Antigenic characterization of bovine ephemeral fever rhabdovirus G and $ G_{NS} $ glycoproteins expressed from recombinant baculoviruses
Abstract Recombinant baculoviruses expressing the BEFV envelope glycoprotein G and non-structural glycoprotein $ G_{NS} $ were constructed. The G protein expressed in insect cells was located on the cell surface and induced spontaneous cell fusion at mildly acidic pH. The expressed G protein reacted...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Johal, Jasjit [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2008 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer-Verlag 2008 |
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| Übergeordnetes Werk: |
Enthalten in: Archives of virology - Wien : Springer, 1939, 153(2008), 9 vom: 15. Juli, Seite 1657-1665 |
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| Übergeordnetes Werk: |
volume:153 ; year:2008 ; number:9 ; day:15 ; month:07 ; pages:1657-1665 |
| Links: |
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| DOI / URN: |
10.1007/s00705-008-0164-0 |
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| Katalog-ID: |
SPR007384602 |
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| 024 | 7 | |a 10.1007/s00705-008-0164-0 |2 doi | |
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| 035 | |a (SPR)s00705-008-0164-0-e | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 100 | 1 | |a Johal, Jasjit |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Antigenic characterization of bovine ephemeral fever rhabdovirus G and $ G_{NS} $ glycoproteins expressed from recombinant baculoviruses |
| 264 | 1 | |c 2008 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a Computermedien |b c |2 rdamedia | ||
| 338 | |a Online-Ressource |b cr |2 rdacarrier | ||
| 500 | |a © Springer-Verlag 2008 | ||
| 520 | |a Abstract Recombinant baculoviruses expressing the BEFV envelope glycoprotein G and non-structural glycoprotein $ G_{NS} $ were constructed. The G protein expressed in insect cells was located on the cell surface and induced spontaneous cell fusion at mildly acidic pH. The expressed G protein reacted with MAbs to continuous and conformational neutralization sites (G1, G2, G3b and G4), but not to conformational site G3a. The expressed $ G_{NS} $ protein was also located on the cell surface but did not exhibit fusogenic activity. The $ G_{NS} $ protein reacted with polyclonal antiserum produced from vaccinia-virus-expressed recombinant $ G_{NS} $ but did not react with G protein antibodies. A $ His_{6} $-tagged, soluble form of the G protein was expressed and purified by $ Ni^{2+} $–NTA chromatography. The purified G protein reacted with BEFV-neutralizing MAbs to all continuous and conformational antigenic sites. The highly protective characteristics of the native BEFV G protein suggest that the secreted, baculovirus-expressed product may be a useful vaccine antigen. | ||
| 650 | 4 | |a Insect Cell |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Rabies Virus |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Antigenic Site |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Fusion Activity |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Infectious Hematopoietic Necrosis Virus |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Gresty, Karryn |4 aut | |
| 700 | 1 | |a Kongsuwan, Kritaya |4 aut | |
| 700 | 1 | |a Walker, Peter J. |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Archives of virology |d Wien : Springer, 1939 |g 153(2008), 9 vom: 15. Juli, Seite 1657-1665 |w (DE-627)253390168 |w (DE-600)1458460-8 |x 1432-8798 |7 nnns |
| 773 | 1 | 8 | |g volume:153 |g year:2008 |g number:9 |g day:15 |g month:07 |g pages:1657-1665 |
