Ebolavirus glycoprotein structure and mechanism of entry

Future Virology

Volumn 4, Issue 6, 2009, Pages 621-635

  Lee, Jeffrey E ^a   Saphire, Erica Ollmann ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Cathepsin; Ebola; Ebolavirus; Filovirus; Fusion protein; Glycoprotein; Membrane fusion; Mucin like domain; Viral attachment; Viral entry

Indexed keywords

CATHEPSIN; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; VIRUS GLYCOPROTEIN; VIRUS HEMAGGLUTININ;

CRYSTAL STRUCTURE; CRYSTALLIZATION; DEMOCRATIC REPUBLIC CONGO; EBOLA VIRUS; ENDOCYTOSIS; GLYCOCALYX; HUMAN; MARBURG VIRUS; MEMBRANE FUSION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN CONFORMATION; PROTEIN GLYCOSYLATION; PROTEIN PROCESSING; REVIEW; SURVIVAL RATE; VIRION; VIRUS ATTACHMENT; VIRUS CELL INTERACTION; VIRUS ENTRY; VIRUS ENVELOPE; VIRUS GENOME; VIRUS HEMORRHAGIC FEVER; VIRUS INFECTIVITY;

EBOLA VIRUS; MARBURGVIRUS; ZAIRE EBOLAVIRUS;

EID: 73949151882     PISSN: 17460794     EISSN: None     Source Type: Journal    
DOI: 10.2217/fvl.09.56     Document Type: Review

References (113)

1. Sanchez A, Geisbert TW, Feldmann H: Filoviridae: Marburg and Ebola viruses. In: Fields Virology. Knipe DM, Howley PM, Griffin DE et al. (Eds). Lippincott Williams and Wilkins, Philadelphia, PA, USA, 1409-1448 (2007). ■ Comprehensive review of Filoviruses.
2. Towner JS, Sealy TK, Khristova ML et al.: Newly discovered ebola virus associated with hemorrhagic fever outbreak in Uganda. PLoS Pathog. 4(11), e1000212 (2008).
3. Kuhn JH: History of filoviral disease outbreaks. In: Filoviruses. Calisher CH (Ed.). SpringerWienNewYork, Wien, Austria (2008). ■ Comprehensive review of Filoviruses.
4. Feldmann H, Geisbert TW, Jahrling PB et al.: Negative sense single stranded RNA viruses. In: Virus Taxonomy: Classification and Nomenclature of Viruses. Fauquet CM, Mayo MA, Maniloff J, Desselberger U, Ball LA (Eds). Elsevier Academic Press, London, UK, 645-653 (2005).
5. Barrette RW, Metwally SA, Rowland JM et al.: Discovery of swine as a host for the Reston ebolavirus. Science 325(5937), 204-206 (2009).
6. Leroy EM, Kumulungui B, Pourrut X et al.: Fruit bats as reservoirs of Ebola virus. Nature 438(7068), 575-576 (2005).
7. Ksiazek TG, Rollin PE, Williams AJ et al.: Clinical virology of Ebola hemorrhagic fever (EHF): virus, virus antigen, and IgG and IgM antibody findings among EHF patients in Kikwit, Democratic Republic of the Congo, 1995. J. Infect. Dis. 179(Suppl. 1), S177-S187 (1999).
8. Geisbert TW, DaddariO-Dicaprio KM, Lewis MG et al.: Vesicular stomatitis virus-based ebola vaccine is well-tolerated and protects immunocompromised nonhuman primates. PLoS Pathog. 4(11), e1000225 (2008). ■ Demonstrates that live-attenuated vesicular stomatitis virus pseudotyped with the Ebolavirus (EBOV) glycoprotein alone is sufficient to protect nonhuman primates from EBOV challenge.
9. Geisbert TW, Geisbert JB, Leung A et al.: Single injection vaccine protects nonhuman primates against Marburg virus and three species of Ebola virus. J. Virol., 83(14), 7296-7304 (2009). ■ Demonstrates that live-attenuated vesicular stomatitis virus pseudotyped with the EBOV glycoprotein alone is sufficient to protect nonhuman primates from EBOV challenge.
10. Jones SM, Feldmann H, Stroher U et al.: Live attenuated recombinant vaccine protects nonhuman primates against Ebola and Marburg viruses. Nat. Med. 11(7), 786-790 (2005). ■ Demonstrates that live-attenuated vesicular stomatitis virus pseudotyped with the EBOV glycoprotein alone is sufficient to protect nonhuman primates from EBOV challenge.
