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Volumn 150, Issue 1, 2010, Pages 202-206

Binding characterization of determinants in porcine aminopeptidase N, the cellular receptor for transmissible gastroenteritis virus

Author keywords

Binding; Coronavirus; PAPN; Receptor

Indexed keywords

AMINO PEPTIDASE; ANTIBODY-BINDING; BINDING; BINDING ABILITIES; BINDING ACTIVITIES; CELLULAR RECEPTORS; CORONAVIRUSES; ENZYME LINKED IMMUNOSORBENT ASSAY; IMMUNOBLOTTING; INHIBITORY EFFECT; PAPN; PLAQUE ASSAY; PROKARYOTIC CELLS; RECEPTOR; RECEPTOR BINDING;

EID: 77957335245     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2010.07.019     Document Type: Article
Times cited : (23)

References (34)
  • 1
    • 0031060291 scopus 로고    scopus 로고
    • Interspecies aminopeptidase-N chimeras reveal species-specific receptor recognition by canine coronavirus, feline infectious peritonitis virus, and transmissible gastroenteritis virus
    • Benbacer L., Kut E., Besnardeau L., Laude H., Delmas B. Interspecies aminopeptidase-N chimeras reveal species-specific receptor recognition by canine coronavirus, feline infectious peritonitis virus, and transmissible gastroenteritis virus. J. Virol. 1997, 71:734-737.
    • (1997) J. Virol. , vol.71 , pp. 734-737
    • Benbacer, L.1    Kut, E.2    Besnardeau, L.3    Laude, H.4    Delmas, B.5
  • 2
    • 70350214491 scopus 로고    scopus 로고
    • Binding capability of the enediyne-associated apoprotein to human tumors and constitution of a ligand oligopeptide-integrated protein
    • Cai L., Chen H., Miao Q., Wu S., Shang Y., Zhen Y. Binding capability of the enediyne-associated apoprotein to human tumors and constitution of a ligand oligopeptide-integrated protein. J. Biotechnol. 2009, 144:142-150.
    • (2009) J. Biotechnol. , vol.144 , pp. 142-150
    • Cai, L.1    Chen, H.2    Miao, Q.3    Wu, S.4    Shang, Y.5    Zhen, Y.6
  • 4
    • 0028308336 scopus 로고
    • Determinants essential for the transmissible gastroenteritis virus-receptor interaction reside within a domain of aminopeptidase-N that is distinct from the enzymatic site
    • Delmas B., Gelfi J., Kut E., Sjostrom H., Noren O., Laude H. Determinants essential for the transmissible gastroenteritis virus-receptor interaction reside within a domain of aminopeptidase-N that is distinct from the enzymatic site. J. Virol. 1994, 68:5216-5224.
    • (1994) J. Virol. , vol.68 , pp. 5216-5224
    • Delmas, B.1    Gelfi, J.2    Kut, E.3    Sjostrom, H.4    Noren, O.5    Laude, H.6
  • 8
    • 33749508665 scopus 로고    scopus 로고
    • Discovery, cloning and heterologous expression of secreted potato proteins reveal erroneous pre-mRNA splicing in Aspergillus oryzae
    • Hamann T., Lange L. Discovery, cloning and heterologous expression of secreted potato proteins reveal erroneous pre-mRNA splicing in Aspergillus oryzae. J. Biotechnol. 2006, 126:265-276.
    • (2006) J. Biotechnol. , vol.126 , pp. 265-276
    • Hamann, T.1    Lange, L.2
  • 9
    • 0031834946 scopus 로고    scopus 로고
    • Characterization of determinants involved in the feline infectious peritonitis virus receptor function of feline aminopeptidase N
    • Hegyi A., Kolb A.F. Characterization of determinants involved in the feline infectious peritonitis virus receptor function of feline aminopeptidase N. J. Gen. Virol. 1998, 79:1387-1391.
    • (1998) J. Gen. Virol. , vol.79 , pp. 1387-1391
    • Hegyi, A.1    Kolb, A.F.2
  • 10
    • 37249033378 scopus 로고    scopus 로고
