메뉴 건너뛰기




Volumn 168, Issue 5, 2017, Pages 904-915.e10

The Ancient Gamete Fusogen HAP2 Is a Eukaryotic Class II Fusion Protein

Author keywords

Chlamydomonas reinhardtii; class II fusion protein; crystal structure; gamete fusion; HAP2; lipid insertion; membrane fusion; sexual reproduction; transmission blocking malaria vaccine; virus entry

Indexed keywords

BLOCKING ANTIBODY; CYSTEINE; HAP2 PROTEIN; INFLUENZA VIRUS HEMAGGLUTININ; LIPOSOME; MEMBRANE FUSION PROTEIN; MEMBRANE PROTEIN; MUTANT PROTEIN; TRYPSIN; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN; VIRUS FUSION PROTEIN; PLANT PROTEIN; PROTOZOAL PROTEIN; RECOMBINANT PROTEIN;

EID: 85014075665     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2017.01.024     Document Type: Article
Times cited : (145)

References (70)
  • 1
    • 79960903181 scopus 로고    scopus 로고
    • Class III viral membrane fusion proteins
    • Backovic, M., Jardetzky, T.S., Class III viral membrane fusion proteins. Adv. Exp. Med. Biol. 714 (2011), 91–101.
    • (2011) Adv. Exp. Med. Biol. , vol.714 , pp. 91-101
    • Backovic, M.1    Jardetzky, T.S.2
  • 2
    • 84881313610 scopus 로고    scopus 로고
    • Regulated membrane protein entry into flagella is facilitated by cytoplasmic microtubules and does not require IFT
    • Belzile, O., Hernandez-Lara, C.I., Wang, Q., Snell, W.J., Regulated membrane protein entry into flagella is facilitated by cytoplasmic microtubules and does not require IFT. Curr. Biol. 23 (2013), 1460–1465.
    • (2013) Curr. Biol. , vol.23 , pp. 1460-1465
    • Belzile, O.1    Hernandez-Lara, C.I.2    Wang, Q.3    Snell, W.J.4
  • 3
    • 84899471338 scopus 로고    scopus 로고
    • Juno is the egg Izumo receptor and is essential for mammalian fertilization
    • Bianchi, E., Doe, B., Goulding, D., Wright, G.J., Juno is the egg Izumo receptor and is essential for mammalian fertilization. Nature 508 (2014), 483–487.
    • (2014) Nature , vol.508 , pp. 483-487
    • Bianchi, E.1    Doe, B.2    Goulding, D.3    Wright, G.J.4
  • 4
    • 67651151027 scopus 로고    scopus 로고
    • Plasmodium berghei HAP2 induces strong malaria transmission-blocking immunity in vivo and in vitro
    • Blagborough, A.M., Sinden, R.E., Plasmodium berghei HAP2 induces strong malaria transmission-blocking immunity in vivo and in vitro. Vaccine 27 (2009), 5187–5194.
    • (2009) Vaccine , vol.27 , pp. 5187-5194
    • Blagborough, A.M.1    Sinden, R.E.2
  • 5
    • 0242300065 scopus 로고    scopus 로고
    • Genomewide screening for fusogenic human endogenous retrovirus envelopes identifies syncytin 2, a gene conserved on primate evolution
    • Blaise, S., de Parseval, N., Bénit, L., Heidmann, T., Genomewide screening for fusogenic human endogenous retrovirus envelopes identifies syncytin 2, a gene conserved on primate evolution. Proc. Natl. Acad. Sci. USA 100 (2003), 13013–13018.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13013-13018
    • Blaise, S.1    de Parseval, N.2    Bénit, L.3    Heidmann, T.4
  • 10
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta. Crystallogr. D. Biol. Crystallogr. 50 (1994), 760–763.
    • (1994) Acta. Crystallogr. D. Biol. Crystallogr. , vol.50 , pp. 760-763
  • 11
    • 84969389441 scopus 로고    scopus 로고
    • Expression and function of endogenous retroviruses in the placenta
    • Denner, J., Expression and function of endogenous retroviruses in the placenta. APMIS 124 (2016), 31–43.
    • (2016) APMIS , vol.124 , pp. 31-43
    • Denner, J.1
  • 12
    • 84873205968 scopus 로고    scopus 로고
    • Crystal structure of glycoprotein C from Rift Valley fever virus
    • Dessau, M., Modis, Y., Crystal structure of glycoprotein C from Rift Valley fever virus. Proc. Natl. Acad. Sci. USA 110 (2013), 1696–1701.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 1696-1701
    • Dessau, M.1    Modis, Y.2
  • 14
    • 84872973964 scopus 로고    scopus 로고
    • Functional and evolutionary insight from the crystal structure of rubella virus protein E1
    • DuBois, R.M., Vaney, M.-C., Tortorici, M.A., Kurdi, R.A., Barba-Spaeth, G., Krey, T., Rey, F.A., Functional and evolutionary insight from the crystal structure of rubella virus protein E1. Nature 493 (2013), 552–556.
