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Volumn 77, Issue 7, 2003, Pages 4435-4438

Human coronavirus 229E: Receptor binding domain and neutralization by soluble receptor at 37°C

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; AMINOPEPTIDASE; VIRUS GLYCOPROTEIN; VIRUS RECEPTOR;

EID: 0037377733     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.77.7.4435-4438.2003     Document Type: Article
Times cited : (70)

References (28)
  • 1
    • 0025019614 scopus 로고
    • Metalloprotease activity of CD13/ aminopeptidase N on the surface of human myeloid cells
    • Ashmun, R. A., and A. T. Look. 1990. Metalloprotease activity of CD13/ aminopeptidase N on the surface of human myeloid cells. Blood 75:462-469.
    • (1990) Blood , vol.75 , pp. 462-469
    • Ashmun, R.A.1    Look, A.T.2
  • 2
    • 0037321751 scopus 로고    scopus 로고
    • Identification of the receptor binding domain of HCoV-229E spike glycoprotein
    • Bonavia, A., B. D. Zelus, D. E. Wentworth, P. J. Talbot, and K. V. Holmes. 2003. Identification of the receptor binding domain of HCoV-229E spike glycoprotein. J. Virol. 77:2530-2538.
    • (2003) J. Virol. , vol.77 , pp. 2530-2538
    • Bonavia, A.1    Zelus, B.D.2    Wentworth, D.E.3    Talbot, P.J.4    Holmes, K.V.5
  • 3
    • 0002437897 scopus 로고
    • The coronavirus surface glycoprotein
    • S. G. Siddell (ed.), Plenum Press, New York, N.Y.
    • Cavanagh, D. 1995. The coronavirus surface glycoprotein, p. 73-113. In S. G. Siddell (ed.), The Coronaviridae. Plenum Press, New York, N.Y.
    • (1995) The Coronaviridae , pp. 73-113
    • Cavanagh, D.1
  • 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., J. Gelfi, E. Kut, H. Sjostrom, O. Noren, and H. Laude. 1994. 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. 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
  • 5
    • 0026729302 scopus 로고
    • Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV
    • Delmas, B., J. Gelfi, R. L'Haridon, L. K. Vogel, H. Sjostrom, O. Noren, and H. Laude. 1992. Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV. Nature 357:417-420.
    • (1992) Nature , vol.357 , pp. 417-420
    • Delmas, B.1    Gelfi, J.2    L'Haridon, R.3    Vogel, L.K.4    Sjostrom, H.5    Noren, O.6    Laude, H.7
  • 6
    • 0028258321 scopus 로고
    • Further characterization of aminopeptidase-N as a receptor for coronaviruses
    • Delmas, B. J., H. Gelfi, H. Sjostrom, O. Noren, and H. Laude. 1993. Further characterization of aminopeptidase-N as a receptor for coronaviruses. Adv. Exp. Med. Biol. 342:293-298.
    • (1993) Adv. Exp. Med. Biol. , vol.342 , pp. 293-298
    • Delmas, B.J.1    Gelfi, H.2    Sjostrom, H.3    Noren, O.4    Laude, H.5
  • 7
    • 0000216683 scopus 로고    scopus 로고
    • The common cold. Rhinoviruses and coronaviruses
    • R. Dolin and F. P. Wright (ed.), Marcel Dekker, New York, N.Y.
    • Denison, M. R. 1999. The common cold. Rhinoviruses and coronaviruses, p. 253-280. In R. Dolin and F. P. Wright (ed.), Viral infections of the respiratory tract. Marcel Dekker, New York, N.Y.
    • (1999) Viral Infections of The Respiratory Tract , pp. 253-280
    • Denison, M.R.1
  • 8
    • 0027971620 scopus 로고
    • Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein
    • Godet, M., J. Grosclaude, B. Delmas, and H. Laude. 1994. Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein. J. Virol. 68:8008-8016.