| 856 | 4 | 0 | |u https://dx.doi.org/10.1007/s00705-008-0164-0 |z lizenzpflichtig |3 Volltext |
| 912 | |a GBV_USEFLAG_A | ||
| 912 | |a SYSFLAG_A | ||
| 912 | |a GBV_SPRINGER | ||
| 912 | |a GBV_ILN_11 | ||
| 912 | |a GBV_ILN_20 | ||
| 912 | |a GBV_ILN_22 | ||
| 912 | |a GBV_ILN_23 | ||
| 912 | |a GBV_ILN_24 | ||
| 912 | |a GBV_ILN_31 | ||
| 912 | |a GBV_ILN_32 | ||
| 912 | |a GBV_ILN_39 | ||
| 912 | |a GBV_ILN_40 | ||
| 912 | |a GBV_ILN_60 | ||
| 912 | |a GBV_ILN_62 | ||
| 912 | |a GBV_ILN_63 | ||
| 912 | |a GBV_ILN_69 | ||
| 912 | |a GBV_ILN_70 | ||
| 912 | |a GBV_ILN_73 | ||
| 912 | |a GBV_ILN_74 | ||
| 912 | |a GBV_ILN_90 | ||
| 912 | |a GBV_ILN_95 | ||
| 912 | |a GBV_ILN_100 | ||
| 912 | |a GBV_ILN_101 | ||
| 912 | |a GBV_ILN_105 | ||
| 912 | |a GBV_ILN_110 | ||
| 912 | |a GBV_ILN_120 | ||
| 912 | |a GBV_ILN_138 | ||
| 912 | |a GBV_ILN_150 | ||
| 912 | |a GBV_ILN_151 | ||
| 912 | |a GBV_ILN_152 | ||
| 912 | |a GBV_ILN_161 | ||
| 912 | |a GBV_ILN_170 | ||
| 912 | |a GBV_ILN_171 | ||
| 912 | |a GBV_ILN_187 | ||
| 912 | |a GBV_ILN_213 | ||
| 912 | |a GBV_ILN_224 | ||
| 912 | |a GBV_ILN_230 | ||
| 912 | |a GBV_ILN_250 | ||
| 912 | |a GBV_ILN_252 | ||
| 912 | |a GBV_ILN_267 | ||
| 912 | |a GBV_ILN_281 | ||
| 912 | |a GBV_ILN_285 | ||
| 912 | |a GBV_ILN_293 | ||
| 912 | |a GBV_ILN_370 | ||
| 912 | |a GBV_ILN_602 | ||
| 912 | |a GBV_ILN_636 | ||
| 912 | |a GBV_ILN_702 | ||
| 912 | |a GBV_ILN_711 | ||
| 912 | |a GBV_ILN_2001 | ||
| 912 | |a GBV_ILN_2003 | ||
| 912 | |a GBV_ILN_2004 | ||
| 912 | |a GBV_ILN_2005 | ||
| 912 | |a GBV_ILN_2006 | ||
| 912 | |a GBV_ILN_2007 | ||
| 912 | |a GBV_ILN_2008 | ||
| 912 | |a GBV_ILN_2009 | ||
| 912 | |a GBV_ILN_2010 | ||
| 912 | |a GBV_ILN_2011 | ||
| 912 | |a GBV_ILN_2014 | ||
| 912 | |a GBV_ILN_2015 | ||
| 912 | |a GBV_ILN_2020 | ||
| 912 | |a GBV_ILN_2021 | ||
| 912 | |a GBV_ILN_2025 | ||
| 912 | |a GBV_ILN_2026 | ||
| 912 | |a GBV_ILN_2027 | ||
| 912 | |a GBV_ILN_2031 | ||
| 912 | |a GBV_ILN_2034 | ||
| 912 | |a GBV_ILN_2037 | ||
| 912 | |a GBV_ILN_2038 | ||
| 912 | |a GBV_ILN_2039 | ||
| 912 | |a GBV_ILN_2044 | ||
| 912 | |a GBV_ILN_2048 | ||
| 912 | |a GBV_ILN_2049 | ||
| 912 | |a GBV_ILN_2050 | ||
| 912 | |a GBV_ILN_2055 | ||
| 912 | |a GBV_ILN_2057 | ||
| 912 | |a GBV_ILN_2059 | ||
| 912 | |a GBV_ILN_2061 | ||
| 912 | |a GBV_ILN_2064 | ||
| 912 | |a GBV_ILN_2065 | ||
| 912 | |a GBV_ILN_2068 | ||
| 912 | |a GBV_ILN_2070 | ||
| 912 | |a GBV_ILN_2086 | ||
| 912 | |a GBV_ILN_2088 | ||
| 912 | |a GBV_ILN_2093 | ||
| 912 | |a GBV_ILN_2106 | ||
| 912 | |a GBV_ILN_2107 | ||
| 912 | |a GBV_ILN_2108 | ||
| 912 | |a GBV_ILN_2110 | ||
| 912 | |a GBV_ILN_2111 | ||
| 912 | |a GBV_ILN_2112 | ||
| 912 | |a GBV_ILN_2113 | ||
| 912 | |a GBV_ILN_2116 | ||
| 912 | |a GBV_ILN_2118 | ||
| 912 | |a GBV_ILN_2119 | ||
| 912 | |a GBV_ILN_2122 | ||
| 912 | |a GBV_ILN_2129 | ||
| 912 | |a GBV_ILN_2143 | ||
| 912 | |a GBV_ILN_2144 | ||
| 912 | |a GBV_ILN_2147 | ||
| 912 | |a GBV_ILN_2148 | ||
| 912 | |a GBV_ILN_2152 | ||
| 912 | |a GBV_ILN_2153 | ||
| 912 | |a GBV_ILN_2188 | ||
| 912 | |a GBV_ILN_2190 | ||
| 912 | |a GBV_ILN_2232 | ||
| 912 | |a GBV_ILN_2336 | ||
| 912 | |a GBV_ILN_2446 | ||
| 912 | |a GBV_ILN_2470 | ||
| 912 | |a GBV_ILN_2472 | ||
| 912 | |a GBV_ILN_2507 | ||
| 912 | |a GBV_ILN_2522 | ||
| 912 | |a GBV_ILN_2548 | ||
| 912 | |a GBV_ILN_4012 | ||
| 912 | |a GBV_ILN_4035 | ||
| 912 | |a GBV_ILN_4037 | ||
| 912 | |a GBV_ILN_4046 | ||
| 912 | |a GBV_ILN_4112 | ||
| 912 | |a GBV_ILN_4125 | ||
| 912 | |a GBV_ILN_4126 | ||
| 912 | |a GBV_ILN_4242 | ||
| 912 | |a GBV_ILN_4246 | ||
| 912 | |a GBV_ILN_4249 | ||
| 912 | |a GBV_ILN_4251 | ||
| 912 | |a GBV_ILN_4305 | ||
| 912 | |a GBV_ILN_4306 | ||