    • Efficiency of cell-free protein synthesis based on a crude cell extract from Escherichia coli, wheat germ, and rabbit reticulocytes
    • Hino M., Kataoka M., Kajimoto K., Yamamoto T., Kido J., Shinohara Y., Baba Y. Efficiency of cell-free protein synthesis based on a crude cell extract from Escherichia coli, wheat germ, and rabbit reticulocytes. J. Biotechnol. 2008, 133:183-189.
    • (2008) J. Biotechnol. , vol.133 , pp. 183-189
    • Hino, M.1    Kataoka, M.2    Kajimoto, K.3    Yamamoto, T.4    Kido, J.5    Shinohara, Y.6    Baba, Y.7
  • 11
    • 0027941838 scopus 로고
    • Families of zinc metalloproteases
    • Hooper N.M. Families of zinc metalloproteases. FEBS Lett. 1994, 354:1-6.
    • (1994) FEBS Lett. , vol.354 , pp. 1-6
    • Hooper, N.M.1
  • 12
    • 4644333528 scopus 로고    scopus 로고
    • Cloning and overexpression of the old yellow enzyme gene of Candida macedoniensis, and its application to the production of a chiral compound
    • Kataoka M., Kotaka A., Thiwthong R., Wada M., Nakamori S., Shimizu S. Cloning and overexpression of the old yellow enzyme gene of Candida macedoniensis, and its application to the production of a chiral compound. J. Biotechnol. 2004, 114:1-9.
    • (2004) J. Biotechnol. , vol.114 , pp. 1-9
    • Kataoka, M.1    Kotaka, A.2    Thiwthong, R.3    Wada, M.4    Nakamori, S.5    Shimizu, S.6
  • 13
    • 0030720509 scopus 로고    scopus 로고
    • Identification of residues critical for the human coronavirus 229E receptor function of human aminopeptidase N
    • Kolb A.F., Hegyi A., Siddell S.G. Identification of residues critical for the human coronavirus 229E receptor function of human aminopeptidase N. J. Gen. Virol. 1997, 78:2795-2802.
    • (1997) J. Gen. Virol. , vol.78 , pp. 2795-2802
    • Kolb, A.F.1    Hegyi, A.2    Siddell, S.G.3
  • 14
    • 0033957648 scopus 로고    scopus 로고
    • Characterization of the sialic acid binding activity of transmissible gastroenteritis coronavirus by analysis of haemagglutination-deficient mutants
    • Krempl C., Ballesteros M.L., Zimmer G., Enjuanes L., Klenk H.D., Herrler G. Characterization of the sialic acid binding activity of transmissible gastroenteritis coronavirus by analysis of haemagglutination-deficient mutants. J. Gen. Virol. 2000, 81:489-496.
    • (2000) J. Gen. Virol. , vol.81 , pp. 489-496
    • Krempl, C.1    Ballesteros, M.L.2    Zimmer, G.3    Enjuanes, L.4    Klenk, H.D.5    Herrler, G.6
  • 15
    • 0035163804 scopus 로고    scopus 로고
    • Sialic acid binding activity of transmissible gastroenteritis coronavirus affects sedimentation behavior of virions and solubilized glycoproteins
    • Krempl C., Herrler G. Sialic acid binding activity of transmissible gastroenteritis coronavirus affects sedimentation behavior of virions and solubilized glycoproteins. J. Virol. 2001, 75:844-849.
    • (2001) J. Virol. , vol.75 , pp. 844-849
    • Krempl, C.1    Herrler, G.2
  • 16
    • 0030893578 scopus 로고    scopus 로고
    • Point mutations in the S protein connect the sialic acid binding activity with the enteropathogenicity of transmissible gastroenteritis coronavirus
    • Krempl C., Schultze B., Laude H., Herrler G. Point mutations in the S protein connect the sialic acid binding activity with the enteropathogenicity of transmissible gastroenteritis coronavirus. J. Virol. 1997, 71:3285-3287.
    • (1997) J. Virol. , vol.71 , pp. 3285-3287
    • Krempl, C.1    Schultze, B.2    Laude, H.3    Herrler, G.4
  • 17
    • 0027428285 scopus 로고
    • Porcine respiratory coronavirus: molecular features and virus-host interactions