11. Tuffs A: Experimental vaccine may have saved Hamburg scientist from Ebola fever. Br. Med. J. 338, B1223 (2009).
12. Geisbert TW, Jahrling PB: Towards a vaccine against Ebola virus. Expert Rev. Vaccines 2(6), 777-789 (2003).
13. Rotz LD, Khan AS, Lillibridge SR, Ostroff SM, Hughes JM: Public health assessment of potential biological terrorism agents. Emerg. Infect. Dis. 8(2), 225-230 (2002).
14. Borio L, Inglesby T, Peters CJ et al.: Hemorrhagic fever viruses as biological weapons: medical and public health management. JAMA 287(18), 2391-2405 (2002).
15. Sanchez A, Trappier SG, Mahy BW, Peters CJ, Nichol ST: The virion glycoproteins of Ebola viruses are encoded in two reading frames and are expressed through transcriptional editing. Proc. Natl Acad. Sci. USA 93(8), 3602-3607 (1996).
16. Volchkov VE, Becker S, Volchkova VA et al.: GP mRNA of Ebola virus is edited by the Ebola virus polymerase and by T7 and vaccinia virus polymerases. Virology 214(2), 421-430 (1995).
17. Volchkova VA, Feldmann H, Klenk HD, Volchkov VE: The nonstructural small glycoprotein sGP of Ebola virus is secreted as an antiparallel-orientated homodimer. Virology 250(2), 408-414 (1998).
18. Volchkova VA, Klenk HD, Volchkov VE: △-peptide is the carboxy-terminal cleavage fragment of the nonstructural small glycoprotein sGP of Ebola virus. Virology 265(1), 164-171 (1999).
19. Barrientos LG, Martin AM, Rollin PE, Sanchez A: Disulfide bond assignment of the Ebola virus secreted glycoprotein sGP. Biochem. Biophys. Res. Commun. 323(2), 696-702 (2004).
20. Falzarano D, Krokhin O, Wahl-Jensen V et al.: Structure-function analysis of the soluble glycoprotein, sGP, of Ebola virus. Chembiochem 7(10), 1605-1611 (2006).
21. Sanchez A, Yang ZY, Xu L, Nabel GJ, Crews T, Peters CJ: Biochemical analysis of the secreted and virion glycoproteins of Ebola virus. J. Virol. 72(8), 6442-6447 (1998).
22. Falzarano D, Krokhin O, Van Domselaar G et al.: Ebola sGP - the first viral glycoprotein shown to be C-mannosylated. Virology 368(1), 83-90 (2007).
23. Maruyama T, Parren PW, Sanchez A et al.: Recombinant human monoclonal antibodies to Ebola virus. J. Infect. Dis. 179(Suppl. 1), S235-S239 (1999).
24. Wahl-Jensen VM, Afanasieva TA, Seebach J, Stroher U, Feldmann H, Schnittler HJ: Effects of Ebola virus glycoproteins on endothelial cell activation and barrier function. J. Virol. 79(16), 10442-10450 (2005).
25. Jeffers SA, Sanders DA, Sanchez A: Covalent modifications of the Ebola virus glycoprotein. J. Virol. 76(24), 12463-12472 (2002).
26. Volchkov VE, Feldmann H, Volchkova VA, Klenk HD: Processing of the Ebola virus glycoprotein by the proprotein convertase furin. Proc. Natl Acad. Sci. USA 95(10), 5762-5767 (1998).
27. Dolnik O, Volchkova V, Garten W et al.: Ectodomain shedding of the glycoprotein GP of Ebola virus. EMBO J. 23(10), 2175-2184 (2004).
28. Yang ZY, Duckers HJ, Sullivan NJ, Sanchez A, Nabel EG, Nabel GJ: Identification of the Ebola virus glycoprotein as the main viral determinant of vascular cell cytotoxicity and injury. Nat. Med. 6(8), 886-889 (2000).
29. Chan SY, Ma MC, Goldsmith MA: Differential induction of cellular detachment by envelope glycoproteins of Marburg and Ebola (Zaire) viruses. J. Gen. Virol. 81(Pt 9), 2155-2159 (2000).
30. Francica JR, Matukonis MK, Bates P: Requirements for cell rounding and surface protein down-regulation by Ebola virus glycoprotein. Virology 383(2), 237-247 (2009).
