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Volumn 4, Issue NOV, 2013, Pages

Human immunodeficiency virus and heparan sulfate: From attachment to entry inhibition

Author keywords

Attachment and entry inhibition; CCR5 CXCR4; Co receptor binding site; Glycosaminoglycan; Gp120; Heparan sulfate; HIV 1; V3 loop

Indexed keywords


EID: 84890320471     PISSN: None     EISSN: 16643224     Source Type: Journal    
DOI: 10.3389/fimmu.2013.00385     Document Type: Review
Times cited : (108)

References (104)
  • 1
    • 0020596551 scopus 로고
    • Isolation of a T-lymphotropic retrovirus from a patient at risk for acquired immune deficiency syndrome (AIDS)
    • doi: 10.1126/science.6189183
    • Barre-Sinoussi F, Chermann JC, Rey F, Nugeyre MT, Chamaret S, Gruest J, et al. Isolation of a T-lymphotropic retrovirus from a patient at risk for acquired immune deficiency syndrome (AIDS). Science (1983) 220:868-71. doi: 10.1126/science.6189183
    • (1983) Science , vol.220 , pp. 868-871
    • Barre-Sinoussi, F.1    Chermann, J.C.2    Rey, F.3    Nugeyre, M.T.4    Chamaret, S.5    Gruest, J.6
  • 2
    • 0035991688 scopus 로고    scopus 로고
    • HIV receptors and cellular tropism
    • doi:10.1080/15216540212652
    • Weiss RA. HIV receptors and cellular tropism. IUBMB Life (2002) 53:201-5. doi:10.1080/15216540212652
    • (2002) IUBMB Life , vol.53 , pp. 201-205
    • Weiss, R.A.1
  • 3
    • 84876864047 scopus 로고    scopus 로고
    • HIV transmission
    • doi:10.1101/cshperspect.a006965
    • Shaw GM, Hunter E. HIV transmission. Cold Spring Harb Perspect Med (2012) 2(11):a006965. doi:10.1101/cshperspect.a006965
    • (2012) Cold Spring Harb Perspect Med , vol.2 , Issue.11
    • Shaw, G.M.1    Hunter, E.2
  • 4
    • 0033012398 scopus 로고    scopus 로고
    • Chemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease
    • doi:10.1146/annurev.immunol.17.1.657
    • Berger EA, Murphy PM, Farber JM. Chemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease. Annu Rev Immunol (1999) 17:657-700. doi:10.1146/annurev.immunol.17.1.657
    • (1999) Annu Rev Immunol , vol.17 , pp. 657-700
    • Berger, E.A.1    Murphy, P.M.2    Farber, J.M.3
  • 5
    • 0032893134 scopus 로고    scopus 로고
    • HIV-1 attachment: another look
    • doi:10.1016/S0966-842X(99)01474-2
    • Ugolini S, Mondor I, Sattentau QJ. HIV-1 attachment: another look. Trends Microbiol (1999) 7:144-9. doi:10.1016/S0966-842X(99)01474-2
    • (1999) Trends Microbiol , vol.7 , pp. 144-149
    • Ugolini, S.1    Mondor, I.2    Sattentau, Q.J.3
  • 6
    • 0037226498 scopus 로고    scopus 로고
    • Entry of viruses through the epithelial barrier: pathogenic trickery
    • doi:10.1038/nrm1005
    • Bomsel M, Alfsen A. Entry of viruses through the epithelial barrier: pathogenic trickery. Nat Rev Mol Cell Biol (2003) 4:57-68. doi:10.1038/nrm1005
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 57-68
    • Bomsel, M.1    Alfsen, A.2
  • 7
    • 33845992460 scopus 로고    scopus 로고
    • R5-and X4-HIV-1 use differentially the endometrial epithelial cells HEC-1A to ensure their own spread: implication for mechanisms of sexual transmission
    • doi:10.1016/j.virol.2006.07.029
    • Saidi H, Magri G, Nasreddine N, Requena M, Belec L. R5-and X4-HIV-1 use differentially the endometrial epithelial cells HEC-1A to ensure their own spread: implication for mechanisms of sexual transmission. Virology (2007) 358:55-68. doi:10.1016/j.virol.2006.07.029
    • (2007) Virology , vol.358 , pp. 55-68
    • Saidi, H.1    Magri, G.2    Nasreddine, N.3    Requena, M.4    Belec, L.5
  • 9
    • 70149088868 scopus 로고    scopus 로고
    • Interactions between heparan sulfate and proteins-design and functional implications
    • doi:10.1016/S1937-6448(09)76003-4
    • Lindahl U, Li JP. Interactions between heparan sulfate and proteins-design and functional implications. Int Rev Cell Mol Biol (2009) 276:105-59. doi:10.1016/S1937-6448(09)76003-4
    • (2009) Int Rev Cell Mol Biol , vol.276 , pp. 105-159
    • Lindahl, U.1    Li, J.P.2
  • 10
    • 70349876852 scopus 로고    scopus 로고
    • The molecular basis and functional implications of chemokine interactions with heparan sulphate
    • doi:10.1016/j.sbi.2009.09.003
    • Lortat-Jacob H. The molecular basis and functional implications of chemokine interactions with heparan sulphate. Curr Opin Struct Biol (2009) 19:543-8. doi:10.1016/j.sbi.2009.09.003
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 543-548
    • Lortat-Jacob, H.1
  • 11
    • 79952105330 scopus 로고    scopus 로고
    • Chemokine oligomerization and interactions with receptors and glycosaminoglycans: the role of structural dynamics in function
    • doi:10.1016/j.yexcr.2011.01.004
    • Salanga CL, Handel TM. Chemokine oligomerization and interactions with receptors and glycosaminoglycans: the role of structural dynamics in function. Exp Cell Res (2011) 317:590-601. doi:10.1016/j.yexcr.2011.01.004
    • (2011) Exp Cell Res , vol.317 , pp. 590-601
    • Salanga, C.L.1    Handel, T.M.2
  • 12
    • 84867255818 scopus 로고    scopus 로고
    • Homeostatic and tissue reparation defaults in mice carrying selective genetic invalidation of CXCL12/proteoglycan interactions
    • doi:10.1161/CIRCULATIONAHA.112.113290
    • Rueda P, Richart A, Recalde A, Gasse P, Vilar J, Guerin C, et al. Homeostatic and tissue reparation defaults in mice carrying selective genetic invalidation of CXCL12/proteoglycan interactions. Circulation (2012) 126:1882-95. doi:10.1161/CIRCULATIONAHA.112.113290
    • (2012) Circulation , vol.126 , pp. 1882-1895
    • Rueda, P.1    Richart, A.2    Recalde, A.3    Gasse, P.4    Vilar, J.5    Guerin, C.6
  • 13
    • 84875421249 scopus 로고    scopus 로고
    • Exploring mechanisms of FGF signalling through the lens of structural biology
    • doi:10.1038/nrm3528
    • Goetz R, Mohammadi M. Exploring mechanisms of FGF signalling through the lens of structural biology. Nat Rev Mol Cell Biol (2013) 14:166-80. doi:10.1038/nrm3528
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 166-180
    • Goetz, R.1    Mohammadi, M.2
  • 14
    • 0030055212 scopus 로고    scopus 로고
    • Heparin decreases the blood clearance of interferon-gamma and increases its activity by limiting the processing of its carboxyl-terminal sequence
    • doi:10.1074/jbc.271.27.16139
    • Lortat-Jacob H, Baltzer F, Grimaud JA. Heparin decreases the blood clearance of interferon-gamma and increases its activity by limiting the processing of its carboxyl-terminal sequence. J Biol Chem (1996) 271:16139-43. doi:10.1074/jbc.271.27.16139
    • (1996) J Biol Chem , vol.271 , pp. 16139-16143
    • Lortat-Jacob, H.1    Baltzer, F.2    Grimaud, J.A.3
  • 15
    • 0034283174 scopus 로고    scopus 로고
    • Conformational changes in serpins: II. The mechanism of activation of antithrombin by heparindagger
    • doi:10.1006/jmbi.2000.3982
