Intracellular localization of Crimean-Congo Hemorrhagic Fever (CCHF) virus glycoproteins

Background Crimean-Congo Hemorrhagic Fever virus (CCHFV), a member of the genus Nairovirus, family Bunyaviridae, is a tick-borne pathogen causing severe disease in humans. To better understand the CCHFV life cycle and explore potential intervention strategies, we studied the biosynthesis and intrace...
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Autor*in:	Haferkamp, Sebastian [verfasserIn] Fernando, Lisa Schwarz, Tino F Feldmann, Heinz Flick, Ramon

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2005

Schlagwörter:	Green Fluorescence Protein Golgi Complex Rift Valley Fever Green Fluorescence Protein Fusion Protein Glycoprotein Precursor

Anmerkung:	© Haferkamp et al; licensee BioMed Central Ltd. 2005. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (

Übergeordnetes Werk:	Enthalten in: Virology journal - London : BioMed Central, 2004, 2(2005), 1 vom: 25. Apr.
Übergeordnetes Werk:	volume:2 ; year:2005 ; number:1 ; day:25 ; month:04

Links:	Volltext

DOI / URN:	10.1186/1743-422X-2-42

Katalog-ID:	SPR029231736

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520			\|a Background Crimean-Congo Hemorrhagic Fever virus (CCHFV), a member of the genus Nairovirus, family Bunyaviridae, is a tick-borne pathogen causing severe disease in humans. To better understand the CCHFV life cycle and explore potential intervention strategies, we studied the biosynthesis and intracellular targeting of the glycoproteins, which are encoded by the M genome segment. Results Following determination of the complete genome sequence of the CCHFV reference strain IbAr10200, we generated expression plasmids for the individual expression of the glycoproteins $ G_{N} $ and $ G_{C} $, using CMV- and chicken β-actin-driven promoters. The cellular localization of recombinantly expressed CCHFV glycoproteins was compared to authentic glycoproteins expressed during virus infection using indirect immunofluorescence assays, subcellular fractionation/western blot assays and confocal microscopy. To further elucidate potential intracellular targeting/retention signals of the two glycoproteins, GFP-fusion proteins containing different parts of the CCHFV glycoprotein were analyzed for their intracellular targeting. The N-terminal glycoprotein $ G_{N} $ localized to the Golgi complex, a process mediated by retention/targeting signal(s) in the cytoplasmic domain and ectodomain of this protein. In contrast, the C-terminal glycoprotein $ G_{C} $ remained in the endoplasmic reticulum but could be rescued into the Golgi complex by co-expression of $ G_{N} $. Conclusion The data are consistent with the intracellular targeting of most bunyavirus glycoproteins and support the general model for assembly and budding of bunyavirus particles in the Golgi compartment.
650		4	\|a Green Fluorescence Protein \|7 (dpeaa)DE-He213
650		4	\|a Golgi Complex \|7 (dpeaa)DE-He213
650		4	\|a Rift Valley Fever \|7 (dpeaa)DE-He213
650		4	\|a Green Fluorescence Protein Fusion Protein \|7 (dpeaa)DE-He213
650		4	\|a Glycoprotein Precursor \|7 (dpeaa)DE-He213
700	1		\|a Fernando, Lisa \|4 aut
700	1		\|a Schwarz, Tino F \|4 aut
700	1		\|a Feldmann, Heinz \|4 aut
700	1		\|a Flick, Ramon \|4 aut
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912			\|a GBV_USEFLAG_A
912			\|a SYSFLAG_A
912			\|a GBV_SPRINGER
912			\|a SSG-OLC-PHA
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_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_65
912			\|a GBV_ILN_69
912			\|a GBV_ILN_73
912			\|a GBV_ILN_74
912			\|a GBV_ILN_95
912			\|a GBV_ILN_105
912			\|a GBV_ILN_110
912			\|a GBV_ILN_151
912			\|a GBV_ILN_161
912			\|a GBV_ILN_170
912			\|a GBV_ILN_206
912			\|a GBV_ILN_213
912			\|a GBV_ILN_230
912			\|a GBV_ILN_285
912			\|a GBV_ILN_293
912			\|a GBV_ILN_602
912			\|a GBV_ILN_702
912			\|a GBV_ILN_2001
912			\|a GBV_ILN_2003
912			\|a GBV_ILN_2005
912			\|a GBV_ILN_2006
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_2031
912			\|a GBV_ILN_2038
912			\|a GBV_ILN_2044
912			\|a GBV_ILN_2048
912			\|a GBV_ILN_2050
912			\|a GBV_ILN_2055
912			\|a GBV_ILN_2056
912			\|a GBV_ILN_2057
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2113
912			\|a GBV_ILN_2190
912			\|a GBV_ILN_4012
912			\|a GBV_ILN_4037
912			\|a GBV_ILN_4112
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4126
912			\|a GBV_ILN_4249
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_4338
912			\|a GBV_ILN_4367
912			\|a GBV_ILN_4700
951			\|a AR
952			\|d 2 \|j 2005 \|e 1 \|b 25 \|c 04