    • (1994) J. Virol. , vol.68 , pp. 8008-8016
    • Godet, M.1    Grosclaude, J.2    Delmas, B.3    Laude, H.4
  • 9
    • 0027422802 scopus 로고
    • Characterization of poliovirus conformational alteration mediated by soluble cell receptors
    • Gomez Yafal, A., G. Kaplan, V. R. Racaniello, and J. M. Hogle. 1993. Characterization of poliovirus conformational alteration mediated by soluble cell receptors. Virology 197:501-505.
    • (1993) Virology , vol.197 , pp. 501-505
    • Gomez Yafal, A.1    Kaplan, G.2    Racaniello, V.R.3    Hogle, J.M.4
  • 11
    • 0027284014 scopus 로고
    • A mouse aminopeptidase N is a marker for antigen-presenting cells and appears to be co-expressed with major histocompatibility complex class II molecules
    • Hansen, A. S., O. Noren, H. Sjostrom, and O. Werdelin. 1993. A mouse aminopeptidase N is a marker for antigen-presenting cells and appears to be co-expressed with major histocompatibility complex class II molecules. Eur. J. Immunol. 23:2358-2364.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 2358-2364
    • Hansen, A.S.1    Noren, O.2    Sjostrom, H.3    Werdelin, O.4
  • 12
    • 0034905041 scopus 로고    scopus 로고
    • The machinery of flavivirus fusion with host cell membranes
    • Heinz, F. X., and S. L. Allison. 2001. The machinery of flavivirus fusion with host cell membranes. Curr. Opin. Microbiol. 4:450-455.
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 450-455
    • Heinz, F.X.1    Allison, S.L.2
  • 13
    • 0002257116 scopus 로고    scopus 로고
    • Coronaviruses
    • D. M. Knipe and P. M. Howley (ed.), Williams & Wilkins, Philadelphia, Pa.
    • Holmes, K. V. 2001. Coronaviruses, p. 1187-1203. In D. M. Knipe and P. M. Howley (ed.), Fields virology. Williams & Wilkins, Philadelphia, Pa.
    • (2001) Fields Virology , pp. 1187-1203
    • Holmes, K.V.1
  • 14
    • 0025001939 scopus 로고
    • Neutralization of poliovirus by cell receptors expressed in insect cells
    • Kaplan, G., M. S. Freistadt, and V. R. Racaniello. 1990. Neutralization of poliovirus by cell receptors expressed in insect cells. J. Virol. 64:4697-4702.
    • (1990) J. Virol. , vol.64 , pp. 4697-4702
    • Kaplan, G.1    Freistadt, M.S.2    Racaniello, V.R.3
  • 16
    • 0037205452 scopus 로고    scopus 로고
    • Quaternary structure of coronavirus spikes in complex with carcinoembryonic antigen-related cell adhesion molecule cellular receptors
    • Lewicki, D. N., and T. M. Gallagher. 2002. Quaternary structure of coronavirus spikes in complex with carcinoembryonic antigen-related cell adhesion molecule cellular receptors. J. Biol. Chem. 277:19727-19734.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19727-19734
    • Lewicki, D.N.1    Gallagher, T.M.2
  • 17
    • 0001989767 scopus 로고    scopus 로고
    • Aminopeptidase N
    • A. J. B. C. M. Kenny (ed.), BIOS Scientific Publishers, Oxford, United Kingdom
    • Noren, O., H. Sjostrom, and J. Olsen. 1997. Aminopeptidase N, p. 175-191. In A. J. B. C. M. Kenny (ed.), Cell-surface peptidases in health and disease. BIOS Scientific Publishers, Oxford, United Kingdom.
    • (1997) Cell-Surface Peptidases in Health and Disease , pp. 175-191
    • Noren, O.1    Sjostrom, H.2    Olsen, J.3
  • 18
    • 0030785478 scopus 로고    scopus 로고
    • Interaction between echovirus 7 and its receptor, decay-accelerating factor (CD55): Evidence for a secondary cellular factor in A-particle formation
    • Powell, R. M., T. Ward, D. J. Evans, and J. W. Almond. 1997. Interaction between echovirus 7 and its receptor, decay-accelerating factor (CD55): evidence for a secondary cellular factor in A-particle formation. J. Virol. 71:9306-9312.