31. Simmons G, Wool-Lewis RJ, Baribaud F, Netter RC, Bates P: Ebola virus glycoproteins induce global surface protein down-modulation and loss of cell adherence. J. Virol. 76(5), 2518-2528 (2002).
32. Sullivan NJ, Peterson M, Yang ZY et al.: Ebola virus glycoprotein toxicity is mediated by a dynamin-dependent protein-trafficking pathway. J. Virol. 79(1), 547-553 (2005).
33. Alazard-Dany N, Volchkova V, Reynard O et al.: Ebola virus glycoprotein GP is not cytotoxic when expressed constitutively at a moderate level. J. Gen. Virol. 87(Pt 5), 1247-1257 (2006).
34. Lee JE, Fusco MH, Hessell AJ, Oswald WB, Burton DR, Saphire EO: Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor. Nature 454(7201), 177-183 (2008). ■■ Describes the first structure of the prefusion, trimeric EBOV glycoprotein in complex with a neutralizing antibody identified from a human survivor of the 1995 Kikwit, Zaire outbreak, and provides a model for EBOV entry and future therapeutic development.
35. Kaletsky RL, Simmons G, Bates P: Proteolysis of the Ebola virus glycoproteins enhances virus binding and infectivity. J. Virol. 81(24), 13378-13384 (2007). ■ First study to demonstrate that cathepsin-cleaved EBOV glycoprotein exhibits improved attachment to target cells.
36. Lee JE, Kuehne A, Abelson DM, Fusco ML, Hart MK, Saphire EO: Complex of a protective antibody with its Ebola virus GP peptide epitope: unusual features of a V λ x light chain. J. Mol. Biol. 375(1), 202-216 (2008).
37. Gallaher WR: Similar structural models of the transmembrane proteins of Ebola and avian sarcoma viruses. Cell 85(4), 477-478 (1996).
38. Wilson IA, Skehel JJ, Wiley DC: Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature 289(5796), 366-373 (1981).
39. Yin HS, Wen X, Paterson RG, Lamb RA, Jardetzky TS: Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation. Nature 439(7072), 38-44 (2006).
40. Rey FA, Heinz FX, Mandl C, Kunz C, Harrison SC: The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution. Nature 375(6529), 291-298 (1995).
41. Modis Y, Ogata S, Clements D, Harrison SC: Structure of the dengue virus envelope protein after membrane fusion. Nature 427(6972), 313-319 (2004).
42. Nybakken GE, Oliphant T, Johnson S, Burke S, Diamond MS, Fremont DH: Structural basis of West Nile virus neutralization by a therapeutic antibody. Nature 437(7059), 764-769 (2005).
43. Roche S, Bressanelli S, Rey FA, Gaudin Y: Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G. Science 313(5784), 187-191 (2006).
44. Roche S, Rey FA, Gaudin Y, Bressanelli S: Structure of the prefusion form of the vesicular stomatitis virus glycoprotein G. Science 315(5813), 843-848 (2007).
45. Heldwein EE, Lou H, Bender FC, Cohen GH, Eisenberg RJ, Harrison SC: Crystal structure of glycoprotein B from herpes simplex virus 1. Science 313(5784), 217-220 (2006).
46. Weissenhorn W, Carfi A, Lee KH, Skehel JJ, Wiley DC: Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain. Mol. Cell 2(5), 605-616 (1998).
47. Ritchie GE: The glycosylation of viral envelope glycoproteins and the effect of glycosidase inhibitors on virus replication and glycoprotein properties. D.Phil thesis. Linacre College, University of Oxford, Oxford, UK (2005).
48. Maruyama T, Rodriguez LL, Jahrling PB et al.: Ebola virus can be effectively neutralized by antibody produced in natural human infection. J. Virol. 73(7), 6024-6030 (1999).
49. Takada A, Feldmann H, Stroeher U et al.: Identification of protective epitopes on ebola virus glycoprotein at the single amino acid level by using recombinant vesicular stomatitis viruses. J. Virol. 77(2), 1069-1074 (2003).
50. Wilson JA, Hevey M, Bakken R et al.: Epitopes involved in antibody-mediated protection from Ebola virus. Science 287(5458), 1664-1666 (2000).
51. Lee JE, Saphire EO: Neutralizing Ebolavirus: structural insights into the envelope glycoprotein and antibodies targeted against it. Curr. Opin. Struct. Biol. 19(4), 408-417 (2009).