| 912 | |a GBV_ILN_4307 | ||
| 912 | |a GBV_ILN_4313 | ||
| 912 | |a GBV_ILN_4322 | ||
| 912 | |a GBV_ILN_4323 | ||
| 912 | |a GBV_ILN_4324 | ||
| 912 | |a GBV_ILN_4325 | ||
| 912 | |a GBV_ILN_4326 | ||
| 912 | |a GBV_ILN_4328 | ||
| 912 | |a GBV_ILN_4333 | ||
| 912 | |a GBV_ILN_4334 | ||
| 912 | |a GBV_ILN_4335 | ||
| 912 | |a GBV_ILN_4336 | ||
| 912 | |a GBV_ILN_4338 | ||
| 912 | |a GBV_ILN_4393 | ||
| 912 | |a GBV_ILN_4700 | ||
| 951 | |a AR | ||
| 952 | |d 153 |j 2008 |e 9 |b 15 |c 07 |h 1657-1665 | ||
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2008 |
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2008 |
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10.1007/s00705-008-0164-0 doi (DE-627)SPR007384602 (SPR)s00705-008-0164-0-e DE-627 ger DE-627 rakwb eng Johal, Jasjit verfasserin aut Antigenic characterization of bovine ephemeral fever rhabdovirus G and $ G_{NS} $ glycoproteins expressed from recombinant baculoviruses 2008 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2008 Abstract Recombinant baculoviruses expressing the BEFV envelope glycoprotein G and non-structural glycoprotein $ G_{NS} $ were constructed. The G protein expressed in insect cells was located on the cell surface and induced spontaneous cell fusion at mildly acidic pH. The expressed G protein reacted with MAbs to continuous and conformational neutralization sites (G1, G2, G3b and G4), but not to conformational site G3a. The expressed $ G_{NS} $ protein was also located on the cell surface but did not exhibit fusogenic activity. The $ G_{NS} $ protein reacted with polyclonal antiserum produced from vaccinia-virus-expressed recombinant $ G_{NS} $ but did not react with G protein antibodies. A $ His_{6} $-tagged, soluble form of the G protein was expressed and purified by $ Ni^{2+} $–NTA chromatography. The purified G protein reacted with BEFV-neutralizing MAbs to all continuous and conformational antigenic sites. The highly protective characteristics of the native BEFV G protein suggest that the secreted, baculovirus-expressed product may be a useful vaccine antigen. Insect Cell (dpeaa)DE-He213 Rabies Virus (dpeaa)DE-He213 Antigenic Site (dpeaa)DE-He213 Fusion Activity (dpeaa)DE-He213 Infectious Hematopoietic Necrosis Virus (dpeaa)DE-He213 Gresty, Karryn aut Kongsuwan, Kritaya aut Walker, Peter J. aut Enthalten in Archives of virology Wien : Springer, 1939 153(2008), 9 vom: 15. Juli, Seite 1657-1665 (DE-627)253390168 (DE-600)1458460-8 1432-8798 nnns volume:153 year:2008 number:9 day:15 month:07 pages:1657-1665 https://dx.doi.org/10.1007/s00705-008-0164-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_252 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_711 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 153 2008 9 15 07 1657-1665 |
| spelling |
10.1007/s00705-008-0164-0 doi (DE-627)SPR007384602 (SPR)s00705-008-0164-0-e DE-627 ger DE-627 rakwb eng Johal, Jasjit verfasserin aut Antigenic characterization of bovine ephemeral fever rhabdovirus G and $ G_{NS} $ glycoproteins expressed from recombinant baculoviruses 2008 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2008 Abstract Recombinant baculoviruses expressing the BEFV envelope glycoprotein G and non-structural glycoprotein $ G_{NS} $ were constructed. The G protein expressed in insect cells was located on the cell surface and induced spontaneous cell fusion at mildly acidic pH. The expressed G protein reacted with MAbs to continuous and conformational neutralization sites (G1, G2, G3b and G4), but not to conformational site G3a. The expressed $ G_{NS} $ protein was also located on the cell surface but did not exhibit fusogenic activity. The $ G_{NS} $ protein reacted with polyclonal