    • Whisstock JC, Pike RN, Jin L, Skinner R, Pei XY, Carrell RW, et al. Conformational changes in serpins: II. The mechanism of activation of antithrombin by heparindagger. J Mol Biol (2000) 301:1287-305. doi:10.1006/jmbi.2000.3982
    • (2000) J Mol Biol , vol.301 , pp. 1287-1305
    • Whisstock, J.C.1    Pike, R.N.2    Jin, L.3    Skinner, R.4    Pei, X.Y.5    Carrell, R.W.6
  • 16
    • 84864472945 scopus 로고    scopus 로고
    • Transport of fibroblast growth factor 2 in the pericellular matrix is controlled by the spatial distribution of its binding sites in heparan sulfate
    • doi:10.1371/journal.pbio.1001361
    • Duchesne L, Octeau V, Bearon RN, Beckett A, Prior IA, Lounis B, et al. Transport of fibroblast growth factor 2 in the pericellular matrix is controlled by the spatial distribution of its binding sites in heparan sulfate. PLoS Biol (2012) 10:e1001361. doi:10.1371/journal.pbio.1001361
    • (2012) PLoS Biol , vol.10
    • Duchesne, L.1    Octeau, V.2    Bearon, R.N.3    Beckett, A.4    Prior, I.A.5    Lounis, B.6
  • 17
    • 84866792640 scopus 로고    scopus 로고
    • Glycosaminoglycan-dependent restriction of FGF diffusion is necessary for lacrimal gland development
    • doi:10.1242/dev.079236
    • Qu X, Pan Y, Carbe C, Powers A, Grobe K, Zhang X. Glycosaminoglycan-dependent restriction of FGF diffusion is necessary for lacrimal gland development. Development (2012) 139:2730-9. doi:10.1242/dev.079236
    • (2012) Development , vol.139 , pp. 2730-2739
    • Qu, X.1    Pan, Y.2    Carbe, C.3    Powers, A.4    Grobe, K.5    Zhang, X.6
  • 18
    • 84871326579 scopus 로고    scopus 로고
    • Inflammatory chemokines direct and restrict leukocyte migration within live tissues as glycan-bound gradients
    • doi:10.1016/j.cub.2012.11.018
    • Sarris M, Masson JB, Maurin D, Aa LM, Boudinot P, Lortat-Jacob H, et al. Inflammatory chemokines direct and restrict leukocyte migration within live tissues as glycan-bound gradients. Curr Biol (2012) 22:2375-82. doi:10.1016/j.cub.2012.11.018
    • (2012) Curr Biol , vol.22 , pp. 2375-2382
    • Sarris, M.1    Masson, J.B.2    Maurin, D.3    Aa, L.M.4    Boudinot, P.5    Lortat-Jacob, H.6
  • 19
    • 56649100319 scopus 로고    scopus 로고
    • The structure of glycosaminoglycans and their interactions with proteins
    • doi:10.1111/j.1747-0285.2008.00741.x
    • Gandhi NS, Mancera RL. The structure of glycosaminoglycans and their interactions with proteins. Chem Biol Drug Des (2008) 72:455-82. doi:10.1111/j.1747-0285.2008.00741.x
    • (2008) Chem Biol Drug Des , vol.72 , pp. 455-482
    • Gandhi, N.S.1    Mancera, R.L.2
  • 20
    • 84873024385 scopus 로고    scopus 로고
    • Heparan sulfate biosynthesis: regulation and variability
    • doi:10.1369/0022155412464972
    • Kreuger J, Kjellen L. Heparan sulfate biosynthesis: regulation and variability. J Histochem Cytochem (2012) 60:898-907. doi:10.1369/0022155412464972
    • (2012) J Histochem Cytochem , vol.60 , pp. 898-907
    • Kreuger, J.1    Kjellen, L.2
  • 21
    • 6344284808 scopus 로고    scopus 로고
    • Heparan sulfate/heparin oligosaccharides protect stromal cell-derived factor-1 (SDF-1)/CXCL12 against proteolysis induced by CD26/dipeptidyl peptidase IV
    • doi:10.1074/jbc.M405392200
    • Sadir R, Imberty A, Baleux F, Lortat-Jacob H. Heparan sulfate/heparin oligosaccharides protect stromal cell-derived factor-1 (SDF-1)/CXCL12 against proteolysis induced by CD26/dipeptidyl peptidase IV. J Biol Chem (2004) 279:43854-60. doi:10.1074/jbc.M405392200
    • (2004) J Biol Chem , vol.279 , pp. 43854-43860
    • Sadir, R.1    Imberty, A.2    Baleux, F.3    Lortat-Jacob, H.4
  • 22
    • 0034852346 scopus 로고    scopus 로고
    • Heparan sulfate: anchor for viral intruders?
    • doi:10.1016/S0300-9084(01)01290-1
    • Spillmann D. Heparan sulfate: anchor for viral intruders? Biochimie (2001) 83:811-7. doi:10.1016/S0300-9084(01)01290-1
    • (2001) Biochimie , vol.83 , pp. 811-817
    • Spillmann, D.1
  • 23
    • 0036139068 scopus 로고    scopus 로고
    • Cell surface heparan sulfate and its roles in assisting viral infections
    • doi:10.1002/med.1026
    • Liu J, Thorp SC. Cell surface heparan sulfate and its roles in assisting viral infections. Med Res Rev (2002) 22:1-25. doi:10.1002/med.1026
    • (2002) Med Res Rev , vol.22 , pp. 1-25
    • Liu, J.1    Thorp, S.C.2
  • 24
    • 33645747062 scopus 로고    scopus 로고
    • Heparan sulphate proteoglycans and viral vectors: ally or foe?
    • doi:10.2174/156652306775515565
    • Vives RR, Lortat-Jacob H, Fender P. Heparan sulphate proteoglycans and viral vectors: ally or foe? Curr Gene Ther (2006) 6:35-44. doi:10.2174/156652306775515565
    • (2006) Curr Gene Ther , vol.6 , pp. 35-44
    • Vives, R.R.1    Lortat-Jacob, H.2    Fender, P.3
  • 25
    • 77953076127 scopus 로고    scopus 로고
    • Proteoglycans in host-pathogen interactions: molecular mechanisms and therapeutic implications
    • doi:10.1017/S1462399409001367
    • Bartlett AH, Park PW. Proteoglycans in host-pathogen interactions: molecular mechanisms and therapeutic implications. Expert Rev Mol Med (2010) 12:e5. doi:10.1017/S1462399409001367
    • (2010) Expert Rev Mol Med , vol.12
    • Bartlett, A.H.1    Park, P.W.2
  • 26
    • 84868014678 scopus 로고    scopus 로고
    • Role of heparan sulfate in sexually transmitted infections
    • doi:10.1093/glycob/cws106
    • Tiwari V, Maus E, Sigar IM, Ramsey KH, Shukla D. Role of heparan sulfate in sexually transmitted infections. Glycobiology (2012) 22:1402-12. doi:10.1093/glycob/cws106
    • (2012) Glycobiology , vol.22 , pp. 1402-1412
    • Tiwari, V.1    Maus, E.2    Sigar, I.M.3    Ramsey, K.H.4    Shukla, D.5
  • 27
    • 76249098780 scopus 로고    scopus 로고
    • Plasmodium falciparum BAEBL binds to heparan sulfate proteoglycans on the human erythrocyte surface
    • doi:10.1074/jbc.M109.021576
    • Kobayashi K, Kato K, Sugi T, Takemae H, Pandey K, Gong H, et al. Plasmodium falciparum BAEBL binds to heparan sulfate proteoglycans on the human erythrocyte surface. J Biol Chem (2010) 285:1716-25. doi:10.1074/jbc.M109.021576
    • (2010) J Biol Chem , vol.285 , pp. 1716-1725
    • Kobayashi, K.1    Kato, K.2    Sugi, T.3    Takemae, H.4    Pandey, K.5    Gong, H.6
  • 28
    • 84861213684 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa pili and flagella mediate distinct binding and signaling events at the apical and basolateral surface of airway epithelium
    • doi:10.1371/journal.ppat.1002616
    • Bucior I, Pielage JF, Engel JN. Pseudomonas aeruginosa pili and flagella mediate distinct binding and signaling events at the apical and basolateral surface of airway epithelium. PLoS Pathog (2012) 8:e1002616. doi:10.1371/journal.ppat.1002616
    • (2012) PLoS Pathog , vol.8
    • Bucior, I.1    Pielage, J.F.2    Engel, J.N.3
  • 29
    • 55449126064 scopus 로고    scopus 로고
    • Molecular mechanisms involved in vascular interactions of the Lyme disease pathogen in a living host
    • doi:10.1371/journal.ppat.1000169