Indexfelder

author_variant	s h sh l f lf t f s tf tfs h f hf r f rf
matchkey_str	article:1743422X:2005----::nrclualclztoocienoghmrhgceec
hierarchy_sort_str	2005
publishDate	2005
allfields	10.1186/1743-422X-2-42 doi (DE-627)SPR029231736 (SPR)1743-422X-2-42-e DE-627 ger DE-627 rakwb eng Haferkamp, Sebastian verfasserin aut Intracellular localization of Crimean-Congo Hemorrhagic Fever (CCHF) virus glycoproteins 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Haferkamp et al; licensee BioMed Central Ltd. 2005. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background Crimean-Congo Hemorrhagic Fever virus (CCHFV), a member of the genus Nairovirus, family Bunyaviridae, is a tick-borne pathogen causing severe disease in humans. To better understand the CCHFV life cycle and explore potential intervention strategies, we studied the biosynthesis and intracellular targeting of the glycoproteins, which are encoded by the M genome segment. Results Following determination of the complete genome sequence of the CCHFV reference strain IbAr10200, we generated expression plasmids for the individual expression of the glycoproteins $ G_{N} $ and $ G_{C} $, using CMV- and chicken β-actin-driven promoters. The cellular localization of recombinantly expressed CCHFV glycoproteins was compared to authentic glycoproteins expressed during virus infection using indirect immunofluorescence assays, subcellular fractionation/western blot assays and confocal microscopy. To further elucidate potential intracellular targeting/retention signals of the two glycoproteins, GFP-fusion proteins containing different parts of the CCHFV glycoprotein were analyzed for their intracellular targeting. The N-terminal glycoprotein $ G_{N} $ localized to the Golgi complex, a process mediated by retention/targeting signal(s) in the cytoplasmic domain and ectodomain of this protein. In contrast, the C-terminal glycoprotein $ G_{C} $ remained in the endoplasmic reticulum but could be rescued into the Golgi complex by co-expression of $ G_{N} $. Conclusion The data are consistent with the intracellular targeting of most bunyavirus glycoproteins and support the general model for assembly and budding of bunyavirus particles in the Golgi compartment. Green Fluorescence Protein (dpeaa)DE-He213 Golgi Complex (dpeaa)DE-He213 Rift Valley Fever (dpeaa)DE-He213 Green Fluorescence Protein Fusion Protein (dpeaa)DE-He213 Glycoprotein Precursor (dpeaa)DE-He213 Fernando, Lisa aut Schwarz, Tino F aut Feldmann, Heinz aut Flick, Ramon aut Enthalten in Virology journal London : BioMed Central, 2004 2(2005), 1 vom: 25. Apr. (DE-627)394165004 (DE-600)2160640-7 1743-422X nnns volume:2 year:2005 number:1 day:25 month:04 https://dx.doi.org/10.1186/1743-422X-2-42 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 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_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 2 2005 1 25 04
spelling	10.1186/1743-422X-2-42 doi (DE-627)SPR029231736 (SPR)1743-422X-2-42-e DE-627 ger DE-627 rakwb eng Haferkamp, Sebastian verfasserin aut Intracellular localization of Crimean-Congo Hemorrhagic Fever (CCHF) virus glycoproteins 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Haferkamp et al; licensee BioMed Central Ltd. 2005. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background Crimean-Congo Hemorrhagic Fever virus (CCHFV), a member of the genus Nairovirus, family Bunyaviridae, is a tick-borne pathogen causing severe disease in humans. To better understand the CCHFV life cycle and explore potential intervention strategies, we studied the biosynthesis and intracellular targeting of the glycoproteins, which are encoded by the M genome segment. Results Following determination of the complete genome sequence of the CCHFV reference strain IbAr10200, we generated expression plasmids for the individual expression of the glycoproteins $ G_{N} $ and $ G_{C} $, using CMV- and chicken β-actin-driven promoters. The cellular localization of recombinantly expressed CCHFV glycoproteins was compared to authentic glycoproteins expressed during virus infection using indirect immunofluorescence assays, subcellular fractionation/western blot assays and confocal microscopy. To further elucidate potential intracellular targeting/retention signals of the two glycoproteins, GFP-fusion proteins containing different parts of the CCHFV glycoprotein were analyzed for their intracellular targeting. The N-terminal glycoprotein $ G_{N} $ localized to the Golgi complex, a