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dc.contributor.authorGladue, Douglas
dc.contributor.authorGómez Lucas, Lidia
dc.contributor.authorLargo, Eneko
dc.contributor.authorVelazquez-Salinas, Lauro
dc.contributor.authorRamirez-Medina, Elizabeth
dc.contributor.authorTorralba, Johana
dc.contributor.authorQueralt-Martin, Maria
dc.contributor.authorAlcaraz, Antonio
dc.contributor.authorNieva, Jose L
dc.contributor.authorBorca, Manuel V.
dc.date.accessioned2023-09-12T07:52:24Z
dc.date.available2023-09-12T07:52:24Z
dc.date.issued2023-05-22
dc.identifier.citationGladue, D. P., Gomez-Lucas, L., Largo, E., Velazquez-Salinas, L., Ramirez-Medina, E., Torralba, J., ... & Borca, M. V. (2023). African Swine Fever Virus Gene B117L Encodes a Small Protein Endowed with Low-pH-Dependent Membrane Permeabilizing Activity. Journal of Virology, e00350-23.ca_CA
dc.identifier.issn0022-538X
dc.identifier.issn1098-5514
dc.identifier.urihttp://hdl.handle.net/10234/204133
dc.description.abstractAfrican swine fever virus (ASFV) is causing a devastating pandemic in domestic and wild swine in Central Europe to East Asia, resulting in economic losses for the swine industry. The virus contains a large double-stranded DNA genome that contains more than 150 genes, most with no experimentally characterized function. In this study, we evaluate the potential function of the product of ASFV gene B117L, a 115-amino-acid integral membrane protein transcribed at late times during the virus replication cycle and showing no homology to any previously published protein. Hydrophobicity distribution along B117L confirmed the presence of a single transmembrane helix, which, in combination with flanking amphipathic sequences, composes a potential membrane-associated C-terminal domain of ca. 50 amino acids. Ectopic transient cell expression of the B117L gene as a green fluorescent protein (GFP) fusion protein revealed the colocalization with markers of the endoplasmic reticulum (ER). Intracellular localization of various B117L constructs also displayed a pattern for the formation of organized smooth ER (OSER) structures compatible with the presence of a single transmembrane helix with a cytoplasmic carboxy terminus. Using partially overlapping peptides, we further demonstrated that the B117L transmembrane helix has the capacity to establish spores and ion channels in membranes at low pH. Furthermore, our evolutionary analysis showed the high conservation of the transmembrane domain during the evolution of the B117L gene, indicating that the integrity of this domain is preserved by the action of the purifying selection. Collectively our data support a viroporin-like assistant role for the B117L gene-encoded product in ASFV entry.ca_CA
dc.format.extent53 p.ca_CA
dc.format.mimetypeapplication/pdfca_CA
dc.language.isoengca_CA
dc.publisherAmerican Society for Microbiologyca_CA
dc.relation.isPartOfJournal of Virology. Vol. 97, No. 6ca_CA
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/ca_CA
dc.subjectafrican swine fever virusca_CA
dc.subjectgene B117Lca_CA
dc.titleAfrican Swine Fever Virus Gene B117L Encodes a Small Protein Endowed with Low-pH-Dependent Membrane Permeabilizing Activityca_CA
dc.typeinfo:eu-repo/semantics/articleca_CA
dc.identifier.doihttps://doi.org/10.1128/jvi.00350-23
dc.rights.accessRightsinfo:eu-repo/semantics/openAccessca_CA
dc.type.versioninfo:eu-repo/semantics/acceptedVersionca_CA
project.funder.nameBasque Governmentca_CA
project.funder.nameNational Pork Boardca_CA
project.funder.nameFoundation for Food and Agriculture Researchca_CA
oaire.awardNumber#IT1449-22ca_CA
oaire.awardNumber21-137ca_CA


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