    • Norman MU, Moriarty TJ, Dresser AR, Millen B, Kubes P, Chaconas G. Molecular mechanisms involved in vascular interactions of the Lyme disease pathogen in a living host. PLoS Pathog (2008) 4:e1000169. doi:10.1371/journal.ppat.1000169
    • (2008) PLoS Pathog , vol.4
    • Norman, M.U.1    Moriarty, T.J.2    Dresser, A.R.3    Millen, B.4    Kubes, P.5    Chaconas, G.6
  • 30
    • 84857754823 scopus 로고    scopus 로고
    • Differential contribution of the repeats to heparin binding of HBHA, a major adhesin of Mycobacterium tuberculosis
    • doi:10.1371/journal.pone.0032421
    • Lebrun P, Raze D, Fritzinger B, Wieruszeski JM, Biet F, Dose A, et al. Differential contribution of the repeats to heparin binding of HBHA, a major adhesin of Mycobacterium tuberculosis. PLoS One (2012) 7:e32421. doi:10.1371/journal.pone.0032421
    • (2012) PLoS One , vol.7
    • Lebrun, P.1    Raze, D.2    Fritzinger, B.3    Wieruszeski, J.M.4    Biet, F.5    Dose, A.6
  • 31
    • 84874486107 scopus 로고    scopus 로고
    • A conformational heparan sulfate binding site essential to infectivity overlaps with the conserved hepatitis B virus a-determinant
    • doi:10.1002/hep.26125
    • Sureau C, Salisse J. A conformational heparan sulfate binding site essential to infectivity overlaps with the conserved hepatitis B virus a-determinant. Hepatology (2013) 57:985-94. doi:10.1002/hep.26125
    • (2013) Hepatology , vol.57 , pp. 985-994
    • Sureau, C.1    Salisse, J.2
  • 32
    • 0036779285 scopus 로고    scopus 로고
    • Cellular glycosaminoglycans and low density lipoprotein receptor are involved in hepatitis C virus adsorption
    • doi:10.1002/jmv.10196
    • Germi R, Crance JM, Garin D, Guimet J, Lortat-Jacob H, Ruigrok RW, et al. Cellular glycosaminoglycans and low density lipoprotein receptor are involved in hepatitis C virus adsorption. J Med Virol (2002) 68:206-15. doi:10.1002/jmv.10196
    • (2002) J Med Virol , vol.68 , pp. 206-215
    • Germi, R.1    Crance, J.M.2    Garin, D.3    Guimet, J.4    Lortat-Jacob, H.5    Ruigrok, R.W.6
  • 33
    • 84874671326 scopus 로고    scopus 로고
    • Proteoglycans act as cellular hepatitis delta virus attachment receptors
    • doi:10.1371/journal.pone.0058340
    • Lamas Longarela O, Schmidt TT, Schoneweis K, Romeo R, Wedemeyer H, Urban S, et al. Proteoglycans act as cellular hepatitis delta virus attachment receptors. PLoS One (2013) 8:e58340. doi:10.1371/journal.pone.0058340
    • (2013) PLoS One , vol.8
    • Lamas Longarela, O.1    Schmidt, T.T.2    Schoneweis, K.3    Romeo, R.4    Wedemeyer, H.5    Urban, S.6
  • 34
    • 72849138163 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans are required for cellular binding of the hepatitis E virus ORF2 capsid protein and for viral infection
    • doi:10.1128/JVI.00717-09
    • Kalia M, Chandra V, Rahman SA, Sehgal D, Jameel S. Heparan sulfate proteoglycans are required for cellular binding of the hepatitis E virus ORF2 capsid protein and for viral infection. J Virol (2009) 83:12714-24. doi:10.1128/JVI.00717-09
    • (2009) J Virol , vol.83 , pp. 12714-12724
    • Kalia, M.1    Chandra, V.2    Rahman, S.A.3    Sehgal, D.4    Jameel, S.5
  • 35
    • 84879831306 scopus 로고    scopus 로고
    • Differential dependence on host cell glycosaminoglycans for infection of epithelial cells by high-risk HPV types
    • doi:10.1371/journal.pone.0068379
    • Cruz L, Meyers C. Differential dependence on host cell glycosaminoglycans for infection of epithelial cells by high-risk HPV types. PLoS One (2013) 8:e68379. doi:10.1371/journal.pone.0068379
    • (2013) PLoS One , vol.8
    • Cruz, L.1    Meyers, C.2
  • 36
    • 0033215527 scopus 로고    scopus 로고
    • A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry
    • doi:10.1016/S0092-8674(00)80058-6
    • Shukla D, Liu J, Blaiklock P, Shworak NW, Bai X, Esko JD, et al. A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry. Cell (1999) 99:13-22. doi:10.1016/S0092-8674(00)80058-6
    • (1999) Cell , vol.99 , pp. 13-22
    • Shukla, D.1    Liu, J.2    Blaiklock, P.3    Shworak, N.W.4    Bai, X.5    Esko, J.D.6
  • 37
    • 65949101737 scopus 로고    scopus 로고
    • HTLV-1 uses HSPG and neuropilin-1 for entry by molecular mimicry of VEGF165
    • doi:10.1182/blood-2008-04-150342
    • Lambert S, Bouttier M, Vassy R, Seigneuret M, Petrow-Sadowski C, Janvier S, et al. HTLV-1 uses HSPG and neuropilin-1 for entry by molecular mimicry of VEGF165. Blood (2009) 113:5176-85. doi:10.1182/blood-2008-04-150342
    • (2009) Blood , vol.113 , pp. 5176-5185
    • Lambert, S.1    Bouttier, M.2    Vassy, R.3    Seigneuret, M.4    Petrow-Sadowski, C.5    Janvier, S.6
  • 39
    • 56349167518 scopus 로고    scopus 로고
    • Polyanionic drugs and viral oncogenesis: a novel approach to control infection, tumor-associated inflammation and angiogenesis
    • doi:10.3390/molecules13112758
    • Urbinati C, Chiodelli P, Rusnati M. Polyanionic drugs and viral oncogenesis: a novel approach to control infection, tumor-associated inflammation and angiogenesis. Molecules (2008) 13:2758-85. doi:10.3390/molecules13112758
    • (2008) Molecules , vol.13 , pp. 2758-2785
    • Urbinati, C.1    Chiodelli, P.2    Rusnati, M.3
  • 40
    • 0036631776 scopus 로고    scopus 로고
    • Heparin binds to murine leukemia virus and inhibits Env-independent attachment and infection
    • doi:10.1128/JVI.76.14.6909-6918.2002
    • Walker SJ, Pizzato M, Takeuchi Y, Devereux S. Heparin binds to murine leukemia virus and inhibits Env-independent attachment and infection. J Virol (2002) 76:6909-18. doi:10.1128/JVI.76.14.6909-6918.2002
    • (2002) J Virol , vol.76 , pp. 6909-6918
    • Walker, S.J.1    Pizzato, M.2    Takeuchi, Y.3    Devereux, S.4
  • 41
    • 29044443281 scopus 로고    scopus 로고
    • Antiviral effect of the heparan sulfate mimetic, PI-88, against dengue and encephalitic flaviviruses
    • doi:10.1016/j.antiviral.2005.08.006
    • Lee E, Pavy M, Young N, Freeman C, Lobigs M. Antiviral effect of the heparan sulfate mimetic, PI-88, against dengue and encephalitic flaviviruses. Antiviral Res (2006) 69:31-8. doi:10.1016/j.antiviral.2005.08.006
    • (2006) Antiviral Res , vol.69 , pp. 31-38
    • Lee, E.1    Pavy, M.2    Young, N.3    Freeman, C.4    Lobigs, M.5
  • 42
    • 34247163691 scopus 로고    scopus 로고
    • Sulfated homologues of heparin inhibit hepatitis C virus entry into mammalian cells
    • doi:10.1128/JVI.02622-06
    • Basu A, Kanda T, Beyene A, Saito K, Meyer K, Ray R. Sulfated homologues of heparin inhibit hepatitis C virus entry into mammalian cells. J Virol (2007) 81:3933-41. doi:10.1128/JVI.02622-06
    • (2007) J Virol , vol.81 , pp. 3933-3941
    • Basu, A.1    Kanda, T.2    Beyene, A.3    Saito, K.4    Meyer, K.5    Ray, R.6
  • 43
    • 0031869503 scopus 로고    scopus 로고
    • Adaptation of Sindbis virus to BHK cells selects for use of heparan sulfate as an attachment receptor
    • Klimstra WB, Ryman KD, Johnston RE. Adaptation of Sindbis virus to BHK cells selects for use of heparan sulfate as an attachment receptor. J Virol (1998) 72:7357-66.