antiserum produced from vaccinia-virus-expressed recombinant $ G_{NS} $ but did not react with G protein antibodies. A $ His_{6} $-tagged, soluble form of the G protein was expressed and purified by $ Ni^{2+} $–NTA chromatography. The purified G protein reacted with BEFV-neutralizing MAbs to all continuous and conformational antigenic sites. The highly protective characteristics of the native BEFV G protein suggest that the secreted, baculovirus-expressed product may be a useful vaccine antigen. Insect Cell (dpeaa)DE-He213 Rabies Virus (dpeaa)DE-He213 Antigenic Site (dpeaa)DE-He213 Fusion Activity (dpeaa)DE-He213 Infectious Hematopoietic Necrosis Virus (dpeaa)DE-He213 Gresty, Karryn aut Kongsuwan, Kritaya aut Walker, Peter J. aut Enthalten in Archives of virology Wien : Springer, 1939 153(2008), 9 vom: 15. Juli, Seite 1657-1665 (DE-627)253390168 (DE-600)1458460-8 1432-8798 nnns volume:153 year:2008 number:9 day:15 month:07 pages:1657-1665 https://dx.doi.org/10.1007/s00705-008-0164-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_252 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_711 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 153 2008 9 15 07 1657-1665 |
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10.1007/s00705-008-0164-0 doi (DE-627)SPR007384602 (SPR)s00705-008-0164-0-e DE-627 ger DE-627 rakwb eng Johal, Jasjit verfasserin aut Antigenic characterization of bovine ephemeral fever rhabdovirus G and $ G_{NS} $ glycoproteins expressed from recombinant baculoviruses 2008 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2008 Abstract Recombinant baculoviruses expressing the BEFV envelope glycoprotein G and non-structural glycoprotein $ G_{NS} $ were constructed. The G protein expressed in insect cells was located on the cell surface and induced spontaneous cell fusion at mildly acidic pH. The expressed G protein reacted with MAbs to continuous and conformational neutralization sites (G1, G2, G3b and G4), but not to conformational site G3a. The expressed $ G_{NS} $ protein was also located on the cell surface but did not exhibit fusogenic activity. The $ G_{NS} $ protein reacted with polyclonal antiserum produced from vaccinia-virus-expressed recombinant $ G_{NS} $ but did not react with G protein antibodies. A $ His_{6} $-tagged, soluble form of the G protein was expressed and purified by $ Ni^{2+} $–NTA chromatography. The purified G protein reacted with BEFV-neutralizing MAbs to all continuous and conformational antigenic sites. The highly protective characteristics of the native BEFV G protein suggest that the secreted, baculovirus-expressed product may be a useful vaccine antigen. Insect Cell (dpeaa)DE-He213 Rabies Virus (dpeaa)DE-He213 Antigenic Site (dpeaa)DE-He213 Fusion Activity (dpeaa)DE-He213 Infectious Hematopoietic Necrosis Virus (dpeaa)DE-He213 Gresty, Karryn aut Kongsuwan, Kritaya aut Walker, Peter J. aut Enthalten in Archives of virology Wien : Springer, 1939 153(2008), 9 vom: 15. Juli, Seite 1657-1665 (DE-627)253390168 (DE-600)1458460-8 1432-8798 nnns volume:153 year:2008 number:9 day:15 month:07 pages:1657-1665 https://dx.doi.org/10.1007/s00705-008-0164-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_252 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_711 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 153 2008 9 15 07 1657-1665 |