process mediated by retention/targeting signal(s) in the cytoplasmic domain and ectodomain of this protein. In contrast, the C-terminal glycoprotein $ G_{C} $ remained in the endoplasmic reticulum but could be rescued into the Golgi complex by co-expression of $ G_{N} $. Conclusion The data are consistent with the intracellular targeting of most bunyavirus glycoproteins and support the general model for assembly and budding of bunyavirus particles in the Golgi compartment. Green Fluorescence Protein (dpeaa)DE-He213 Golgi Complex (dpeaa)DE-He213 Rift Valley Fever (dpeaa)DE-He213 Green Fluorescence Protein Fusion Protein (dpeaa)DE-He213 Glycoprotein Precursor (dpeaa)DE-He213 Fernando, Lisa aut Schwarz, Tino F aut Feldmann, Heinz aut Flick, Ramon aut Enthalten in Virology journal London : BioMed Central, 2004 2(2005), 1 vom: 25. Apr. (DE-627)394165004 (DE-600)2160640-7 1743-422X nnns volume:2 year:2005 number:1 day:25 month:04 https://dx.doi.org/10.1186/1743-422X-2-42 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 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_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 2 2005 1 25 04
allfields_unstemmed	10.1186/1743-422X-2-42 doi (DE-627)SPR029231736 (SPR)1743-422X-2-42-e DE-627 ger DE-627 rakwb eng Haferkamp, Sebastian verfasserin aut Intracellular localization of Crimean-Congo Hemorrhagic Fever (CCHF) virus glycoproteins 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Haferkamp et al; licensee BioMed Central Ltd. 2005. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background Crimean-Congo Hemorrhagic Fever virus (CCHFV), a member of the genus Nairovirus, family Bunyaviridae, is a tick-borne pathogen causing severe disease in humans. To better understand the CCHFV life cycle and explore potential intervention strategies, we studied the biosynthesis and intracellular targeting of the glycoproteins, which are encoded by the M genome segment. Results Following determination of the complete genome sequence of the CCHFV reference strain IbAr10200, we generated expression plasmids for the individual expression of the glycoproteins $ G_{N} $ and $ G_{C} $, using CMV- and chicken β-actin-driven promoters. The cellular localization of recombinantly expressed CCHFV glycoproteins was compared to authentic glycoproteins expressed during virus infection using indirect immunofluorescence assays, subcellular fractionation/western blot assays and confocal microscopy. To further elucidate potential intracellular targeting/retention signals of the two glycoproteins, GFP-fusion proteins containing different parts of the CCHFV glycoprotein were analyzed for their intracellular targeting. The N-terminal glycoprotein $ G_{N} $ localized to the Golgi complex, a process mediated by retention/targeting signal(s) in the cytoplasmic domain and ectodomain of this protein. In contrast, the C-terminal glycoprotein $ G_{C} $ remained in the endoplasmic reticulum but could be rescued into the Golgi complex by co-expression of $ G_{N} $. Conclusion The data are consistent with the intracellular targeting of most bunyavirus glycoproteins and support the general model for assembly and budding of bunyavirus particles in the Golgi compartment. Green Fluorescence Protein (dpeaa)DE-He213 Golgi Complex (dpeaa)DE-He213 Rift Valley Fever (dpeaa)DE-He213 Green Fluorescence Protein Fusion Protein (dpeaa)DE-He213 Glycoprotein Precursor (dpeaa)DE-He213 Fernando, Lisa aut Schwarz, Tino F aut Feldmann, Heinz aut Flick, Ramon aut Enthalten in Virology journal London : BioMed Central, 2004 2(2005), 1 vom: 25. Apr. (DE-627)394165004 (DE-600)2160640-7 1743-422X nnns volume:2 year:2005 number:1 day:25 month:04 https://dx.doi.org/10.1186/1743-422X-2-42 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 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_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 2 2005 1 25 04