    • (1998) J Virol , vol.72 , pp. 7357-7366
    • Klimstra, W.B.1    Ryman, K.D.2    Johnston, R.E.3
  • 44
    • 0033819352 scopus 로고    scopus 로고
    • Passage of classical swine fever virus in cultured swine kidney cells selects virus variants that bind to heparan sulfate due to a single amino acid change in envelope protein E(rns)
    • doi:10.1128/JVI.74.20.9553-9561.2000
    • Hulst MM, Van Gennip HG, Moormann RJ. Passage of classical swine fever virus in cultured swine kidney cells selects virus variants that bind to heparan sulfate due to a single amino acid change in envelope protein E(rns). J Virol (2000) 74:9553-61. doi:10.1128/JVI.74.20.9553-9561.2000
    • (2000) J Virol , vol.74 , pp. 9553-9561
    • Hulst, M.M.1    Van Gennip, H.G.2    Moormann, R.J.3
  • 45
    • 0035024156 scopus 로고    scopus 로고
    • Adaptation of tick-borne encephalitis virus to BHK-21 cells results in the formation of multiple heparan sulfate binding sites in the envelope protein and attenuation in vivo
    • doi:10.1128/JVI.75.12.5627-5637.2001
    • Mandl CW, Kroschewski H, Allison SL, Kofler R, Holzmann H, Meixner T, et al. Adaptation of tick-borne encephalitis virus to BHK-21 cells results in the formation of multiple heparan sulfate binding sites in the envelope protein and attenuation in vivo. J Virol (2001) 75:5627-37. doi:10.1128/JVI.75.12.5627-5637.2001
    • (2001) J Virol , vol.75 , pp. 5627-5637
    • Mandl, C.W.1    Kroschewski, H.2    Allison, S.L.3    Kofler, R.4    Holzmann, H.5    Meixner, T.6
  • 46
    • 33645031982 scopus 로고    scopus 로고
    • Heparin-binding and patterns of virulence for two recombinant strains of Sindbis virus
    • doi:10.1016/j.virol.2005.11.034
    • Bear JS, Byrnes AP, Griffin DE. Heparin-binding and patterns of virulence for two recombinant strains of Sindbis virus. Virology (2006) 347:183-90. doi:10.1016/j.virol.2005.11.034
    • (2006) Virology , vol.347 , pp. 183-190
    • Bear, J.S.1    Byrnes, A.P.2    Griffin, D.E.3
  • 47
    • 77949406401 scopus 로고    scopus 로고
    • Directional spread of surface-associated retroviruses regulated by differential virus-cell interactions
    • doi:10.1128/JVI.02155-09
    • Sherer NM, Jin J, Mothes W. Directional spread of surface-associated retroviruses regulated by differential virus-cell interactions. J Virol (2010) 84:3248-58. doi:10.1128/JVI.02155-09
    • (2010) J Virol , vol.84 , pp. 3248-3258
    • Sherer, N.M.1    Jin, J.2    Mothes, W.3
  • 48
    • 79954617024 scopus 로고    scopus 로고
    • Fusing structure and function: a structural view of the herpesvirus entry machinery
    • doi:10.1038/nrmicro2548
    • Connolly SA, Jackson JO, Jardetzky TS, Longnecker R. Fusing structure and function: a structural view of the herpesvirus entry machinery. Nat Rev Microbiol (2011) 9:369-81. doi:10.1038/nrmicro2548
    • (2011) Nat Rev Microbiol , vol.9 , pp. 369-381
    • Connolly, S.A.1    Jackson, J.O.2    Jardetzky, T.S.3    Longnecker, R.4
  • 49
    • 1842850945 scopus 로고    scopus 로고
    • Herpes simplex virus: receptors and ligands for cell entry
    • doi:10.1111/j.1462-5822.2004.00389.x
    • Spear PG. Herpes simplex virus: receptors and ligands for cell entry. Cell Microbiol (2004) 6:401-10. doi:10.1111/j.1462-5822.2004.00389.x
    • (2004) Cell Microbiol , vol.6 , pp. 401-410
    • Spear, P.G.1
  • 50
    • 79959589596 scopus 로고    scopus 로고
    • Synthesis of 3-O-sulfonated heparan sulfate octasaccharides that inhibit the herpes simplex virus type 1 host-cell interaction
    • doi:10.1038/nchem.1073
    • Hu YP, Lin SY, Huang CY, Zulueta MM, Liu JY, Chang W, et al. Synthesis of 3-O-sulfonated heparan sulfate octasaccharides that inhibit the herpes simplex virus type 1 host-cell interaction. Nat Chem (2011) 3:557-63. doi:10.1038/nchem.1073
    • (2011) Nat Chem , vol.3 , pp. 557-563
    • Hu, Y.P.1    Lin, S.Y.2    Huang, C.Y.3    Zulueta, M.M.4    Liu, J.Y.5    Chang, W.6
  • 51
    • 73349125484 scopus 로고    scopus 로고
    • Spermatozoa capture HIV-1 through heparan sulfate and efficiently transmit the virus to dendritic cells
    • doi:10.1084/jem.20091579
    • Ceballos A, Remes Lenicov F, Sabatte J, Rodriguez Rodrigues C, Cabrini M, Jancic C, et al. Spermatozoa capture HIV-1 through heparan sulfate and efficiently transmit the virus to dendritic cells. J Exp Med (2009) 206:2717-33. doi:10.1084/jem.20091579
    • (2009) J Exp Med , vol.206 , pp. 2717-2733
    • Ceballos, A.1    Remes Lenicov, F.2    Sabatte, J.3    Rodriguez Rodrigues, C.4    Cabrini, M.5    Jancic, C.6
  • 52
    • 0345569681 scopus 로고    scopus 로고
    • Inhibiting sexual transmission of HIV-1 infection
    • doi:10.1038/nrmicro729
    • Shattock RJ, Moore JP. Inhibiting sexual transmission of HIV-1 infection. Nat Rev Microbiol (2003) 1:25-34. doi:10.1038/nrmicro729
    • (2003) Nat Rev Microbiol , vol.1 , pp. 25-34
    • Shattock, R.J.1    Moore, J.P.2
  • 53
    • 0031023496 scopus 로고    scopus 로고
    • Transcytosis of infectious human immunodeficiency virus across a tight human epithelial cell line barrier
    • doi:10.1038/nm0197-42
    • Bomsel M. Transcytosis of infectious human immunodeficiency virus across a tight human epithelial cell line barrier. Nat Med (1997) 3:42-7. doi:10.1038/nm0197-42
    • (1997) Nat Med , vol.3 , pp. 42-47
    • Bomsel, M.1
  • 54
    • 44349159423 scopus 로고    scopus 로고
    • Setting the stage: host invasion by HIV
    • doi:10.1038/nri2302
    • Hladik F, McElrath MJ. Setting the stage: host invasion by HIV. Nat Rev Immunol (2008) 8:447-57. doi:10.1038/nri2302
    • (2008) Nat Rev Immunol , vol.8 , pp. 447-457
    • Hladik, F.1    McElrath, M.J.2
  • 55
    • 0346243730 scopus 로고    scopus 로고
    • Human genital epithelial cells capture cell-free human immunodeficiency virus type 1 and transmit the virus to CD4+ Cells: implications for mechanisms of sexual transmission
    • doi:10.1086/379248
    • Wu Z, Chen Z, Phillips DM. Human genital epithelial cells capture cell-free human immunodeficiency virus type 1 and transmit the virus to CD4+ Cells: implications for mechanisms of sexual transmission. J Infect Dis (2003) 188:1473-82. doi:10.1086/379248
