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The interplays between Crimean-Congo hemorrhagic fever virus (CCHFV) M segment-encoded accessory proteins and structural proteins promote virus assembly and infectivity

Freitas, Natalia ; Enguehard, Margot ; Denolly, Solene ; Levy, Camille ; Neveu, Gregory ; Lerolle, Solene ; Devignot, Stephanie ; Weber, Friedemann ; Bergeron, Eric ; Legros, Vincent ; Cosset, Francois-Loic Kuhn, Jens H.

PLoS pathogens, 2020-09, Vol.16 (9), p.e1008850 [Periódico revisado por pares]

San Francisco: Public Library of Science

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The interplays between Crimean-Congo hemorrhagic fever virus (CCHFV) M segment-encoded accessory proteins and structural proteins promote virus assembly and infectivity
Autor: Freitas, Natalia ; Enguehard, Margot ; Denolly, Solene ; Levy, Camille ; Neveu, Gregory ; Lerolle, Solene ; Devignot, Stephanie ; Weber, Friedemann ; Bergeron, Eric ; Legros, Vincent ; Cosset, Francois-Loic
Kuhn, Jens H.
Assuntos: Arachnids ; Assembly ; Biology and Life Sciences ; Bunyaviruses ; Cleavage ; Complementation ; Crimean hemorrhagic fever ; Deletion ; Egress ; Fever ; Genetic aspects ; Genomes ; Glycoprotein gp160 ; Glycoproteins ; Glycosylation ; Golgi apparatus ; Health aspects ; Health risks ; Hemorrhage ; Human health and pathology ; Infectious diseases ; Infectivity ; Life Sciences ; Localization ; Membrane proteins ; Microbiology and Parasitology ; Mucin ; Nonstructural proteins ; Particle production ; Pathogens ; Peptides ; Proteins ; Public health ; Research and Analysis Methods ; Ribonucleic acid ; RNA ; RNA polymerase ; Secretion ; Segments ; Structural proteins ; Veterinary medicine ; Viral proteins ; Virions ; Virology ; Virulence (Microbiology) ; Viruses
É parte de: PLoS pathogens, 2020-09, Vol.16 (9), p.e1008850
Notas: new_version
PMCID: PMC7529341
The authors have declared that no competing interests exist.
Descrição: Crimean-Congo hemorrhagic fever virus (CCHFV) is a tick-borne orthonairovirus that has become a serious threat to the public health. CCHFV has a single-stranded, tripartite RNA genome composed of L, M, and S segments. Cleavage of the M polyprotein precursor generates the two envelope glycoproteins (GPs) as well as three secreted nonstructural proteins GP38 and GP85 or GP160, representing GP38 only or GP38 linked to a mucin-like protein (MLD), and a double-membrane-spanning protein called NSm. Here, we examined the relevance of each M-segment non-structural proteins in virus assembly, egress and infectivity using a well-established CCHFV virus-like-particle system (tc-VLP). Deletion of MLD protein had no impact on infectivity although it reduced by 60% incorporation of GPs into particles. Additional deletion of GP38 abolished production of infectious tc-VLPs. The loss of infectivity was associated with impaired Gc maturation and exclusion from the Golgi, showing that Gn is not sufficient to target CCHFV GPs to the site of assembly. Consistent with this, efficient complementation was achieved in cells expressing MLD-GP38 in trans with increased levels of preGc to Gc conversion, co-targeting to the Golgi, resulting in particle incorporation and restored infectivity. Contrastingly, a MLD-GP38 variant retained in the ER allowed preGc cleavage but failed to rescue miss-localization or infectivity. NSm deletion, conversely, did not affect trafficking of Gc but interfered with Gc processing, particle formation and secretion. NSm expression affected N-glycosylation of different viral proteins most likely due to increased speed of trafficking through the secretory pathway. This highlights a potential role of NSm in overcoming Golgi retention and facilitating CCHFV egress. Thus, deletions of GP38 or NSm demonstrate their important role on CCHFV particle production and infectivity. GP85 is an essential viral factor for preGc cleavage, trafficking and Gc incorporation into particles, whereas NSm protein is involved in CCHFV assembly and virion secretion.
Editor: San Francisco: Public Library of Science
Idioma: Inglês

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The interplays between Crimean-Congo hemorrhagic fever virus (CCHFV) M segment-encoded accessory proteins and structural proteins promote virus assembly and infectivity

Freitas, Natalia ; Enguehard, Margot ; Denolly, Solene ; Levy, Camille ; Neveu, Gregory ; Lerolle, Solene ; Devignot, Stephanie ; Weber, Friedemann ; Bergeron, Eric ; Legros, Vincent ; Cosset, Francois-Loic Kuhn, Jens H.

San Francisco: Public Library of Science

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