    • Laude H., Reeth K.V., Pensaert K.A. Porcine respiratory coronavirus: molecular features and virus-host interactions. Vet. Res. 1993, 24:125-150.
    • (1993) Vet. Res. , vol.24 , pp. 125-150
    • Laude, H.1    Reeth, K.V.2    Pensaert, K.A.3
  • 18
    • 77749233790 scopus 로고    scopus 로고
    • Cloning, prokaryotic expression, and biological analysis of recombinant chicken IFN-gamma
    • Li G., Zeng Y., Yin J., Lillehoj H.S., Ren X. Cloning, prokaryotic expression, and biological analysis of recombinant chicken IFN-gamma. Hybridoma (Larchmt) 2010, 29:1-6.
    • (2010) Hybridoma (Larchmt) , vol.29 , pp. 1-6
    • Li, G.1    Zeng, Y.2    Yin, J.3    Lillehoj, H.S.4    Ren, X.5
  • 19
    • 69249235476 scopus 로고    scopus 로고
    • Comparative analysis on the effect of glycyrrhizin diammonium and lithium chloride on infectious bronchitis virus infection in vitro
    • Li J., Yin J., Sui X., Li G., Ren X. Comparative analysis on the effect of glycyrrhizin diammonium and lithium chloride on infectious bronchitis virus infection in vitro. Avian Pathol. 2009, 38:215-221.
    • (2009) Avian Pathol. , vol.38 , pp. 215-221
    • Li, J.1    Yin, J.2    Sui, X.3    Li, G.4    Ren, X.5
  • 20
    • 64549131661 scopus 로고    scopus 로고
    • Expression and functional analysis of porcine aminopeptidase N produced in prokaryotic expression system
    • Liu B., Li G., Sui X., Yin J., Wang H., Ren X. Expression and functional analysis of porcine aminopeptidase N produced in prokaryotic expression system. J. Biotechnol. 2009, 141:91-96.
    • (2009) J. Biotechnol. , vol.141 , pp. 91-96
    • Liu, B.1    Li, G.2    Sui, X.3    Yin, J.4    Wang, H.5    Ren, X.6
  • 21
    • 77955901367 scopus 로고    scopus 로고
    • Production and characterization of a monoclonal antibody against spike protein of transmissible gastroenteritis virus
    • doi:10.1089/hyb.2010.0009
    • Meng F., Yin J., Li X., Yang W., Li G., Ren X. Production and characterization of a monoclonal antibody against spike protein of transmissible gastroenteritis virus. Hybridoma (Larchmt) 2010, 29(4). doi:10.1089/hyb.2010.0009.
    • (2010) Hybridoma (Larchmt) , vol.29 , Issue.4
    • Meng, F.1    Yin, J.2    Li, X.3    Yang, W.4    Li, G.5    Ren, X.6
  • 22
    • 0036904752 scopus 로고    scopus 로고
    • The role of feline aminopeptidase N as a receptor for infectious bronchitis virus
    • Miguel B., Pharr G.T., Wang C. The role of feline aminopeptidase N as a receptor for infectious bronchitis virus. Arch. Virol. 2002, 147:2047-2056.
    • (2002) Arch. Virol. , vol.147 , pp. 2047-2056
    • Miguel, B.1    Pharr, G.T.2    Wang, C.3
  • 24
    • 53749091904 scopus 로고    scopus 로고
    • Importance of cholesterol for infection of cells by transmissible gastroenteritis virus
    • Ren X., Wang M., Yin J., Ren Y., Li G. Importance of cholesterol for infection of cells by transmissible gastroenteritis virus. Virus Res. 2008, 137:220-224.
    • (2008) Virus Res. , vol.137 , pp. 220-224
    • Ren, X.1    Wang, M.2    Yin, J.3    Ren, Y.4    Li, G.5
  • 25
    • 77952580827 scopus 로고    scopus 로고
    • Heterologous expression of fused genes encoding the glycoprotein 5 from PRRSV: a way for producing functional protein in prokaryotic microorganism
    • Ren X., Wang M., Yin J., Ren Y., Li G. Heterologous expression of fused genes encoding the glycoprotein 5 from PRRSV: a way for producing functional protein in prokaryotic microorganism. J. Biotechnol. 2010, 147:130-135.
    • (2010) J. Biotechnol. , vol.147 , pp. 130-135
    • Ren, X.1    Wang, M.2    Yin, J.3    Ren, Y.4    Li, G.5