    • (2003) J Infect Dis , vol.188 , pp. 1473-1482
    • Wu, Z.1    Chen, Z.2    Phillips, D.M.3
  • 56
    • 33845803152 scopus 로고    scopus 로고
    • Cell-free human immunodeficiency virus type 1 transcytosis through primary genital epithelial cells
    • doi:10.1128/JVI.01303-06
    • Bobardt MD, Chatterji U, Selvarajah S, Van Der Schueren B, David G, Kahn B, et al. Cell-free human immunodeficiency virus type 1 transcytosis through primary genital epithelial cells. J Virol (2007) 81:395-405. doi:10.1128/JVI.01303-06
    • (2007) J Virol , vol.81 , pp. 395-405
    • Bobardt, M.D.1    Chatterji, U.2    Selvarajah, S.3    Van Der Schueren, B.4    David, G.5    Kahn, B.6
  • 57
    • 84885455013 scopus 로고    scopus 로고
    • HIV-1 gp120 induces TLR2-and TLR4-mediated innate immune activation in human female genital epithelium
    • doi:10.4049/jimmunol.1301482
    • Nazli A, Kafka JK, Ferreira VH, Anipindi V, Mueller K, Osborne BJ, et al. HIV-1 gp120 induces TLR2-and TLR4-mediated innate immune activation in human female genital epithelium. J Immunol (2013) 191(8):4246-58. doi:10.4049/jimmunol.1301482
    • (2013) J Immunol , vol.191 , Issue.8 , pp. 4246-4258
    • Nazli, A.1    Kafka, J.K.2    Ferreira, V.H.3    Anipindi, V.4    Mueller, K.5    Osborne, B.J.6
  • 58
    • 33646695905 scopus 로고    scopus 로고
    • Expression of HIV receptors, alternate receptors and co-receptors on tonsillar epithelium: implications for HIV binding and primary oral infection
    • doi:10.1186/1743-422X-3-25
    • Kumar RB, Maher DM, Herzberg MC, Southern PJ. Expression of HIV receptors, alternate receptors and co-receptors on tonsillar epithelium: implications for HIV binding and primary oral infection. Virol J (2006) 3:25. doi:10.1186/1743-422X-3-25
    • (2006) Virol J , vol.3 , pp. 25
    • Kumar, R.B.1    Maher, D.M.2    Herzberg, M.C.3    Southern, P.J.4
  • 59
    • 34248202589 scopus 로고    scopus 로고
    • HIV-1 infection of trophoblasts is independent of gp120/CD4 Interactions but relies on heparan sulfate proteoglycans
    • doi:10.1086/515576
    • Vidricaire G, Gauthier S, Tremblay MJ. HIV-1 infection of trophoblasts is independent of gp120/CD4 Interactions but relies on heparan sulfate proteoglycans. J Infect Dis (2007) 195:1461-71. doi:10.1086/515576
    • (2007) J Infect Dis , vol.195 , pp. 1461-1471
    • Vidricaire, G.1    Gauthier, S.2    Tremblay, M.J.3
  • 60
    • 0037237790 scopus 로고    scopus 로고
    • Syndecan captures, protects, and transmits HIV to T lymphocytes
    • doi:10.1016/S1074-7613(02)00504-6
    • Bobardt MD, Saphire AC, Hung HC, Yu X, Van Der Schueren B, Zhang Z, et al. Syndecan captures, protects, and transmits HIV to T lymphocytes. Immunity (2003) 18:27-39. doi:10.1016/S1074-7613(02)00504-6
    • (2003) Immunity , vol.18 , pp. 27-39
    • Bobardt, M.D.1    Saphire, A.C.2    Hung, H.C.3    Yu, X.4    Van Der Schueren, B.5    Zhang, Z.6
  • 61
    • 0242268531 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 enters primary human brain microvascular endothelial cells by a mechanism involving cell surface proteoglycans independent of lipid rafts
    • doi:10.1128/JVI.77.22.12140-12151.2003
    • Argyris EG, Acheampong E, Nunnari G, Mukhtar M, Williams KJ, Pomerantz RJ. Human immunodeficiency virus type 1 enters primary human brain microvascular endothelial cells by a mechanism involving cell surface proteoglycans independent of lipid rafts. J Virol (2003) 77:12140-51. doi:10.1128/JVI.77.22.12140-12151.2003
    • (2003) J Virol , vol.77 , pp. 12140-12151
    • Argyris, E.G.1    Acheampong, E.2    Nunnari, G.3    Mukhtar, M.4    Williams, K.J.5    Pomerantz, R.J.6
  • 62
    • 4344708057 scopus 로고    scopus 로고
    • Binding, internalization, and membrane incorporation of human immunodeficiency virus-1 at the blood-brain barrier is differentially regulated
    • doi:10.1016/j.neuroscience.2004.06.021
    • Banks WA, Robinson SM, Wolf KM, Bess JW Jr, Arthur LO. Binding, internalization, and membrane incorporation of human immunodeficiency virus-1 at the blood-brain barrier is differentially regulated. Neuroscience (2004) 128:143-53. doi:10.1016/j.neuroscience.2004.06.021
    • (2004) Neuroscience , vol.128 , pp. 143-153
    • Banks, W.A.1    Robinson, S.M.2    Wolf, K.M.3    Bess Jr., J.W.4    Arthur, L.O.5
  • 63
    • 2642547187 scopus 로고    scopus 로고
    • Contribution of proteoglycans to human immunodeficiency virus type 1 brain invasion
    • doi:10.1128/JVI.78.12.6567-6584.2004
    • Bobardt MD, Salmon P, Wang L, Esko JD, Gabuzda D, Fiala M, et al. Contribution of proteoglycans to human immunodeficiency virus type 1 brain invasion. J Virol (2004) 78:6567-84. doi:10.1128/JVI.78.12.6567-6584.2004
    • (2004) J Virol , vol.78 , pp. 6567-6584
    • Bobardt, M.D.1    Salmon, P.2    Wang, L.3    Esko, J.D.4    Gabuzda, D.5    Fiala, M.6
  • 64
    • 38949104363 scopus 로고    scopus 로고
    • HIV-1 p17 binds heparan sulfate proteoglycans to activated CD4(+) T cells
    • doi:10.1016/j.virusres.2007.10.006
    • Poiesi C, De Francesco MA, Baronio M, Manca N. HIV-1 p17 binds heparan sulfate proteoglycans to activated CD4(+) T cells. Virus Res (2008) 132:25-32. doi:10.1016/j.virusres.2007.10.006
    • (2008) Virus Res , vol.132 , pp. 25-32
    • Poiesi, C.1    De Francesco, M.A.2    Baronio, M.3    Manca, N.4
  • 65
    • 0035793619 scopus 로고    scopus 로고
    • Internalization of HIV-1 tat requires cell surface heparan sulfate proteoglycans
    • doi:10.1074/jbc.M006701200
    • Tyagi M, Rusnati M, Presta M, Giacca M. Internalization of HIV-1 tat requires cell surface heparan sulfate proteoglycans. J Biol Chem (2001) 276:3254-61. doi:10.1074/jbc.M006701200
    • (2001) J Biol Chem , vol.276 , pp. 3254-3261
    • Tyagi, M.1    Rusnati, M.2    Presta, M.3    Giacca, M.4
  • 66
    • 80052079059 scopus 로고    scopus 로고
    • Characterization of the mechanisms of HIV-1 Vpr(52-96) internalization in cells