    • (1997) J. Virol. , vol.71 , pp. 9306-9312
    • Powell, R.M.1    Ward, T.2    Evans, D.J.3    Almond, J.W.4
  • 19
    • 0033082368 scopus 로고    scopus 로고
    • CD13 - Not just a marker in leukemia typing
    • Riemann, D., A. Kehlen, and J. Langner. 1999. CD13 - not just a marker in leukemia typing. Immunol. Today 20:83-88.
    • (1999) Immunol. Today , vol.20 , pp. 83-88
    • Riemann, D.1    Kehlen, A.2    Langner, J.3
  • 20
    • 0027135201 scopus 로고
    • Human and simian immunodeficiency viruses: Virus-receptor interactions
    • Signoret, N., P. Poignard, D. Blanc, and Q. J. Sattentau. 1993. Human and simian immunodeficiency viruses: virus-receptor interactions. Trc ads Microbiol. 1:328-333.
    • (1993) Trc Ads Microbiol. , vol.1 , pp. 328-333
    • Signoret, N.1    Poignard, P.2    Blanc, D.3    Sattentau, Q.J.4
  • 21
    • 0034473056 scopus 로고    scopus 로고
    • Structure and function of aminopeptidase N
    • J. A. S. Langner (ed.), Kluwer Academic/Plenum Publishers, New York, N.Y.
    • Sjostrom, H., O. Noren, and J. Olsen. 2000. Structure and function of aminopeptidase N, p. 25-34. In J. A. S. Langner (ed.), Cellular peptidases in immune functions and diseases 2. Kluwer Academic/Plenum Publishers, New York, N.Y.
    • (2000) Cellular Peptidases in Immune Functions and Diseases 2 , pp. 25-34
    • Sjostrom, H.1    Noren, O.2    Olsen, J.3
  • 22
    • 0034252567 scopus 로고    scopus 로고
    • Membrane fusion mechanisms: The influenza hemagglutinin paradigm and its implications for intracellular fusion
    • Stegmann, T. 2000. Membrane fusion mechanisms: the influenza hemagglutinin paradigm and its implications for intracellular fusion. Traffic 1:598-604.
    • (2000) Traffic , vol.1 , pp. 598-604
    • Stegmann, T.1
  • 23
    • 0029861760 scopus 로고    scopus 로고
    • Feline aminopeptidase N serves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup I
    • Tresnan, D. B., R. Levis, and K. V. Holmes. 1996. Feline aminopeptidase N serves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup I. J. Virol. 70:8669-8674.
    • (1996) J. Virol. , vol.70 , pp. 8669-8674
    • Tresnan, D.B.1    Levis, R.2    Holmes, K.V.3
  • 24
    • 0026612567 scopus 로고
    • The apical sorting signal on human aminopeptidase N is not located in the stalk but in the catalytic head group
    • Vogel, L. K., O. Noren, and H. Sjostrom. 1992. The apical sorting signal on human aminopeptidase N is not located in the stalk but in the catalytic head group. FEBS Lett. 308:14-17.
    • (1992) FEBS Lett. , vol.308 , pp. 14-17
    • Vogel, L.K.1    Noren, O.2    Sjostrom, H.3
  • 25
    • 0023082135 scopus 로고
    • The structure and function of the hemagglutinin membrane glycoprotein of influenza virus
    • Wiley, D. C., and J. J. Skehel. 1987. The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu. Rev. Biochem. 56:365-394.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 365-394
    • Wiley, D.C.1    Skehel, J.J.2
  • 27
    • 0037223630 scopus 로고    scopus 로고
    • Confirmational changes in the spike glycoprotein of murine coronavirus are induced at 37°C either by soluble murine CEACAMI receptor glycoproteins or by pH 8
    • Zelus, B. D., J. H. Schickli, D. M. Blau, S. R. Weiss, and K. V. Holmes. 2003. Confirmational changes in the spike glycoprotein of murine coronavirus are induced at 37°C either by soluble murine CEACAMI receptor glycoproteins or by pH 8. J. Virol. 77:830-840.
    • (2003) J. Virol. , vol.77 , pp. 830-840
    • Zelus, B.D.1    Schickli, J.H.2    Blau, D.M.3    Weiss, S.R.4    Holmes, K.V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.