allfieldsGer	10.1186/1743-422X-2-42 doi (DE-627)SPR029231736 (SPR)1743-422X-2-42-e DE-627 ger DE-627 rakwb eng Haferkamp, Sebastian verfasserin aut Intracellular localization of Crimean-Congo Hemorrhagic Fever (CCHF) virus glycoproteins 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Haferkamp et al; licensee BioMed Central Ltd. 2005. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background Crimean-Congo Hemorrhagic Fever virus (CCHFV), a member of the genus Nairovirus, family Bunyaviridae, is a tick-borne pathogen causing severe disease in humans. To better understand the CCHFV life cycle and explore potential intervention strategies, we studied the biosynthesis and intracellular targeting of the glycoproteins, which are encoded by the M genome segment. Results Following determination of the complete genome sequence of the CCHFV reference strain IbAr10200, we generated expression plasmids for the individual expression of the glycoproteins $ G_{N} $ and $ G_{C} $, using CMV- and chicken β-actin-driven promoters. The cellular localization of recombinantly expressed CCHFV glycoproteins was compared to authentic glycoproteins expressed during virus infection using indirect immunofluorescence assays, subcellular fractionation/western blot assays and confocal microscopy. To further elucidate potential intracellular targeting/retention signals of the two glycoproteins, GFP-fusion proteins containing different parts of the CCHFV glycoprotein were analyzed for their intracellular targeting. The N-terminal glycoprotein $ G_{N} $ localized to the Golgi complex, a process mediated by retention/targeting signal(s) in the cytoplasmic domain and ectodomain of this protein. In contrast, the C-terminal glycoprotein $ G_{C} $ remained in the endoplasmic reticulum but could be rescued into the Golgi complex by co-expression of $ G_{N} $. Conclusion The data are consistent with the intracellular targeting of most bunyavirus glycoproteins and support the general model for assembly and budding of bunyavirus particles in the Golgi compartment. Green Fluorescence Protein (dpeaa)DE-He213 Golgi Complex (dpeaa)DE-He213 Rift Valley Fever (dpeaa)DE-He213 Green Fluorescence Protein Fusion Protein (dpeaa)DE-He213 Glycoprotein Precursor (dpeaa)DE-He213 Fernando, Lisa aut Schwarz, Tino F aut Feldmann, Heinz aut Flick, Ramon aut Enthalten in Virology journal London : BioMed Central, 2004 2(2005), 1 vom: 25. Apr. (DE-627)394165004 (DE-600)2160640-7 1743-422X nnns volume:2 year:2005 number:1 day:25 month:04 https://dx.doi.org/10.1186/1743-422X-2-42 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 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_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 2 2005 1 25 04
allfieldsSound	10.1186/1743-422X-2-42 doi (DE-627)SPR029231736 (SPR)1743-422X-2-42-e DE-627 ger DE-627 rakwb eng Haferkamp, Sebastian verfasserin aut Intracellular localization of Crimean-Congo Hemorrhagic Fever (CCHF) virus glycoproteins 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Haferkamp et al; licensee BioMed Central Ltd. 2005. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background Crimean-Congo Hemorrhagic Fever virus (CCHFV), a member of the genus Nairovirus, family Bunyaviridae, is a tick-borne pathogen causing severe disease in humans. To better understand the CCHFV life cycle and explore potential intervention strategies, we studied the biosynthesis and intracellular targeting of the glycoproteins, which are encoded by the M genome segment. Results Following determination of the complete genome sequence of the CCHFV reference strain IbAr10200, we generated expression plasmids for the individual expression of the glycoproteins $ G_{N} $ and $ G_{C} $, using CMV- and chicken β-actin-driven promoters. The cellular localization of recombinantly expressed CCHFV glycoproteins was compared to authentic glycoproteins expressed during virus infection using indirect immunofluorescence assays, subcellular fractionation/western blot assays and confocal microscopy. To further elucidate potential intracellular targeting/retention signals of the two glycoproteins, GFP-fusion proteins containing different parts of the CCHFV glycoprotein were analyzed for their intracellular targeting. The N-terminal glycoprotein $ G_{N} $ localized to the Golgi complex, a process mediated by retention/targeting signal(s) in the cytoplasmic domain and ectodomain of this protein. In contrast, the C-terminal glycoprotein $ G_{C} $ remained in the endoplasmic reticulum but could be rescued into the Golgi complex by co-expression of $ G_{N} $. Conclusion The data are consistent with the intracellular targeting of most bunyavirus glycoproteins and support the general model for assembly and budding of bunyavirus particles in the Golgi compartment. Green Fluorescence Protein (dpeaa)DE-He213 Golgi Complex (dpeaa)DE-He213 Rift Valley Fever (dpeaa)DE-He213 Green Fluorescence Protein Fusion Protein (dpeaa)DE-He213 Glycoprotein Precursor (dpeaa)DE-He213 Fernando, Lisa aut Schwarz, Tino F aut Feldmann, Heinz aut Flick, Ramon aut Enthalten in Virology journal London : BioMed Central, 2004 2(2005), 1 vom: 25. Apr. (DE-627)394165004 (DE-600)2160640-7 1743-422X nnns volume:2 year:2005 number:1 day:25 month:04 https://dx.doi.org/10.1186/1743-422X-2-42 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 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_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 2 2005 1 25 04