    • doi:10.1016/j.biochi.2011.05.033
    • Greiner VJ, Shvadchak V, Fritz J, Arntz Y, Didier P, Frisch B, et al. Characterization of the mechanisms of HIV-1 Vpr(52-96) internalization in cells. Biochimie (2011) 93:1647-58. doi:10.1016/j.biochi.2011.05.033
    • (2011) Biochimie , vol.93 , pp. 1647-1658
    • Greiner, V.J.1    Shvadchak, V.2    Fritz, J.3    Arntz, Y.4    Didier, P.5    Frisch, B.6
  • 67
    • 78649640372 scopus 로고    scopus 로고
    • In vitro evaluation of viability, integrity, and inflammation in genital epithelia upon exposure to pharmaceutical excipients and candidate microbicides
    • doi:10.1128/AAC.00456-10
    • Gali Y, Delezay O, Brouwers J, Addad N, Augustijns P, Bourlet T, et al. In vitro evaluation of viability, integrity, and inflammation in genital epithelia upon exposure to pharmaceutical excipients and candidate microbicides. Antimicrob Agents Chemother (2010) 54:5105-14. doi:10.1128/AAC.00456-10
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 5105-5114
    • Gali, Y.1    Delezay, O.2    Brouwers, J.3    Addad, N.4    Augustijns, P.5    Bourlet, T.6
  • 68
    • 79955099301 scopus 로고    scopus 로고
    • The rise and fall of polyanionic inhibitors of the human immunodeficiency virus type 1
    • doi:10.1016/j.antiviral.2011.03.176
    • Pirrone V, Wigdahl B, Krebs FC. The rise and fall of polyanionic inhibitors of the human immunodeficiency virus type 1. Antiviral Res (2011) 90:168-82. doi:10.1016/j.antiviral.2011.03.176
    • (2011) Antiviral Res , vol.90 , pp. 168-182
    • Pirrone, V.1    Wigdahl, B.2    Krebs, F.C.3
  • 69
    • 0021720872 scopus 로고
    • T-lymphocyte T4 molecule behaves as the receptor for human retrovirus LAV
    • doi:10.1038/312767a0
    • Klatzmann D, Champagne E, Chamaret S, Gruest J, Guetard D, Hercend T, et al. T-lymphocyte T4 molecule behaves as the receptor for human retrovirus LAV. Nature (1984) 312:767-8. doi:10.1038/312767a0
    • (1984) Nature , vol.312 , pp. 767-768
    • Klatzmann, D.1    Champagne, E.2    Chamaret, S.3    Gruest, J.4    Guetard, D.5    Hercend, T.6
  • 70
    • 0032546952 scopus 로고    scopus 로고
    • A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding
    • doi:10.1126/science.280.5371.1949
    • Rizzuto CD, Wyatt R, Hernandez-Ramos N, Sun Y, Kwong PD, Hendrickson WA, et al. A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding. Science (1998) 280:1949-53. doi:10.1126/science.280.5371.1949
    • (1998) Science , vol.280 , pp. 1949-1953
    • Rizzuto, C.D.1    Wyatt, R.2    Hernandez-Ramos, N.3    Sun, Y.4    Kwong, P.D.5    Hendrickson, W.A.6
  • 71
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 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) 393:648-59. doi:10.1038/31405
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 72
    • 13844302894 scopus 로고    scopus 로고
    • Structure of an unliganded simian immunodeficiency virus gp120 core
    • doi:10.1038/nature03327
    • Chen B, Vogan EM, Gong H, Skehel JJ, Wiley DC, Harrison SC. Structure of an unliganded simian immunodeficiency virus gp120 core. Nature (2005) 433:834-41. doi:10.1038/nature03327
    • (2005) Nature , vol.433 , pp. 834-841
    • Chen, B.1    Vogan, E.M.2    Gong, H.3    Skehel, J.J.4    Wiley, D.C.5    Harrison, S.C.6
  • 73
  • 74
    • 16144365650 scopus 로고    scopus 로고
    • CD4-induced interaction of primary HIV-1 gp120 glycoproteins with the chemokine receptor CCR-5
    • doi:10.1038/384179a0
    • Wu L, Gerard NP, Wyatt R, Choe H, Parolin C, Ruffing N, et al. CD4-induced interaction of primary HIV-1 gp120 glycoproteins with the chemokine receptor CCR-5. Nature (1996) 384:179-83. doi:10.1038/384179a0
    • (1996) Nature , vol.384 , pp. 179-183
    • Wu, L.1    Gerard, N.P.2    Wyatt, R.3    Choe, H.4    Parolin, C.5    Ruffing, N.6
  • 76
    • 0023201996 scopus 로고
    • Inhibitory effect of dextran sulfate and heparin on the replication of human immunodeficiency virus (HIV) in vitro
    • doi:10.1016/0166-3542(87)90001-5
    • Ito M, Baba M, Sato A, Pauwels R, De Clercq E, Shigeta S. Inhibitory effect of dextran sulfate and heparin on the replication of human immunodeficiency virus (HIV) in vitro. Antiviral Res (1987) 7:361-7. doi:10.1016/0166-3542(87)90001-5
    • (1987) Antiviral Res , vol.7 , pp. 361-367
    • Ito, M.1    Baba, M.2    Sato, A.3    Pauwels, R.4    De Clercq, E.5    Shigeta, S.6
  • 77
    • 0023709207 scopus 로고
    • Sulfated polysaccharides are potent and selective inhibitors of various enveloped viruses, including herpes simplex virus, cytomegalovirus, vesicular stomatitis virus, and human immunodeficiency virus
    • doi:10.1128/AAC.32.11.1742
    • Baba M, Snoeck R, Pauwels R, De Clercq E. Sulfated polysaccharides are potent and selective inhibitors of various enveloped viruses, including herpes simplex virus, cytomegalovirus, vesicular stomatitis virus, and human immunodeficiency virus. Antimicrob Agents Chemother (1988) 32:1742-5. doi:10.1128/AAC.32.11.1742
    • (1988) Antimicrob Agents Chemother , vol.32 , pp. 1742-1745
    • Baba, M.1    Snoeck, R.2    Pauwels, R.3    De Clercq, E.4
  • 78
    • 0023912916 scopus 로고
    • Dextran sulfate suppression of viruses in the HIV family: inhibition of virion binding to CD4+ cells
    • doi:10.1126/science.2452480
    • Mitsuya H, Looney DJ, Kuno S, Ueno R, Wong-Staal F, Broder S. Dextran sulfate suppression of viruses in the HIV family: inhibition of virion binding to CD4+ cells. Science (1988) 240:646-9. doi:10.1126/science.2452480
    • (1988) Science , vol.240 , pp. 646-649
    • Mitsuya, H.1    Looney, D.J.2    Kuno, S.3    Ueno, R.4    Wong-Staal, F.5    Broder, S.6
  • 79
    • 0030459394 scopus 로고    scopus 로고
    • Role of cell surface glycosaminoglycans of human T cells in human immunodeficiency virus type-1 (HIV-1) infection
    • Ohshiro Y, Murakami T, Matsuda K, Nishioka K, Yoshida K, Yamamoto N. Role of cell surface glycosaminoglycans of human T cells in human immunodeficiency virus type-1 (HIV-1) infection. Microbiol Immunol (1996) 40:827-35.