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10.1007/s00705-008-0164-0 doi (DE-627)SPR007384602 (SPR)s00705-008-0164-0-e DE-627 ger DE-627 rakwb eng Johal, Jasjit verfasserin aut Antigenic characterization of bovine ephemeral fever rhabdovirus G and $ G_{NS} $ glycoproteins expressed from recombinant baculoviruses 2008 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2008 Abstract Recombinant baculoviruses expressing the BEFV envelope glycoprotein G and non-structural glycoprotein $ G_{NS} $ were constructed. The G protein expressed in insect cells was located on the cell surface and induced spontaneous cell fusion at mildly acidic pH. The expressed G protein reacted with MAbs to continuous and conformational neutralization sites (G1, G2, G3b and G4), but not to conformational site G3a. The expressed $ G_{NS} $ protein was also located on the cell surface but did not exhibit fusogenic activity. The $ G_{NS} $ protein reacted with polyclonal antiserum produced from vaccinia-virus-expressed recombinant $ G_{NS} $ but did not react with G protein antibodies. A $ His_{6} $-tagged, soluble form of the G protein was expressed and purified by $ Ni^{2+} $–NTA chromatography. The purified G protein reacted with BEFV-neutralizing MAbs to all continuous and conformational antigenic sites. The highly protective characteristics of the native BEFV G protein suggest that the secreted, baculovirus-expressed product may be a useful vaccine antigen. Insect Cell (dpeaa)DE-He213 Rabies Virus (dpeaa)DE-He213 Antigenic Site (dpeaa)DE-He213 Fusion Activity (dpeaa)DE-He213 Infectious Hematopoietic Necrosis Virus (dpeaa)DE-He213 Gresty, Karryn aut Kongsuwan, Kritaya aut Walker, Peter J. aut Enthalten in Archives of virology Wien : Springer, 1939 153(2008), 9 vom: 15. Juli, Seite 1657-1665 (DE-627)253390168 (DE-600)1458460-8 1432-8798 nnns volume:153 year:2008 number:9 day:15 month:07 pages:1657-1665 https://dx.doi.org/10.1007/s00705-008-0164-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_252 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_711 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 153 2008 9 15 07 1657-1665 |
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10.1007/s00705-008-0164-0 doi (DE-627)SPR007384602 (SPR)s00705-008-0164-0-e DE-627 ger DE-627 rakwb eng Johal, Jasjit verfasserin aut Antigenic characterization of bovine ephemeral fever rhabdovirus G and $ G_{NS} $ glycoproteins expressed from recombinant baculoviruses 2008 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2008 Abstract Recombinant baculoviruses expressing the BEFV envelope glycoprotein G and non-structural glycoprotein $ G_{NS} $ were constructed. The G protein expressed in insect cells was located on the cell surface and induced spontaneous cell fusion at mildly acidic pH. The expressed G protein reacted with MAbs to continuous and conformational neutralization sites (G1, G2, G3b and G4), but not to conformational site G3a. The expressed $ G_{NS} $ protein was also located on the cell surface but did not exhibit fusogenic activity. The $ G_{NS} $ protein reacted with polyclonal antiserum produced from vaccinia-virus-expressed recombinant $ G_{NS} $ but did not react with G protein antibodies. A $ His_{6} $-tagged, soluble form of the G protein was expressed and purified by $ Ni^{2+} $–NTA chromatography. The purified G protein reacted with BEFV-neutralizing MAbs to all continuous and conformational antigenic sites. The highly protective characteristics of the native BEFV G protein suggest that the secreted, baculovirus-expressed product may be a useful vaccine antigen. Insect Cell (dpeaa)DE-He213 Rabies Virus (dpeaa)DE-He213 Antigenic Site (dpeaa)DE-He213 Fusion Activity (dpeaa)DE-He213 Infectious Hematopoietic Necrosis Virus (dpeaa)DE-He213 Gresty, Karryn aut Kongsuwan, Kritaya aut Walker, Peter J. aut Enthalten in Archives of virology Wien : Springer, 1939 153(2008), 9 vom: 15. Juli, Seite 1657-1665 (DE-627)253390168 (DE-600)1458460-8 1432-8798 nnns volume:153 year:2008 number:9 day:15 month:07 pages:1657-1665 https://dx.doi.org/10.1007/s00705-008-0164-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_252 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_711 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 153 2008 9 15 07 1657-1665 |