language	English
source	Enthalten in Virology journal 2(2005), 1 vom: 25. Apr. volume:2 year:2005 number:1 day:25 month:04
sourceStr	Enthalten in Virology journal 2(2005), 1 vom: 25. Apr. volume:2 year:2005 number:1 day:25 month:04
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Green Fluorescence Protein Golgi Complex Rift Valley Fever Green Fluorescence Protein Fusion Protein Glycoprotein Precursor
isfreeaccess_bool	false
container_title	Virology journal
authorswithroles_txt_mv	Haferkamp, Sebastian @@aut@@ Fernando, Lisa @@aut@@ Schwarz, Tino F @@aut@@ Feldmann, Heinz @@aut@@ Flick, Ramon @@aut@@
publishDateDaySort_date	2005-04-25T00:00:00Z
hierarchy_top_id	394165004
id	SPR029231736
language_de	englisch
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author	Haferkamp, Sebastian
spellingShingle	Haferkamp, Sebastian misc Green Fluorescence Protein misc Golgi Complex misc Rift Valley Fever misc Green Fluorescence Protein Fusion Protein misc Glycoprotein Precursor Intracellular localization of Crimean-Congo Hemorrhagic Fever (CCHF) virus glycoproteins
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topic_title	Intracellular localization of Crimean-Congo Hemorrhagic Fever (CCHF) virus glycoproteins Green Fluorescence Protein (dpeaa)DE-He213 Golgi Complex (dpeaa)DE-He213 Rift Valley Fever (dpeaa)DE-He213 Green Fluorescence Protein Fusion Protein (dpeaa)DE-He213 Glycoprotein Precursor (dpeaa)DE-He213
topic	misc Green Fluorescence Protein misc Golgi Complex misc Rift Valley Fever misc Green Fluorescence Protein Fusion Protein misc Glycoprotein Precursor
topic_unstemmed	misc Green Fluorescence Protein misc Golgi Complex misc Rift Valley Fever misc Green Fluorescence Protein Fusion Protein misc Glycoprotein Precursor
topic_browse	misc Green Fluorescence Protein misc Golgi Complex misc Rift Valley Fever misc Green Fluorescence Protein Fusion Protein misc Glycoprotein Precursor
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title	Intracellular localization of Crimean-Congo Hemorrhagic Fever (CCHF) virus glycoproteins
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title_full	Intracellular localization of Crimean-Congo Hemorrhagic Fever (CCHF) virus glycoproteins
author_sort	Haferkamp, Sebastian
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author_browse	Haferkamp, Sebastian Fernando, Lisa Schwarz, Tino F Feldmann, Heinz Flick, Ramon
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author-letter	Haferkamp, Sebastian
doi_str_mv	10.1186/1743-422X-2-42
title_sort	intracellular localization of crimean-congo hemorrhagic fever (cchf) virus glycoproteins
title_auth	Intracellular localization of Crimean-Congo Hemorrhagic Fever (CCHF) virus glycoproteins
abstract	Background Crimean-Congo Hemorrhagic Fever virus (CCHFV), a member of the genus Nairovirus, family Bunyaviridae, is a tick-borne pathogen causing severe disease in humans. To better understand the CCHFV life cycle and explore potential intervention strategies, we studied the biosynthesis and intracellular targeting of the glycoproteins, which are encoded by the M genome segment. Results Following determination of the complete genome sequence of the CCHFV reference strain IbAr10200, we generated expression plasmids for the individual expression of the glycoproteins $ G_{N} $ and $ G_{C} $, using CMV- and chicken β-actin-driven promoters. The cellular localization of recombinantly expressed CCHFV glycoproteins was compared to authentic glycoproteins expressed during virus infection using indirect immunofluorescence assays, subcellular fractionation/western blot assays and confocal microscopy. To further elucidate potential intracellular targeting/retention signals of the two glycoproteins, GFP-fusion proteins containing different parts of the CCHFV glycoprotein were analyzed for their intracellular targeting. The N-terminal glycoprotein $ G_{N} $ localized to the Golgi complex, a process mediated by retention/targeting signal(s) in the cytoplasmic domain and ectodomain of this protein. In contrast, the C-terminal glycoprotein $ G_{C} $ remained in the endoplasmic reticulum but could be rescued into the Golgi complex by co-expression of $ G_{N} $. Conclusion The data are consistent with the intracellular targeting of most bunyavirus glycoproteins and support the general model for assembly and budding of bunyavirus particles in the Golgi compartment. © Haferkamp et al; licensee BioMed Central Ltd. 2005. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (
abstractGer	Background Crimean-Congo Hemorrhagic Fever virus (CCHFV), a member of the genus Nairovirus, family Bunyaviridae, is a tick-borne pathogen causing severe disease in humans. To better understand the CCHFV life cycle and explore potential intervention strategies, we studied the biosynthesis and intracellular targeting of the glycoproteins, which are encoded by the M genome segment. Results Following determination of the complete genome sequence of the CCHFV reference strain IbAr10200, we generated expression plasmids for the individual expression of the glycoproteins $ G_{N} $ and $ G_{C} $, using CMV- and chicken β-actin-driven promoters. The cellular localization of recombinantly expressed CCHFV glycoproteins was compared to authentic glycoproteins expressed during virus infection using indirect immunofluorescence assays, subcellular fractionation/western blot assays and confocal microscopy. To further elucidate potential intracellular targeting/retention signals of the two glycoproteins, GFP-fusion proteins containing different parts of the CCHFV glycoprotein were analyzed for their intracellular targeting. The N-terminal glycoprotein $ G_{N} $ localized to the Golgi complex, a process mediated by retention/targeting signal(s) in the cytoplasmic domain and ectodomain of this protein. In contrast, the C-terminal glycoprotein $ G_{C} $ remained in the endoplasmic reticulum but could be rescued into the Golgi complex by co-expression of $ G_{N} $. Conclusion The data are consistent with the intracellular targeting of most bunyavirus glycoproteins and support the general model for assembly and budding of bunyavirus particles in the Golgi compartment. © Haferkamp et al; licensee BioMed Central Ltd. 2005. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (
abstract_unstemmed	Background Crimean-Congo Hemorrhagic Fever virus (CCHFV), a member of the genus Nairovirus, family Bunyaviridae, is a tick-borne pathogen causing severe disease in humans. To better understand the CCHFV life cycle and explore potential intervention strategies, we studied the biosynthesis and intracellular targeting of the glycoproteins, which are encoded by the M genome segment. Results Following determination of the complete genome sequence of the CCHFV reference strain IbAr10200, we generated expression plasmids for the individual expression of the glycoproteins $ G_{N} $ and $ G_{C} $, using CMV- and chicken β-actin-driven promoters. The cellular localization of recombinantly expressed CCHFV glycoproteins was compared to authentic glycoproteins expressed during virus infection using indirect immunofluorescence assays, subcellular fractionation/western blot assays and confocal microscopy. To further elucidate potential intracellular targeting/retention signals of the two glycoproteins, GFP-fusion proteins containing different parts of the CCHFV glycoprotein were analyzed for their intracellular targeting. The N-terminal glycoprotein $ G_{N} $ localized to the Golgi complex, a process mediated by retention/targeting signal(s) in the cytoplasmic domain and ectodomain of this protein. In contrast, the C-terminal glycoprotein $ G_{C} $ remained in the endoplasmic reticulum but could be rescued into the Golgi complex by co-expression of $ G_{N} $. Conclusion The data are consistent with the intracellular targeting of most bunyavirus glycoproteins and support the general model for assembly and budding of bunyavirus particles in the Golgi compartment. © Haferkamp et al; licensee BioMed Central Ltd. 2005. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (
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title_short	Intracellular localization of Crimean-Congo Hemorrhagic Fever (CCHF) virus glycoproteins
url	https://dx.doi.org/10.1186/1743-422X-2-42
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author2	Fernando, Lisa Schwarz, Tino F Feldmann, Heinz Flick, Ramon
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Intracellular localization of Crimean-Congo Hemorrhagic Fever (CCHF) virus glycoproteins

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