Robinson, C.J.6    Brady, R.O.7    Medin, J.A.8
  • 27
    • 33645037987 scopus 로고    scopus 로고
    • A novel soluble mimic of the glycolipid, globotriaosyl ceramide inhibits HIV infection
    • Lund N, Branch DR, Mylvaganam M, et al. A novel soluble mimic of the glycolipid, globotriaosyl ceramide inhibits HIV infection. AIDS. 2006;20:333-343.
    • (2006) AIDS , vol.20 , pp. 333-343
    • Lund, N.1    Branch, D.R.2    Mylvaganam, M.3
  • 29
    • 57649180469 scopus 로고    scopus 로고
    • Induction of HIV-1 resistance: Cell susceptibility to infection is an inverse function of globotriaosyl ceramide levels
    • Ramkumar S, Sakac D, Binnington B, Branch DR, Lingwood CA. Induction of HIV-1 resistance: cell susceptibility to infection is an inverse function of globotriaosyl ceramide levels. Glycobiology. 2009;19:76-82.
    • (2009) Glycobiology , vol.19 , pp. 76-82
    • Ramkumar, S.1    Sakac, D.2    Binnington, B.3    Branch, D.R.4    Lingwood, C.A.5
  • 31
    • 0037083724 scopus 로고    scopus 로고
    • VPAC1 is a cellular neuroendocrine receptor expressed on T cells that actively facilitates productive HIV-1 infection
    • DOI 10.1097/00002030-200202150-00001
    • Branch DR, Valenta LJ, Yousefi S, et al. VPAC1 is a cellular neuroendocrine receptor expressed on T cells that actively facilitates productive HIV-1 infection. AIDS. 2002;16:309-319. (Pubitemid 34165361)
    • (2002) AIDS , vol.16 , Issue.3 , pp. 309-319
    • Branch, D.R.1    Valenta, L.J.E.2    Yousefi, S.3    Sakac, D.4    Singla, R.5    Bali, M.6    Sahai, B.M.7    Ma, X.-Z.8
  • 32
    • 34247201596 scopus 로고    scopus 로고
    • HIV-1 integration is inhibited by stimulation of the VPAC2 neuroendocrine receptor
    • DOI 10.1016/j.virol.2006.12.012, PII S0042682206009007
    • Bokaei PB, Ma XZ, Sakac D, Branch DR. HIV-1 integration is inhibited by stimulation of the VPAC2 neuroendocrine receptor. Virology. 2007;362:38-49. (Pubitemid 46617687)
    • (2007) Virology , vol.362 , Issue.1 , pp. 38-49
    • Bokaei, P.B.1    Ma, X.-Z.2    Sakac, D.3    Branch, D.R.4
  • 33
    • 33745260683 scopus 로고    scopus 로고
    • Treatment of the neutral glycosphingolipid lysosomal storage disease via inhibition of the ABC drug transporter, MDR1: Cyclosporine a can lower serum and liver globotriaosyl ceramide levels in the Fabry mouse model
    • Mattocks M, Bond M, Bagovitch M, et al. Treatment of the neutral glycosphingolipid lysosomal storage disease via inhibition of the ABC drug transporter, MDR1: cyclosporine A can lower serum and liver globotriaosyl ceramide levels in the Fabry mouse model. FEBS J. 2006;273:2064-2075.
    • (2006) FEBS J , vol.273 , pp. 2064-2075
    • Mattocks, M.1    Bond, M.2    Bagovitch, M.3
  • 37
    • 70449344254 scopus 로고    scopus 로고
    • Accessed June 12, 2002
    • GenBank, Kojima et al. http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db= nuccore&id=7959010. Accessed June 12, 2002.
    • GenBank, K.1
  • 38
    • 0033591332 scopus 로고    scopus 로고
    • Improved inhibitors of glucosylceramide synthase
    • Lee L, Abe A, Shayman JA. Improved inhibitors of glucosylceramide synthase. J Biol Chem. 1999;274:14662-14669.