    • (1996) Microbiol Immunol , vol.40 , pp. 827-835
    • Ohshiro, Y.1    Murakami, T.2    Matsuda, K.3    Nishioka, K.4    Yoshida, K.5    Yamamoto, N.6
  • 80
    • 0028335108 scopus 로고
    • Anti-HIV-1 activity of chemically modified heparins: correlation between binding to the V3 loop of gp120 and inhibition of cellular HIV-1 infection in vitro
    • doi:10.1021/bi00188a029
    • Rider CC, Coombe DR, Harrop HA, Hounsell EF, Bauer C, Feeney J, et al. Anti-HIV-1 activity of chemically modified heparins: correlation between binding to the V3 loop of gp120 and inhibition of cellular HIV-1 infection in vitro. Biochemistry (1994) 33:6974-80. doi:10.1021/bi00188a029
    • (1994) Biochemistry , vol.33 , pp. 6974-6980
    • Rider, C.C.1    Coombe, D.R.2    Harrop, H.A.3    Hounsell, E.F.4    Bauer, C.5    Feeney, J.6
  • 81
    • 0031932210 scopus 로고    scopus 로고
    • Heparin and its derivatives bind to HIV-1 recombinant envelope glycoproteins, rather than to recombinant HIV-1 receptor, CD4
    • doi:10.1093/glycob/8.2.131
    • Harrop HA, Rider CC. Heparin and its derivatives bind to HIV-1 recombinant envelope glycoproteins, rather than to recombinant HIV-1 receptor, CD4. Glycobiology (1998) 8:131-7. doi:10.1093/glycob/8.2.131
    • (1998) Glycobiology , vol.8 , pp. 131-137
    • Harrop, H.A.1    Rider, C.C.2
  • 82
    • 0028914092 scopus 로고
    • Mediation of human immunodeficiency virus type 1 binding by interaction of cell surface heparan sulfate proteoglycans with the V3 region of envelope gp120-gp41
    • Roderiquez G, Oravecz T, Yanagishita M, Bou-Habib DC, Mostowski H, Norcross MA. Mediation of human immunodeficiency virus type 1 binding by interaction of cell surface heparan sulfate proteoglycans with the V3 region of envelope gp120-gp41. J Virol (1995) 69:2233-9.
    • (1995) J Virol , vol.69 , pp. 2233-2239
    • Roderiquez, G.1    Oravecz, T.2    Yanagishita, M.3    Bou-Habib, D.C.4    Mostowski, H.5    Norcross, M.A.6
  • 83
    • 0025271999 scopus 로고
    • Dextran sulfate and other polyanionic anti-HIV compounds specifically interact with the viral gp120 glycoprotein expressed by T-cells persistently infected with HIV-1
    • doi:10.1016/0042-6822(90)90440-3
    • Schols D, Pauwels R, Desmyter J, De Clercq E. Dextran sulfate and other polyanionic anti-HIV compounds specifically interact with the viral gp120 glycoprotein expressed by T-cells persistently infected with HIV-1. Virology (1990) 175:556-61. doi:10.1016/0042-6822(90)90440-3
    • (1990) Virology , vol.175 , pp. 556-561
    • Schols, D.1    Pauwels, R.2    Desmyter, J.3    De Clercq, E.4
  • 84
    • 0026019437 scopus 로고
    • Dextran sulfate blocks antibody binding to the principal neutralizing domain of human immunodeficiency virus type 1 without interfering with gp120-CD4 interactions
    • Callahan LN, Phelan M, Mallinson M, Norcross MA. Dextran sulfate blocks antibody binding to the principal neutralizing domain of human immunodeficiency virus type 1 without interfering with gp120-CD4 interactions. J Virol (1991) 65:1543-50.
    • (1991) J Virol , vol.65 , pp. 1543-1550
    • Callahan, L.N.1    Phelan, M.2    Mallinson, M.3    Norcross, M.A.4
  • 85
    • 0033013344 scopus 로고    scopus 로고
    • Cell-surface heparan sulfate facilitates human immunodeficiency virus type 1 entry into some cell lines but not primary lymphocytes
    • doi:10.1016/S0168-1702(99)00018-0
    • Ibrahim J, Griffin P, Coombe DR, Rider CC, James W. Cell-surface heparan sulfate facilitates human immunodeficiency virus type 1 entry into some cell lines but not primary lymphocytes. Virus Res (1999) 60:159-69. doi:10.1016/S0168-1702(99)00018-0
    • (1999) Virus Res , vol.60 , pp. 159-169
    • Ibrahim, J.1    Griffin, P.2    Coombe, D.R.3    Rider, C.C.4    James, W.5
  • 86
    • 0038735440 scopus 로고    scopus 로고
    • Susceptibility to highly sulphated glycosaminoglycans of human immunodeficiency virus type 1 replication in peripheral blood lymphocytes and monocyte-derived macrophages cell cultures
    • doi:10.1016/S0166-3542(02)00209-7
    • Bartolini B, Di Caro A, Cavallaro RA, Liverani L, Mascellani G, La Rosa G, et al. Susceptibility to highly sulphated glycosaminoglycans of human immunodeficiency virus type 1 replication in peripheral blood lymphocytes and monocyte-derived macrophages cell cultures. Antiviral Res (2003) 58:139-47. doi:10.1016/S0166-3542(02)00209-7
    • (2003) Antiviral Res , vol.58 , pp. 139-147
    • Bartolini, B.1    Di Caro, A.2    Cavallaro, R.A.3    Liverani, L.4    Mascellani, G.5    La Rosa, G.6
  • 88
    • 0034848936 scopus 로고    scopus 로고
    • Syndecans serve as attachment receptors for human immunodeficiency virus type 1 on macrophages
    • doi:10.1128/JVI.75.19.9187-9200.2001
    • Saphire AC, Bobardt MD, Zhang Z, David G, Gallay PA. Syndecans serve as attachment receptors for human immunodeficiency virus type 1 on macrophages. J Virol (2001) 75:9187-200. doi:10.1128/JVI.75.19.9187-9200.2001
    • (2001) J Virol , vol.75 , pp. 9187-9200
    • Saphire, A.C.1    Bobardt, M.D.2    Zhang, Z.3    David, G.4    Gallay, P.A.5
  • 89
    • 66249094195 scopus 로고    scopus 로고
    • Apical interactions of HIV type 1 with polarized HEC-1 cell monolayer modulate R5-HIV type 1 spread by submucosal macrophages
    • doi:10.1089/aid.2008.0156
    • Saidi H, Magri G, Carbonneil C, Bouhlal H, Hocini H, Belec L. Apical interactions of HIV type 1 with polarized HEC-1 cell monolayer modulate R5-HIV type 1 spread by submucosal macrophages. AIDS Res Hum Retroviruses (2009) 25:497-509. doi:10.1089/aid.2008.0156
    • (2009) AIDS Res Hum Retroviruses , vol.25 , pp. 497-509
    • Saidi, H.1    Magri, G.2    Carbonneil, C.3    Bouhlal, H.4    Hocini, H.5    Belec, L.6
  • 90
    • 26444555502 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans mediate attachment and entry of human T-cell leukemia virus type 1 virions into CD4+ T cells
    • doi:10.1128/JVI.79.20.12692-12702.2005
    • Jones KS, Petrow-Sadowski C, Bertolette DC, Huang Y, Ruscetti FW. Heparan sulfate proteoglycans mediate attachment and entry of human T-cell leukemia virus type 1 virions into CD4+ T cells. J Virol (2005) 79:12692-702. doi:10.1128/JVI.79.20.12692-12702.2005
    • (2005) J Virol , vol.79 , pp. 12692-12702
    • Jones, K.S.1    Petrow-Sadowski, C.2    Bertolette, D.C.3    Huang, Y.4    Ruscetti, F.W.5
  • 91
    • 0026705746 scopus 로고
    • The V3 region of the envelope glycoprotein of human immunodeficiency virus type 1 binds sulfated polysaccharides and CD4-derived synthetic peptides
    • Batinic D, Robey FA. The V3 region of the envelope glycoprotein of human immunodeficiency virus type 1 binds sulfated polysaccharides and CD4-derived synthetic peptides. J Biol Chem (1992) 267:6664-71.