52. Parren PWHI, Geisbert TW, Maruyama T, Jahrling PB, Burton DR: Pre- and post-exposure prophylaxis of Ebola virus infection in an animal model by passive transfer of a neutralizing human antibody. J. Virol. 76(12), 6408-6412 (2002).
53. Oswald WB, Geisbert TW, Davis KJ et al.: Neutralizing antibody fails to impact the course of Ebola virus infection in monkeys. PLoS Pathog. 3(1), e9 (2007).
54. Ekiert DC, Bhabha G, Elsliger MA et al.: Antibody recognition of a highly conserved influenza virus epitope. Science 324(5924), 246-251 (2009).
55. Sui J, Hwang WC, Perez S et al.: Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses. Nat. Struct. Mol. Biol. 16(3), 265-273 (2009).
56. Casadevall A, Scharff MD: Return to the past: the case for antibody-based therapies in infectious diseases. Clin. Infect. Dis. 21(1), 150-161 (1995).
57. Hangartner L, Zinkernagel RM, Hengartner H: Antiviral antibody responses: the two extremes of a wide spectrum. Nat. Rev. Immunol. 6(3), 231-243 (2006).
58. Parren PW, Burton DR: The antiviral activity of antibodies in vitro and in vivo. Adv. Immunol. 77, 195-262 (2001).
59. Mupapa K, Massamba M, Kibadi K et al.: Treatment of Ebola hemorrhagic fever with blood transfusions from convalescent patients. J. Infect. Dis. 179(Suppl. 1), S18-S23 (1999).
60. Borisevich IV, Mikhailov VV, Krasnianskii VP et al.: Development and study of the properties of immunoglobulin against Ebola fever. Vopr. Virusol. 40(6), 270-273 (1995).
61. Gupta M, Mahanty S, Bray M, Ahmed R, Rollin PE: Passive transfer of antibodies protects immunocompetent and imunodeficient mice against lethal Ebola virus infection without complete inhibition of viral replication. J. Virol. 75(10), 4649-4654 (2001).
62. Mikhailov VV, Borisevich IV, Chernikova NK, Potryvaeva NV, Krasnianskii VP: The evaluation in hamadryas baboons of the possibility for the specific prevention of Ebola fever. Vopr. Virusol. 39(2), 82-84 (1994).
63. Kudoyarova-Zubavichene NM, Sergeyev NN, Chepurnov AA, Netesov SV: Preparation and use of hyperimmune serum for prophylaxis and therapy of Ebola virus infections. J. Infect. Dis. 179(Suppl. 1), S218-S223 (1999).
64. Sadek RF, Khan AS, Stevens G, Peters CJ, Ksiazek TG: Ebola hemorrhagic fever, Democratic Republic of the Congo, 1995: determinants of survival. J. Infect. Dis. 179(Suppl. 1), S24-S27 (1999).
65. Jahrling PB, Geisbert J, Swearengen JR et al.: Passive immunization of Ebola virus-infected cynomolgus monkeys with immunoglobulin from hyperimmune horses. Arch. Virol. Suppl. 11, 135-140 (1996).
66. Jahrling PB, Geisbert JB, Swearengen JR, Larsen T, Geisbert TW: Ebola hemorrhagic fever: evaluation of passive immunotherapy in nonhuman primates. J. Infect. Dis. 196(Suppl. 2), S400-S403 (2007).
67. Jahrling PB, Geisbert TW, Geisbert JB et al.: Evaluation of immune globulin and recombinant interferon-α2b for treatment of experimental Ebola virus infections. J. Infect. Dis. 179(Suppl. 1), S224-S234 (1999).
68. Alvarez CP, Lasala F, Carrillo J, Muniz O, Corbi AL, Delgado R: C-type lectins DC-SIGN and L-SIGN mediate cellular entry by Ebola virus in cis and in trans. J. Virol., 76(13), 6841-6844 (2002).
69. Simmons G, Reeves JD, Grogan CC et al.: DC-SIGN and DC-SIGNR bind Ebola glycoproteins and enhance infection of macrophages and endothelial cells. Virology 305(1), 115-123 (2003).
70. Dominguez-Soto A, Aragoneses-Fenoll L, MartiN-Gayo E et al.: The DC-SIGN-related lectin LSECtin mediates antigen capture and pathogen binding by human myeloid cells. Blood 109(12), 5337-5345 (2007).
71. Gramberg T, Soilleux E, Fisch T et al.: Interactions of LSECtin and DC-SIGN/ DC-SIGNR with viral ligands: differential pH dependence, internalization and virion binding. Virology 373(1), 189-201 (2008).