    • (2013) Nature , vol.493 , pp. 552-556
    • DuBois, R.M.1    Vaney, M.-C.2    Tortorici, M.A.3    Kurdi, R.A.4    Barba-Spaeth, G.5    Krey, T.6    Rey, F.A.7
  • 15
    • 84908365418 scopus 로고    scopus 로고
    • Evidence for participation of GCS1 in fertilization of the starlet sea anemone Nematostella vectensis: implication of a common mechanism of sperm-egg fusion in plants and animals
    • Ebchuqin, E., Yokota, N., Yamada, L., Yasuoka, Y., Akasaka, M., Arakawa, M., Deguchi, R., Mori, T., Sawada, H., Evidence for participation of GCS1 in fertilization of the starlet sea anemone Nematostella vectensis: implication of a common mechanism of sperm-egg fusion in plants and animals. Biochem. Biophys. Res. Commun. 451 (2014), 522–528.
    • (2014) Biochem. Biophys. Res. Commun. , vol.451 , pp. 522-528
    • Ebchuqin, E.1    Yokota, N.2    Yamada, L.3    Yasuoka, Y.4    Akasaka, M.5    Arakawa, M.6    Deguchi, R.7    Mori, T.8    Sawada, H.9
  • 19
    • 0035941478 scopus 로고    scopus 로고
    • New BEL-like LTR-retrotransposons in Fugu rubripes, Caenorhabditis elegans, and Drosophila melanogaster
    • Frame, I.G., Cutfield, J.F., Poulter, R.T., New BEL-like LTR-retrotransposons in Fugu rubripes, Caenorhabditis elegans, and Drosophila melanogaster. Gene 263 (2001), 219–230.
    • (2001) Gene , vol.263 , pp. 219-230
    • Frame, I.G.1    Cutfield, J.F.2    Poulter, R.T.3
  • 20
    • 0141429172 scopus 로고    scopus 로고
    • Visualization of the target-membrane-inserted fusion protein of Semliki Forest virus by combined electron microscopy and crystallography
    • Gibbons, D.L., Erk, I., Reilly, B., Navaza, J., Kielian, M., Rey, F.A., Lepault, J., Visualization of the target-membrane-inserted fusion protein of Semliki Forest virus by combined electron microscopy and crystallography. Cell 114 (2003), 573–583.
    • (2003) Cell , vol.114 , pp. 573-583
    • Gibbons, D.L.1    Erk, I.2    Reilly, B.3    Navaza, J.4    Kielian, M.5    Rey, F.A.6    Lepault, J.7
  • 21
    • 1642540249 scopus 로고    scopus 로고
    • Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus
    • Gibbons, D.L., Vaney, M.C., Roussel, A., Vigouroux, A., Reilly, B., Lepault, J., Kielian, M., Rey, F.A., Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus. Nature 427 (2004), 320–325.
    • (2004) Nature , vol.427 , pp. 320-325
    • Gibbons, D.L.1    Vaney, M.C.2    Roussel, A.3    Vigouroux, A.4    Reilly, B.5    Lepault, J.6    Kielian, M.7    Rey, F.A.8
  • 22
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: analysis of multiple sequence alignments in PostScript
    • Gouet, P., Courcelle, E., Stuart, D.I., Métoz, F., ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15 (1999), 305–308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Métoz, F.4
  • 25
    • 84937761010 scopus 로고    scopus 로고
    • Viral membrane fusion
    • Harrison, S.C., Viral membrane fusion. Virology 479-480 (2015), 498–507.
    • (2015) Virology , vol.479-480 , pp. 498-507
    • Harrison, S.C.1
  • 27
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • Holm, L., Park, J., DaliLite workbench for protein structure comparison. Bioinformatics 16 (2000), 566–567.
    • (2000) Bioinformatics , vol.16 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 29
    • 85027632383 scopus 로고
    • Automatic indexing of rotation diffraction patterns
    • Kabsch, W., Automatic indexing of rotation diffraction patterns. J. Appl. Cryst. 21 (1988), 67–72.