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Enthalten in Archives of virology 153(2008), 9 vom: 15. Juli, Seite 1657-1665 volume:153 year:2008 number:9 day:15 month:07 pages:1657-1665 |
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Insect Cell Rabies Virus Antigenic Site Fusion Activity Infectious Hematopoietic Necrosis Virus |
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Johal, Jasjit @@aut@@ Gresty, Karryn @@aut@@ Kongsuwan, Kritaya @@aut@@ Walker, Peter J. @@aut@@ |
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The G protein expressed in insect cells was located on the cell surface and induced spontaneous cell fusion at mildly acidic pH. The expressed G protein reacted with MAbs to continuous and conformational neutralization sites (G1, G2, G3b and G4), but not to conformational site G3a. The expressed $ G_{NS} $ protein was also located on the cell surface but did not exhibit fusogenic activity. The $ G_{NS} $ protein reacted with polyclonal antiserum produced from vaccinia-virus-expressed recombinant $ G_{NS} $ but did not react with G protein antibodies. A $ His_{6} $-tagged, soluble form of the G protein was expressed and purified by $ Ni^{2+} $–NTA chromatography. The purified G protein reacted with BEFV-neutralizing MAbs to all continuous and conformational antigenic sites. 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Johal, Jasjit |
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Johal, Jasjit misc Insect Cell misc Rabies Virus misc Antigenic Site misc Fusion Activity misc Infectious Hematopoietic Necrosis Virus Antigenic characterization of bovine ephemeral fever rhabdovirus G and $ G_{NS} $ glycoproteins expressed from recombinant baculoviruses |
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Antigenic characterization of bovine ephemeral fever rhabdovirus G and $ G_{NS} $ glycoproteins expressed from recombinant baculoviruses Insect Cell (dpeaa)DE-He213 Rabies Virus (dpeaa)DE-He213 Antigenic Site (dpeaa)DE-He213 Fusion Activity (dpeaa)DE-He213 Infectious Hematopoietic Necrosis Virus (dpeaa)DE-He213 |
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misc Insect Cell misc Rabies Virus misc Antigenic Site misc Fusion Activity misc Infectious Hematopoietic Necrosis Virus |
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Antigenic characterization of bovine ephemeral fever rhabdovirus G and $ G_{NS} $ glycoproteins expressed from recombinant baculoviruses |
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Antigenic characterization of bovine ephemeral fever rhabdovirus G and $ G_{NS} $ glycoproteins expressed from recombinant baculoviruses |
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Johal, Jasjit Gresty, Karryn Kongsuwan, Kritaya Walker, Peter J. |
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antigenic characterization of bovine ephemeral fever rhabdovirus g and $ g_{ns} $ glycoproteins expressed from recombinant baculoviruses |
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Antigenic characterization of bovine ephemeral fever rhabdovirus G and $ G_{NS} $ glycoproteins expressed from recombinant baculoviruses |
| abstract |
