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Tytuł:
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Role of the conserved E2 residue G259 in classical swine fever virus production and replication.
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Autorzy:
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Yi W; State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China.
Zheng F; State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China.
Zhu H; State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China.
Wu Y; State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China.
Wei J; State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China.
Pan Z; State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China. Electronic address: .
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Źródło:
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Virus research [Virus Res] 2022 May; Vol. 313, pp. 198747. Date of Electronic Publication: 2022 Mar 18.
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Typ publikacji:
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Journal Article; Research Support, Non-U.S. Gov't
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Język:
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English
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Imprint Name(s):
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Original Publication: Amsterdam : Elsevier Science, c1984-
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MeSH Terms:
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Classical Swine Fever*
Classical Swine Fever Virus*/genetics
Diarrhea Viruses, Bovine Viral*/genetics
Pestivirus*
Animals ; Swine ; Viral Envelope Proteins
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Contributed Indexing:
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Keywords: Classical swine fever virus; E2 glycoprotein; Infectious virus production
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Substance Nomenclature:
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0 (Viral Envelope Proteins)
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Entry Date(s):
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Date Created: 20220322 Date Completed: 20220405 Latest Revision: 20220531
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Update Code:
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20240104
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DOI:
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10.1016/j.virusres.2022.198747
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PMID:
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35314201
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The E2 glycoprotein of classical swine fever virus (CSFV) plays multiple roles in the viral life cycle. The chimeric live attenuated C strain with the E2 substitution of bovine viral diarrhea virus (BVDV) is a promising marker vaccine candidate. In this study, the recombinant chimeric CSFV/bE2 cDNA clone harboring heterologous E2 (bE2) of BVDV was constructed by genetic approaches. Recombinant infectious virus rCSFV/bE2 (P11) was recovered by 11 serial passages of transfected PK15 cells. Viral genome sequencing showed that a glutamic acid to glycine mutation (E260G) at position 260 of the bE2 was observed in rCSFV/bE2 P11. Alignment of amino acid sequences displayed that the glycine was one of three conserved residues in pestivirus E2. When the glutamic acid to glycine substitution (E260G) was introduced into chimeric CSFV/bE2 cDNA clone, the high-titer infectious rCSFV/bE2 E260G was rescued. The glycine to glutamic acid substitution at corresponding position in CSFV E2 resulted in significantly decreased rCSFV/E2 G259E production. We further identified that the conserved E2 residue G259 played a critical role in the release and binding activity of CSFV and that the E2 residues G259 and V111 modulated synergistically infectious virus production and replication.
(Copyright © 2022 Elsevier B.V. All rights reserved.)