  • 26
    • 77951842863 scopus 로고    scopus 로고
    • Phages harboring specific peptides to N protein of PRRSV distinguish the virus from other viruses
    • Ren X., Wang M., Yin J., Ren Y., Li G. Phages harboring specific peptides to N protein of PRRSV distinguish the virus from other viruses. J. Clin. Microbiol. 2010, 48:1875-1881.
    • (2010) J. Clin. Microbiol. , vol.48 , pp. 1875-1881
    • Ren, X.1    Wang, M.2    Yin, J.3    Ren, Y.4    Li, G.5
  • 27
    • 0142060813 scopus 로고    scopus 로고
    • Binding of transmissible gastroenteritis coronavirus to brush border membrane sialoglycoproteins
    • Schwegmann-Wessels C., Zimmer G., Schröder B., Breves G., Herrler G. Binding of transmissible gastroenteritis coronavirus to brush border membrane sialoglycoproteins. J. Virol. 2003, 77:11846-11848.
    • (2003) J. Virol. , vol.77 , pp. 11846-11848
    • Schwegmann-Wessels, C.1    Zimmer, G.2    Schröder, B.3    Breves, G.4    Herrler, G.5
  • 28
    • 0024226792 scopus 로고
    • Coronaviruses: structure and genome expression
    • Spaan W., Cavanagh D., Horzinek C. Coronaviruses: structure and genome expression. J. Gen. Virol. 1988, 69:2939-2952.
    • (1988) J. Gen. Virol. , vol.69 , pp. 2939-2952
    • Spaan, W.1    Cavanagh, D.2    Horzinek, C.3
  • 29
    • 74849090646 scopus 로고    scopus 로고
    • Antiviral effect of diammonium glycyrrhizinate and lithium chloride on cell infection by pseudorabies herpesvirus
    • Sui X., Yin J., Ren X. Antiviral effect of diammonium glycyrrhizinate and lithium chloride on cell infection by pseudorabies herpesvirus. Antiviral Res. 2010, 85:346-353.
    • (2010) Antiviral Res. , vol.85 , pp. 346-353
    • Sui, X.1    Yin, J.2    Ren, X.3
  • 30
    • 0031754016 scopus 로고    scopus 로고
    • Feline aminopeptidase N is a receptor for all group I coronaviruses
    • Tresnan D.B., Holmes K.V. Feline aminopeptidase N is a receptor for all group I coronaviruses. Adv. Exp. Med. Biol. 1998, 440:69-75.
    • (1998) Adv. Exp. Med. Biol. , vol.440 , pp. 69-75
    • Tresnan, D.B.1    Holmes, K.V.2
  • 31
    • 0029861760 scopus 로고    scopus 로고
    • Feline aminopeptidase Nserves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup I
    • Tresnan D.B., Levis R., Holmes K.V. Feline aminopeptidase Nserves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup I. J. Virol. 1996, 70:8669-8674.
    • (1996) J. Virol. , vol.70 , pp. 8669-8674
    • Tresnan, D.B.1    Levis, R.2    Holmes, K.V.3
  • 32
    • 33846517378 scopus 로고    scopus 로고
    • Mutational analysis of aminopeptidase N, a receptor for several group 1 coronaviruses, identifies key determinants of viral host range
    • Tusell S.M., Schittone S.A., Holmes K.V. Mutational analysis of aminopeptidase N, a receptor for several group 1 coronaviruses, identifies key determinants of viral host range. J. Virol. 2007, 81:1261-1273.
    • (2007) J. Virol. , vol.81 , pp. 1261-1273
    • Tusell, S.M.1    Schittone, S.A.2    Holmes, K.V.3
  • 34
    • 34548110776 scopus 로고    scopus 로고
    • Select what you need: a comparative evaluation of the advantages and limitations of frequently used expression systems for foreign genes
    • Yin J., Li G., Ren X., Herrler G. Select what you need: a comparative evaluation of the advantages and limitations of frequently used expression systems for foreign genes. J. Biotechnol. 2007, 127:335-347.
    • (2007) J. Biotechnol. , vol.127 , pp. 335-347
    • Yin, J.1    Li, G.2    Ren, X.3    Herrler, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.