    • (1988) J. Appl. Cryst. , vol.21 , pp. 67-72
    • Kabsch, W.1
  • 30
    • 53549088587 scopus 로고    scopus 로고
    • The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines
    • Kadlec, J., Loureiro, S., Abrescia, N.G., Stuart, D.I., Jones, I.M., The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines. Nat. Struct. Mol. Biol. 15 (2008), 1024–1030.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1024-1030
    • Kadlec, J.1    Loureiro, S.2    Abrescia, N.G.3    Stuart, D.I.4    Jones, I.M.5
  • 32
    • 31344432402 scopus 로고    scopus 로고
    • Virus membrane-fusion proteins: more than one way to make a hairpin
    • Kielian, M., Rey, F.A., Virus membrane-fusion proteins: more than one way to make a hairpin. Nat. Rev. Microbiol. 4 (2006), 67–76.
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 67-76
    • Kielian, M.1    Rey, F.A.2
  • 33
    • 84873849253 scopus 로고    scopus 로고
    • Structure of a dengue virus envelope protein late-stage fusion intermediate
    • Klein, D.E., Choi, J.L., Harrison, S.C., Structure of a dengue virus envelope protein late-stage fusion intermediate. J. Virol. 87 (2013), 2287–2293.
    • (2013) J. Virol. , vol.87 , pp. 2287-2293
    • Klein, D.E.1    Choi, J.L.2    Harrison, S.C.3
  • 34
    • 0028152964 scopus 로고
    • Membrane and protein interactions of a soluble form of the Semliki Forest virus fusion protein
    • Klimjack, M.R., Jeffrey, S., Kielian, M., Membrane and protein interactions of a soluble form of the Semliki Forest virus fusion protein. J. Virol. 68 (1994), 6940–6946.
    • (1994) J. Virol. , vol.68 , pp. 6940-6946
    • Klimjack, M.R.1    Jeffrey, S.2    Kielian, M.3
  • 36
    • 26444506252 scopus 로고    scopus 로고
    • Domain III from class II fusion proteins functions as a dominant-negative inhibitor of virus membrane fusion
    • Liao, M., Kielian, M., Domain III from class II fusion proteins functions as a dominant-negative inhibitor of virus membrane fusion. J. Cell Biol. 171 (2005), 111–120.
    • (2005) J. Cell Biol. , vol.171 , pp. 111-120
    • Liao, M.1    Kielian, M.2
  • 37
    • 77951997126 scopus 로고    scopus 로고
    • In vitro reconstitution reveals key intermediate states of trimer formation by the dengue virus membrane fusion protein
    • Liao, M., Sánchez-San Martín, C., Zheng, A., Kielian, M., In vitro reconstitution reveals key intermediate states of trimer formation by the dengue virus membrane fusion protein. J. Virol. 84 (2010), 5730–5740.
    • (2010) J. Virol. , vol.84 , pp. 5730-5740
    • Liao, M.1    Sánchez-San Martín, C.2    Zheng, A.3    Kielian, M.4
  • 38
    • 0001384802 scopus 로고
    • The Mechanism of Fertilization
    • Lillie, F.R., The Mechanism of Fertilization. Science 38 (1913), 524–528.
    • (1913) Science , vol.38 , pp. 524-528
    • Lillie, F.R.1
  • 40
    • 77951245390 scopus 로고    scopus 로고
    • Membrane fusion triggers rapid degradation of two gamete-specific, fusion-essential proteins in a membrane block to polygamy in Chlamydomonas
    • Liu, Y., Misamore, M.J., Snell, W.J., Membrane fusion triggers rapid degradation of two gamete-specific, fusion-essential proteins in a membrane block to polygamy in Chlamydomonas. Development 137 (2010), 1473–1481.
    • (2010) Development , vol.137 , pp. 1473-1481
    • Liu, Y.1    Misamore, M.J.2    Snell, W.J.3
  • 41
    • 84923287323 scopus 로고    scopus 로고
    • The cytoplasmic domain of the gamete membrane fusion protein HAP2 targets the protein to the fusion site in Chlamydomonas and regulates the fusion reaction
    • Liu, Y., Pei, J., Grishin, N., Snell, W.J., The cytoplasmic domain of the gamete membrane fusion protein HAP2 targets the protein to the fusion site in Chlamydomonas and regulates the fusion reaction. Development 142 (2015), 962–971.
    • (2015) Development , vol.142 , pp. 962-971
    • Liu, Y.1    Pei, J.2    Grishin, N.3    Snell, W.J.4
  • 42
    • 84871961238 scopus 로고    scopus 로고
    • Structure of the St. Louis encephalitis virus postfusion envelope trimer
    • Luca, V.C., Nelson, C.A., Fremont, D.H., Structure of the St. Louis encephalitis virus postfusion envelope trimer. J. Virol. 87 (2013), 818–828.