    • (1999) J Biol Chem , vol.274 , pp. 14662-14669
    • Lee, L.1    Abe, A.2    Shayman, J.A.3
  • 40
    • 0025055421 scopus 로고
    • Glycosphingolipid patterns of peripheral blood lymphocytes, monocytes, and granulocytes are cell specific
    • Kiguchi K, Henning-Chubb CB, Huberman E. Glycosphingolipid patterns of peripheral blood lymphocytes, monocytes, and granulocytes are cell specific. J Biochem. 1990;107:8-14. (Pubitemid 20027260)
    • (1990) Journal of Biochemistry , vol.107 , Issue.1 , pp. 8-14
    • Kiguchi, K.1    Henning-Chubb, C.B.2    Huberman, E.3
  • 41
    • 0021875198 scopus 로고
    • Glycosphingolipids of the globo-series are associated with the monocytic lineage of human myeloid cells
    • DOI 10.1111/j.1432-1033.1985.tb08910.x
    • Kniep B, Monner DA, Schwulera U, Muhlradt PF. Glycosphingolipids of the globo-series are associated with the monocytic lineage of human myeloid cells. Eur J Biochem. 1985;149:187-191. (Pubitemid 15013500)
    • (1985) European Journal of Biochemistry , vol.149 , Issue.1 , pp. 187-191
    • Kniep, B.1    Monner, D.A.2    Schwulera, U.3    Muhlradt, P.F.4
  • 42
    • 0018614040 scopus 로고
    • P blood group regulation of glycosphingolipid levels in human erythrocytes
    • Fletcher KS, Bremer EG, Schwarting GA. P blood group regulation of glycosphingolipid levels in human erythrocytes. J Biol Chem. 1979;254:11196-11198. (Pubitemid 10136129)
    • (1979) Journal of Biological Chemistry , vol.254 , Issue.22 , pp. 11196-11198
    • Fletcher, K.S.1    Bremer, E.G.2    Schwarting, G.A.3
  • 43
    • 0034834457 scopus 로고    scopus 로고
    • Lipid rafts and HIV pathogenesis: Host membrane cholesterol is required for infection by HIV type 1
    • DOI 10.1089/088922201300343690
    • Liao Z, Cimakasky LM, Hampton R, Nguyen DH, Hildreth JE. Lipid rafts and HIV pathogenesis: host membrane cholesterol is required for infection by HIV type 1. AIDS Res Hum Retroviruses. 2001;17:1009-1019. (Pubitemid 32881320)
    • (2001) AIDS Research and Human Retroviruses , vol.17 , Issue.11 , pp. 1009-1019
    • Liao, Z.1    Cimakasky, L.M.2    Hampton, R.3    Nguyen, D.H.4    Hildreth, J.E.K.5
  • 44
    • 0036148171 scopus 로고    scopus 로고
    • Segregation of CD4 and CXCR4 into distinct lipid microdomains in T lymphocytes suggests a mechanism for membrane destabilization by human immunodeficiency virus
    • DOI 10.1128/JVI.76.4.1802-1815.2002
    • Kozak SL, Heard JM, Kabat D. Segregation of CD4 and CXCR4 into distinct lipid microdomains in T lymphocytes suggests a mechanism for membrane destabilization by human immunodeficiency virus. J Virol. 2002;76:1802-1815. (Pubitemid 34094628)
    • (2002) Journal of Virology , vol.76 , Issue.4 , pp. 1802-1815
    • Kozak, S.L.1    Heard, J.M.2    Kabat, D.3
  • 45
    • 14644444219 scopus 로고    scopus 로고
    • Dynamic reorganization of chemokine receptors, cholesterol, lipid rafts, and adhesion molecules to sites of CD4 engagement
    • DOI 10.1016/j.yexcr.2004.11.022
    • Nguyen DH, Giri B, Collins G, Taub DD. Dynamic reorganization of chemokine receptors, cholesterol, lipid rafts, and adhesion molecules to sites of CD4 engagement. Exp Cell Res. 2005;304:559-569. (Pubitemid 40321132)
    • (2005) Experimental Cell Research , vol.304 , Issue.2 , pp. 559-569
    • Nguyen, D.H.1    Giri, B.2    Collins, G.3    Taub, D.D.4