72. Takada A, Fujioka K, Tsuiji M et al.: Human macrophage C-type lectin specific for galactose and N-acetylgalactosamine promotes filovirus entry. J. Virol. 78(6), 2943-2947 (2004).
73. Takada A, Watanabe S, Ito H, Okazaki K, Kida H, Kawaoka Y: Downregulation of beta1 integrins by Ebola virus glycoprotein: implication for virus entry. Virology 278(1), 20-26 (2000).
74. Shimojima M, Takada A, Ebihara H et al.: Tyro3 family-mediated cell entry of Ebola and Marburg viruses. J. Virol. 80(20), 10109-10116 (2006).
75. Empig CJ, Goldsmith MA: Association of the caveola vesicular system with cellular entry by filoviruses. J. Virol. 76(10), 5266-5270 (2002).
76. Sanchez A: Analysis of filovirus entry into Vero E6 cells, using inhibitors of endocytosis, endosomal acidification, structural integrity, and cathepsin (B and L) activity. J. Infect. Dis. 196(Suppl. 2), S251-S258 (2007).
77. Simmons G, Rennekamp AJ, Chai N, Vandenberghe LH, Riley JL, Bates P: Folate receptor α and caveolae are not required for Ebola virus glycoprotein-mediated viral infection. J. Virol. 77(24), 13433-13438 (2003).
78. Brindley MA, Hughes L, Ruiz A et al.: Ebola virus glycoprotein 1: identification of residues important for binding and postbinding events. J. Virol. 81(14), 7702-7709 (2007).
79. Manicassamy B, Wang J, Jiang H, Rong L: Comprehensive analysis of Ebola virus GP1 in viral entry. J. Virol. 79(8), 4793-4805 (2005).
80. Mpanju OM, Towner JS, Dover JE, Nichol ST, Wilson CA: Identification of two amino acid residues on Ebola virus glycoprotein 1 critical for cell entry. Virus Res. 121(2), 205-214 (2006).
81. Kuhn JH, Radoshitzky SR, Guth AC et al.: Conserved receptor-binding domains of Lake Victoria Marburgvirus and Zaire Ebolavirus bind a common receptor. J. Biol. Chem. 281(23), 15951-15958 (2006).
82. Dube D, Brecher MB, Delos SE et al.: The primed ebolavirus glycoprotein (19-kilodalton GP1,2): sequence and residues critical for host cell binding. J. Virol., 83(7), 2883-2891 (2009). ■ Identifies the cathepsin cleavage site on glycoprotein1 and shows that the patch of lysine residues on the surface of glycoprotein1 are involved in viral attachment.
83. Chandran K, Sullivan NJ, Felbor U, Whelan SP, Cunningham JM: Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science 308(5728), 1643-1645 (2005). ■■ Describes the original identification of the essential role for cathepsin B and L in EBOV glycoprotein-mediated entry.
84. Schornberg K, Matsuyama S, Kabsch K, Delos S, Bouton A, White J: Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein. J. Virol. 80(8), 4174-4178 (2006).
85. Diederich S, Thiel L, Maisner A: Role of endocytosis and cathepsin-mediated activation in Nipah virus entry. Virology 375(2), 391-400 (2008).
86. Pager CT, Craft WW, Jr., Patch J, Dutch RE: A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L. Virology 346(2), 251-257 (2006).
87. Pager CT, Dutch RE: Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein. J. Virol. 79(20), 12714-12720 (2005).
88. Simmons G, Gosalia DN, Rennekamp AJ, Reeves JD, Diamond SL, Bates P: Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry. Proc. Natl Acad. Sci. USA 102(33), 11876-11881 (2005).
89. Spear PG: Herpes simplex virus: receptors and ligands for cell entry. Cell Microbiol. 6(5), 401-410 (2004).
90. Harrison SC: Mechanism of membrane fusion by viral envelope proteins. Adv. Virus Res. 64, 231-261 (2005). ■■ Thorough and informative review on the three classes of viral membrane fusion proteins and their mechanisms of viral entry.
91. Harrison SC: Viral membrane fusion. Nat. Struct. Mol. Biol. 15(7), 690-698 (2008). ■■ Thorough and informative review on the three classes of viral membrane fusion proteins and their mechanisms of viral entry.