Abstract Recombinant baculoviruses expressing the BEFV envelope glycoprotein G and non-structural glycoprotein $ G_{NS} $ were constructed. The G protein expressed in insect cells was located on the cell surface and induced spontaneous cell fusion at mildly acidic pH. The expressed G protein reacted with MAbs to continuous and conformational neutralization sites (G1, G2, G3b and G4), but not to conformational site G3a. The expressed $ G_{NS} $ protein was also located on the cell surface but did not exhibit fusogenic activity. The $ G_{NS} $ protein reacted with polyclonal antiserum produced from vaccinia-virus-expressed recombinant $ G_{NS} $ but did not react with G protein antibodies. A $ His_{6} $-tagged, soluble form of the G protein was expressed and purified by $ Ni^{2+} $–NTA chromatography. The purified G protein reacted with BEFV-neutralizing MAbs to all continuous and conformational antigenic sites. The highly protective characteristics of the native BEFV G protein suggest that the secreted, baculovirus-expressed product may be a useful vaccine antigen. © Springer-Verlag 2008 |
| abstractGer |
Abstract Recombinant baculoviruses expressing the BEFV envelope glycoprotein G and non-structural glycoprotein $ G_{NS} $ were constructed. The G protein expressed in insect cells was located on the cell surface and induced spontaneous cell fusion at mildly acidic pH. The expressed G protein reacted with MAbs to continuous and conformational neutralization sites (G1, G2, G3b and G4), but not to conformational site G3a. The expressed $ G_{NS} $ protein was also located on the cell surface but did not exhibit fusogenic activity. The $ G_{NS} $ protein reacted with polyclonal antiserum produced from vaccinia-virus-expressed recombinant $ G_{NS} $ but did not react with G protein antibodies. A $ His_{6} $-tagged, soluble form of the G protein was expressed and purified by $ Ni^{2+} $–NTA chromatography. The purified G protein reacted with BEFV-neutralizing MAbs to all continuous and conformational antigenic sites. The highly protective characteristics of the native BEFV G protein suggest that the secreted, baculovirus-expressed product may be a useful vaccine antigen. © Springer-Verlag 2008 |
| abstract_unstemmed |
Abstract Recombinant baculoviruses expressing the BEFV envelope glycoprotein G and non-structural glycoprotein $ G_{NS} $ were constructed. The G protein expressed in insect cells was located on the cell surface and induced spontaneous cell fusion at mildly acidic pH. The expressed G protein reacted with MAbs to continuous and conformational neutralization sites (G1, G2, G3b and G4), but not to conformational site G3a. The expressed $ G_{NS} $ protein was also located on the cell surface but did not exhibit fusogenic activity. The $ G_{NS} $ protein reacted with polyclonal antiserum produced from vaccinia-virus-expressed recombinant $ G_{NS} $ but did not react with G protein antibodies. A $ His_{6} $-tagged, soluble form of the G protein was expressed and purified by $ Ni^{2+} $–NTA chromatography. The purified G protein reacted with BEFV-neutralizing MAbs to all continuous and conformational antigenic sites. The highly protective characteristics of the native BEFV G protein suggest that the secreted, baculovirus-expressed product may be a useful vaccine antigen. © Springer-Verlag 2008 |
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| container_issue |
9 |
| title_short |
Antigenic characterization of bovine ephemeral fever rhabdovirus G and $ G_{NS} $ glycoproteins expressed from recombinant baculoviruses |
| url |
https://dx.doi.org/10.1007/s00705-008-0164-0 |
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Gresty, Karryn Kongsuwan, Kritaya Walker, Peter J. |
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10.1007/s00705-008-0164-0 |
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2024-07-04T03:03:36.291Z |
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| score |
7.4020243 |