    • (2013) J. Virol. , vol.87 , pp. 818-828
    • Luca, V.C.1    Nelson, C.A.2    Fremont, D.H.3
  • 43
    • 0033799581 scopus 로고    scopus 로고
    • Poised for contagion: evolutionary origins of the infectious abilities of invertebrate retroviruses
    • Malik, H.S., Henikoff, S., Eickbush, T.H., Poised for contagion: evolutionary origins of the infectious abilities of invertebrate retroviruses. Genome Res. 10 (2000), 1307–1318.
    • (2000) Genome Res. , vol.10 , pp. 1307-1318
    • Malik, H.S.1    Henikoff, S.2    Eickbush, T.H.3
  • 47
    • 0038508866 scopus 로고    scopus 로고
    • The Chlamydomonas Fus1 protein is present on the mating type plus fusion organelle and required for a critical membrane adhesion event during fusion with minus gametes
    • Misamore, M.J., Gupta, S., Snell, W.J., The Chlamydomonas Fus1 protein is present on the mating type plus fusion organelle and required for a critical membrane adhesion event during fusion with minus gametes. Mol. Biol. Cell 14 (2003), 2530–2542.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2530-2542
    • Misamore, M.J.1    Gupta, S.2    Snell, W.J.3
  • 49
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • Modis, Y., Ogata, S., Clements, D., Harrison, S.C., Structure of the dengue virus envelope protein after membrane fusion. Nature 427 (2004), 313–319.
    • (2004) Nature , vol.427 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 51
    • 30344459431 scopus 로고    scopus 로고
    • Generative cell specific 1 is essential for angiosperm fertilization
    • Mori, T., Kuroiwa, H., Higashiyama, T., Kuroiwa, T., Generative cell specific 1 is essential for angiosperm fertilization. Nat. Cell Biol. 8 (2006), 64–71.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 64-71
    • Mori, T.1    Kuroiwa, H.2    Higashiyama, T.3    Kuroiwa, T.4
  • 52
    • 84892813896 scopus 로고    scopus 로고
    • Gamete attachment requires GEX2 for successful fertilization in Arabidopsis
    • Mori, T., Igawa, T., Tamiya, G., Miyagishima, S.Y., Berger, F., Gamete attachment requires GEX2 for successful fertilization in Arabidopsis. Curr. Biol. 24 (2014), 170–175.
    • (2014) Curr. Biol. , vol.24 , pp. 170-175
    • Mori, T.1    Igawa, T.2    Tamiya, G.3    Miyagishima, S.Y.4    Berger, F.5
  • 53
    • 66149103151 scopus 로고    scopus 로고
    • Crystal structure of dengue virus type 1 envelope protein in the postfusion conformation and its implications for membrane fusion
    • Nayak, V., Dessau, M., Kucera, K., Anthony, K., Ledizet, M., Modis, Y., Crystal structure of dengue virus type 1 envelope protein in the postfusion conformation and its implications for membrane fusion. J. Virol. 83 (2009), 4338–4344.
    • (2009) J. Virol. , vol.83 , pp. 4338-4344
    • Nayak, V.1    Dessau, M.2    Kucera, K.3    Anthony, K.4    Ledizet, M.5    Modis, Y.6
  • 54
    • 84877946500 scopus 로고    scopus 로고
    • Comparative genomics in Chlamydomonas and Plasmodium identifies an ancient nuclear envelope protein family essential for sexual reproduction in protists, fungi, plants, and vertebrates
    • Ning, J., Otto, T.D., Pfander, C., Schwach, F., Brochet, M., Bushell, E., Goulding, D., Sanders, M., Lefebvre, P.A., Pei, J., et al. Comparative genomics in Chlamydomonas and Plasmodium identifies an ancient nuclear envelope protein family essential for sexual reproduction in protists, fungi, plants, and vertebrates. Genes Dev. 27 (2013), 1198–1215.
    • (2013) Genes Dev. , vol.27 , pp. 1198-1215
    • Ning, J.1    Otto, T.D.2    Pfander, C.3    Schwach, F.4    Brochet, M.5    Bushell, E.6    Goulding, D.7    Sanders, M.8    Lefebvre, P.A.9    Pei, J.10
  • 55
    • 84887168706 scopus 로고    scopus 로고
    • The cell biology of mammalian fertilization
    • Okabe, M., The cell biology of mammalian fertilization. Development 140 (2013), 4471–4479.