    • (1992) J Biol Chem , vol.267 , pp. 6664-6671
    • Batinic, D.1    Robey, F.A.2
  • 92
    • 0033920212 scopus 로고    scopus 로고
    • Selective interactions of polyanions with basic surfaces on human immunodeficiency virus type 1 gp120
    • doi:10.1128/JVI.74.4.1948-1960.2000
    • Moulard M, Lortat-Jacob H, Mondor I, Roca G, Wyatt R, Sodroski J, et al. Selective interactions of polyanions with basic surfaces on human immunodeficiency virus type 1 gp120. J Virol (2000) 74:1948-60. doi:10.1128/JVI.74.4.1948-1960.2000
    • (2000) J Virol , vol.74 , pp. 1948-1960
    • Moulard, M.1    Lortat-Jacob, H.2    Mondor, I.3    Roca, G.4    Wyatt, R.5    Sodroski, J.6
  • 93
    • 0025987790 scopus 로고
    • Pharmacokinetics, toxicity, and activity of intravenous dextran sulfate in human immunodeficiency virus infection
    • doi:10.1128/AAC.35.12.2544
    • Flexner C, Barditch-Crovo PA, Kornhauser DM, Farzadegan H, Nerhood LJ, Chaisson RE, et al. Pharmacokinetics, toxicity, and activity of intravenous dextran sulfate in human immunodeficiency virus infection. Antimicrob Agents Chemother (1991) 35:2544-50. doi:10.1128/AAC.35.12.2544
    • (1991) Antimicrob Agents Chemother , vol.35 , pp. 2544-2550
    • Flexner, C.1    Barditch-Crovo, P.A.2    Kornhauser, D.M.3    Farzadegan, H.4    Nerhood, L.J.5    Chaisson, R.E.6
  • 94
    • 11144234551 scopus 로고    scopus 로고
    • A novel strategy for defining critical amino acid residues involved in protein/glycosaminoglycan interactions
    • doi:10.1074/jbc.M409760200
    • Vives RR, Crublet E, Andrieu JP, Gagnon J, Rousselle P, Lortat-Jacob H. A novel strategy for defining critical amino acid residues involved in protein/glycosaminoglycan interactions. J Biol Chem (2004) 279:54327-33. doi:10.1074/jbc.M409760200
    • (2004) J Biol Chem , vol.279 , pp. 54327-54333
    • Vives, R.R.1    Crublet, E.2    Andrieu, J.P.3    Gagnon, J.4    Rousselle, P.5    Lortat-Jacob, H.6
  • 95
    • 47249111824 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoprotein gp120 features four heparan sulfate binding domains, including the co-receptor binding site
    • doi:10.1074/jbc.M800066200
    • Crublet E, Andrieu JP, Vives RR, Lortat-Jacob H. The HIV-1 envelope glycoprotein gp120 features four heparan sulfate binding domains, including the co-receptor binding site. J Biol Chem (2008) 283:15193-200. doi:10.1074/jbc.M800066200
    • (2008) J Biol Chem , vol.283 , pp. 15193-15200
    • Crublet, E.1    Andrieu, J.P.2    Vives, R.R.3    Lortat-Jacob, H.4
  • 96
    • 0036838693 scopus 로고    scopus 로고
    • Identification of conserved and variable structures in the human immunodeficiency virus gp120 glycoprotein of importance for CXCR4 binding
    • doi:10.1128/JVI.76.21.10791-10800.2002
    • Basmaciogullari S, Babcock GJ, Van Ryk D, Wojtowicz W, Sodroski J. Identification of conserved and variable structures in the human immunodeficiency virus gp120 glycoprotein of importance for CXCR4 binding. J Virol (2002) 76:10791-800. doi:10.1128/JVI.76.21.10791-10800.2002
    • (2002) J Virol , vol.76 , pp. 10791-10800
    • Basmaciogullari, S.1    Babcock, G.J.2    Van Ryk, D.3    Wojtowicz, W.4    Sodroski, J.5
  • 97
    • 51349162563 scopus 로고    scopus 로고
    • Molecular architecture of native HIV-1 gp120 trimers
    • doi:10.1038/nature07159
    • Liu J, Bartesaghi A, Borgnia MJ, Sapiro G, Subramaniam S. Molecular architecture of native HIV-1 gp120 trimers. Nature (2008) 455:109-13. doi:10.1038/nature07159
    • (2008) Nature , vol.455 , pp. 109-113
    • Liu, J.1    Bartesaghi, A.2    Borgnia, M.J.3    Sapiro, G.4    Subramaniam, S.5
  • 98
    • 20444404968 scopus 로고    scopus 로고
    • Heparan sulfate targets the HIV-1 envelope glycoprotein gp120 coreceptor binding site
    • doi:10.1074/jbc.M500911200
    • Vives RR, Imberty A, Sattentau QJ, Lortat-Jacob H. Heparan sulfate targets the HIV-1 envelope glycoprotein gp120 coreceptor binding site. J Biol Chem (2005) 280:21353-7. doi:10.1074/jbc.M500911200
    • (2005) J Biol Chem , vol.280 , pp. 21353-21357
    • Vives, R.R.1    Imberty, A.2    Sattentau, Q.J.3    Lortat-Jacob, H.4
  • 99
    • 70349338616 scopus 로고    scopus 로고
    • A synthetic CD4-heparan sulfate glycoconjugate inhibits CCR5 and CXCR4 HIV-1 attachment and entry
    • doi:10.1038/nchembio.207
    • Baleux F, Loureiro-Morais L, Hersant Y, Clayette P, Arenzana-Seisdedos F, Bonnaffe D, et al. A synthetic CD4-heparan sulfate glycoconjugate inhibits CCR5 and CXCR4 HIV-1 attachment and entry. Nat Chem Biol (2009) 5:743-8. doi:10.1038/nchembio.207
    • (2009) Nat Chem Biol , vol.5 , pp. 743-748
    • Baleux, F.1    Loureiro-Morais, L.2    Hersant, Y.3    Clayette, P.4    Arenzana-Seisdedos, F.5    Bonnaffe, D.6
  • 100
    • 84856370035 scopus 로고    scopus 로고
    • A synthetic heparan sulfate-mimetic peptide conjugated to a mini CD4 displays very high anti-HIV-1 activity independently of coreceptor usage
    • doi:10.1016/j.chembiol.2011.12.009
    • Connell BJ, Baleux F, Coic YM, Clayette P, Bonnaffe D, Lortat-Jacob H. A synthetic heparan sulfate-mimetic peptide conjugated to a mini CD4 displays very high anti-HIV-1 activity independently of coreceptor usage. Chem Biol (2012) 19:131-9. doi:10.1016/j.chembiol.2011.12.009
    • (2012) Chem Biol , vol.19 , pp. 131-139
    • Connell, B.J.1    Baleux, F.2    Coic, Y.M.3    Clayette, P.4    Bonnaffe, D.5    Lortat-Jacob, H.6
  • 101
    • 34848868199 scopus 로고    scopus 로고
    • Structures of the CCR5 N terminus and of a tyrosine-sulfated antibody with HIV-1 gp120 and CD4
    • doi:10.1126/science.1145373
    • Huang CC, Lam SN, Acharya P, Tang M, Xiang SH, Hussan SS, et al. Structures of the CCR5 N terminus and of a tyrosine-sulfated antibody with HIV-1 gp120 and CD4. Science (2007) 317:1930-4. doi:10.1126/science.1145373
    • (2007) Science , vol.317 , pp. 1930-1934
    • Huang, C.C.1    Lam, S.N.2    Acharya, P.3    Tang, M.4    Xiang, S.H.5    Hussan, S.S.6
  • 102
    • 73549092165 scopus 로고    scopus 로고
    • Entry inhibitors in the treatment of HIV-1 infection
    • doi:10.1016/j.antiviral.2009.07.022
    • Tilton JC, Doms RW. Entry inhibitors in the treatment of HIV-1 infection. Antiviral Res (2010) 85:91-100. doi:10.1016/j.antiviral.2009.07.022
    • (2010) Antiviral Res , vol.85 , pp. 91-100
    • Tilton, J.C.1    Doms, R.W.2
  • 103
    • 77249134151 scopus 로고    scopus 로고
    • Twenty-six years of anti-HIV drug discovery: where do we stand and where do we go?
    • doi:10.1021/jm900492g
    • Mehellou Y, De Clercq E. Twenty-six years of anti-HIV drug discovery: where do we stand and where do we go? J Med Chem (2010) 53:521-38. doi:10.1021/jm900492g
    • (2010) J Med Chem , vol.53 , pp. 521-538
    • Mehellou, Y.1    De Clercq, E.2
  • 104
    • 84861888183 scopus 로고    scopus 로고
    • Structure and physicochemical characterisation of heparin
    • doi:10.1007/978-3-642-23056-1_5
    • Mulloy B. Structure and physicochemical characterisation of heparin. Handb Exp Pharmacol (2012) 207:77-98. doi:10.1007/978-3-642-23056-1_5
    • (2012) Handb Exp Pharmacol , vol.207 , pp. 77-98
    • Mulloy, B.1


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