  • 46
    • 0032484486 scopus 로고    scopus 로고
    • CCR5 coreceptor usage of non-syncytium-inducing primary HIV-1 is independent of phylogenetically distinct global HIV-1 isolates: Delineation of consensus motif in the V3 domain that predicts CCR-5 usage
    • DOI 10.1006/viro.1997.8924
    • Xiao L, Owen SM, Goldman I, et al. CCR5 coreceptor usage of non-syncytium-inducing primary HIV-1 is independent of phylogenetically distinct global HIV-1 isolates: delineation of consensus motif in the V3 domain that predicts CCR-5 usage. Virology. 1998;240:83-92. (Pubitemid 28394126)
    • (1998) Virology , vol.240 , Issue.1 , pp. 83-92
    • Xiao, L.1    Owen, S.M.2    Goldman, I.3    Lal, A.A.4    Dejong, J.J.5    Goudsmit, J.6    Lal, R.B.7
  • 47
    • 0031596253 scopus 로고    scopus 로고
    • T-trophic human immunodeficiency virus type 1 (HIV-1)-derived V3 loop peptides directly bind to CXCR-4 and inhibit T-tropic HIV-1 infection
    • Sakaida H, Hori T, Yonezawa A, et al. T-tropic human immunodeficiency virus type 1 (HIV-1)-derived V3 loop peptides directly bind to CXCR-4 and inhibit T-tropic HIV-1 infection. J Virol. 1998;72:9763-9770. (Pubitemid 28520841)
    • (1998) Journal of Virology , vol.72 , Issue.12 , pp. 9763-9770
    • Sakaida, H.1    Hori, T.2    Yonezawa, A.3    Sato, A.4    Isaka, Y.5    Yoshie, O.6    Hattori, T.7    Uchiyama, T.8
  • 48
    • 0029731557 scopus 로고    scopus 로고
    • Spc3, a V3 loop-derived synthetic peptide inhibitor of HIV-1 infection, binds to cell surface glycosphingolipids
    • DOI 10.1021/bi961205g
    • Delezay O, Hammache D, Fantini J, Yahi N. SPC3, a V3 loop-derived synthetic peptide inhibitor of HIV-1 infection, binds to cell surface glycosphingolipids. Biochemistry. 1996;35:15663-15671. (Pubitemid 26422303)
    • (1996) Biochemistry , vol.35 , Issue.49 , pp. 15663-15671
    • Delezay, O.1    Hammache, D.2    Fantini, J.3    Yahi, N.4
  • 49
    • 0034527810 scopus 로고    scopus 로고
    • Role of glycosphingolipid microdomains in CD4-dependent HIV-1 fusion
    • DOI 10.1023/A:1026537122903
    • Fantini J, Hammache D, Piéroni G, Yahi N. Role of glycosphingolipid microdomains in CD4-dependent HIV-1 fusion. Glycoconj J. 2000;17:199-204. (Pubitemid 32055906)
    • (2000) Glycoconjugate Journal , vol.17 , Issue.3-4 , pp. 199-204
    • Fantini, J.1    Hammache, D.2    Pieroni, G.3    Yahi, N.4
  • 50
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp 120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • DOI 10.1038/31405
    • Kwong PD, Wyatt R, Robinson J, Sweet RW, Sodroski J, Hendrickson WA. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature. 1998;393:648-659. (Pubitemid 28289647)
    • (1998) Nature , vol.393 , Issue.6686 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 52
    • 0032911088 scopus 로고    scopus 로고
    • Recruitment of renal tublular epithelial cells expressing verotoxin-1 (Stx1) receptors in HIV-1 transgenic mice with renal disease
    • Liu XH, Lingwood CA, Ray PE. Recruitment of renal tublular epithelial cells expressing verotoxin-1 (Stx1) receptors in HIV-1 transgenic mice with renal disease. Kidney Int. 1999;55:554-561.
    • (1999) Kidney Int , vol.55 , pp. 554-561
    • Liu, X.H.1    Lingwood, C.A.2    Ray, P.E.3


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