    • (2013) Development , vol.140 , pp. 4471-4479
    • Okabe, M.1
  • 57
    • 85013645762 scopus 로고    scopus 로고
    • Structure-function studies link class II viral fusogens and the ancestral gamete fusion protein HAP2
    • Published online February 23, 2017
    • Pinello, J.F., Lai, A.L., Millet, J.K., Cassidy-Hanley, D., Freed, J.H., Clark, T.G., Structure-function studies link class II viral fusogens and the ancestral gamete fusion protein HAP2. Curr. Biol., 27, 2017, 10.1016/j.cub.2017.01.049 Published online February 23, 2017.
    • (2017) Curr. Biol. , vol.27
    • Pinello, J.F.1    Lai, A.L.2    Millet, J.K.3    Cassidy-Hanley, D.4    Freed, J.H.5    Clark, T.G.6
  • 58
    • 33745974537 scopus 로고    scopus 로고
    • Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G
    • Roche, S., Bressanelli, S., Rey, F.A., Gaudin, Y., Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G. Science 313 (2006), 187–191.
    • (2006) Science , vol.313 , pp. 187-191
    • Roche, S.1    Bressanelli, S.2    Rey, F.A.3    Gaudin, Y.4
  • 59
    • 0017252476 scopus 로고
    • Gametogenesis and fertilization in Plasmodium yoelii nigeriensis: a transmission electron microscope study
    • Sinden, R.E., Canning, E.U., Spain, B., Gametogenesis and fertilization in Plasmodium yoelii nigeriensis: a transmission electron microscope study. Proc. R. Soc. Lond. B Biol. Sci. 193 (1976), 55–76.
    • (1976) Proc. R. Soc. Lond. B Biol. Sci. , vol.193 , pp. 55-76
    • Sinden, R.E.1    Canning, E.U.2    Spain, B.3
  • 60
    • 69449086120 scopus 로고    scopus 로고
    • Flagellar adhesion, flagellar-generated signaling, and gamete fusion during mating
    • E.H. Harris D.B. Stern G.B. Witman Elsevier
    • Snell, W.J., Goodenough, U.W., Flagellar adhesion, flagellar-generated signaling, and gamete fusion during mating. Harris, E.H., Stern, D.B., Witman, G.B., (eds.) The Chlamydomonas Sourcebook, 2009, Elsevier, 369–394.
    • (2009) The Chlamydomonas Sourcebook , pp. 369-394
    • Snell, W.J.1    Goodenough, U.W.2
  • 61
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • W244–248
    • Söding, J., Biegert, A., Lupas, A.N., The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res., 33, 2005 W244–248.
    • (2005) Nucleic Acids Res. , vol.33
    • Söding, J.1    Biegert, A.2    Lupas, A.N.3
  • 63
    • 70449578273 scopus 로고    scopus 로고
    • Evolutionary history of the HAP2/GCS1 gene and sexual reproduction in metazoans
    • Steele, R.E., Dana, C.E., Evolutionary history of the HAP2/GCS1 gene and sexual reproduction in metazoans. PLoS ONE, 4, 2009, e7680.
    • (2009) PLoS ONE , vol.4 , pp. e7680
    • Steele, R.E.1    Dana, C.E.2
  • 64
    • 0036198006 scopus 로고    scopus 로고
    • Membrane interactions of the tick-borne encephalitis virus fusion protein E at low pH
    • Stiasny, K., Allison, S.L., Schalich, J., Heinz, F.X., Membrane interactions of the tick-borne encephalitis virus fusion protein E at low pH. J. Virol. 76 (2002), 3784–3790.
    • (2002) J. Virol. , vol.76 , pp. 3784-3790
    • Stiasny, K.1    Allison, S.L.2    Schalich, J.3    Heinz, F.X.4
  • 66
    • 33846094853 scopus 로고    scopus 로고
    • Arabidopsis HAP2 (GCS1) is a sperm-specific gene required for pollen tube guidance and fertilization
    • von Besser, K., Frank, A.C., Johnson, M.A., Preuss, D., Arabidopsis HAP2 (GCS1) is a sperm-specific gene required for pollen tube guidance and fertilization. Development 133 (2006), 4761–4769.
    • (2006) Development , vol.133 , pp. 4761-4769
    • von Besser, K.1    Frank, A.C.2    Johnson, M.A.3    Preuss, D.4
  • 69
  • 70
    • 77249172226 scopus 로고    scopus 로고
    • Is HAP2-GCS1 an ancestral gamete fusogen?
    • Wong, J.L., Johnson, M.A., Is HAP2-GCS1 an ancestral gamete fusogen?. Trends Cell Biol. 20 (2010), 134–141.
    • (2010) Trends Cell Biol. , vol.20 , pp. 134-141
    • Wong, J.L.1    Johnson, M.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.