92. Lamb RA, Jardetzky TS: Structural basis of viral invasion: lessons from paramyxovirus F. Curr. Opin Struct. Biol. 17(4), 427-436 (2007). ■■ Thorough and informative review on the three classes of viral membrane fusion proteins and their mechanisms of viral entry.
93. White JM, Delos SE, Brecher M, Schornberg K: Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme. Crit. Rev. Biochem. Mol. Biol. 43(3), 189-219 (2008). ■■ Thorough and informative review on the three classes of viral membrane fusion proteins and their mechanisms of viral entry.
94. Stieneke-Grober A, Vey M, Angliker H et al.: Influenza virus hemagglutinin with multibasic cleavage site is activated by furin, a subtilisin-like endoprotease. EMBO J. 11(7), 2407-2414 (1992).
95. Hallenberger S, Bosch V, Angliker H, Shaw E, Klenk HD, Garten W: Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160. Nature 360(6402), 358-361 (1992).
96. Chen J, Lee KH, Steinhauer DA, Stevens DJ, Skehel JJ, Wiley DC: Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation. Cell 95(3), 409-417 (1998).
97. Thoennes S, Li ZN, Lee BJ et al.: Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion. Virology 370(2), 403-414 (2008).
98. Wool-Lewis RJ, Bates P: Endoproteolytic processing of the Ebola virus envelope glycoprotein: cleavage is not required for function. J. Virol. 73(2), 1419-1426. (1999).
99. Neumann G, Geisbert TW, Ebihara H et al.: Proteolytic processing of the Ebola virus glycoprotein is not critical for Ebola virus replication in nonhuman primates. J. Virol. 81(6), 2995-2998 (2007).
100. Bullough PA, Hughson FM, Skehel JJ, Wiley DC: Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371(6492), 37-43 (1994).
101. Kampmann T, Mueller DS, Mark AE, Young PR, Kobe B: The role of histidine residues in low-pH-mediated viral membrane fusion. Structure 14(10), 1481-1487 (2006).
102. Trkola A, Dragic T, Arthos J et al.: CD4-dependent, antibody-sensitive interactions between HIV-1 and its co-receptor CCR-5. Nature 384(6605), 184-187 (1996).
103. Wu L, Gerard NP, Wyatt R et al.: CD4-induced interaction of primary HIV-1 gp120 glycoproteins with the chemokine receptor CCR-5. Nature 384(6605), 179-183 (1996).
104. Smith JG, Mothes W, Blacklow SC, Cunningham JM: The mature avian leukosis virus subgroup A envelope glycoprotein is metastable, and refolding induced by the synergistic effects of receptor binding and low pH is coupled to infection. J. Virol. 78(3), 1403-1410 (2004).
105. Chan SY, Speck RF, Ma MC, Goldsmith MA: Distinct mechanisms of entry by envelope glycoproteins of Marburg and Ebola (Zaire) viruses. J. Virol. 74(10), 4933-4937 (2000).
106. Takada A, Robison C, Goto H et al.: A system for functional analysis of Ebola virus glycoprotein. Proc. Natl Acad. Sci. USA 94(26), 14764-14769 (1997).
107. Wool-Lewis RJ, Bates P: Characterization of Ebola virus entry by using pseudotyped viruses: identification of receptor-deficient cell lines. J. Virol. 72(4), 3155-3160 (1998).
108. Malashkevich VN, Schneider BJ, McNally ML, Milhollen MA, Pang JX, Kim PS: Core structure of the envelope glycoprotein GP2 from Ebola virus at 1.9-Å resolution. Proc. Natl Acad. Sci. USA 96(6), 2662-2667 (1999).
109. Freitas MS, Gaspar LP, Lorenzoni M et al.: Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts. J. Biol. Chem. 282(37), 27306-27314 (2007).
110. Gomara MJ, Mora P, Mingarro I, Nieva JL: Roles of a conserved proline in the internal fusion peptide of Ebola glycoprotein. FEBS Lett. 569(1-3), 261-266 (2004).
111. Chan DC, Fass D, Berger JM, Kim PS: Core structure of gp41 from the HIV envelope glycoprotein. Cell 89(2), 263-273 (1997).
112. Chandran K, Li Q, Fabozzi G, Sullivan NJ, Cunningham JM: Cysteine cathepsins are host factors for filovirus infection. In: Keystone Symposia: Cell Biology of Virus Entry, Replication and Pathogenesis. Keystone Symposia, Victoria, BC, Canada, 29 (2008).
113. Model of EBOV GP-mediated entry. www.nature.com/nature/journal/v454/ n7201/index.html