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African Swine Fever Virus Gene B117L Encodes a Small Protein Endowed with Low-pH-Dependent Membrane Permeabilizing Activity

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العنوان: African Swine Fever Virus Gene B117L Encodes a Small Protein Endowed with Low-pH-Dependent Membrane Permeabilizing Activity
المؤلفون: Gladue, Douglas P., Gómez-Lucas, Lidia, Largo, Eneko, Velázquez-Salinas, Lauro, Ramírez-Medina, Elizabeth, Torralba, Johana, Queralt, María, Alcaraz, Antonio, Nieva, José Luis, Borca, Manuel V.
المساهمون: Eusko Jaurlaritza, National Pork Board (US), Foundation for Food & Agriculture Research, Gladue, Douglas P.
بيانات النشر: American Society for Microbiology
سنة النشر: 2023
المجموعة: Digital.CSIC (Consejo Superior de Investigaciones Científicas / Spanish National Research Council)
مصطلحات موضوعية: ASFV, B117L, Viroporin
الوصف: African 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. IMPORTANCE ASFV is responsible for an extensively distributed pandemic causing important economic losses in the pork industry in Eurasia. The development of countermeasures is partially limited by the insufficient knowledge regarding the function of the majority of the more than 150 genes present on ...
نوع الوثيقة: article in journal/newspaper
اللغة: English
تدمد: 0022-538X
1098-5514
Relation: Gladue, Douglas P.; Gómez-Lucas, Lidia; Largo, Eneko; Velázquez-Salinas, Lauro; Ramírez-Medina, Elizabeth; Torralba, Johana; Queralt, María; Alcaraz, Antonio; Nieva, José Luis; Borca, Manuel V.; 2023; Supplemental Material African Swine Fever Virus Gene B117L Encodes a Small Protein Endowed with Low-pH-Dependent Membrane Permeabilizing Activity [Dataset]; American Society for Microbiology; https://doi.org/10.1128/jvi.00350-23; https://doi.org/10.1128/jvi.00350-23; Sí; Journal of Virology 97(6): e00350-23 (2023); http://hdl.handle.net/10261/339033; http://dx.doi.org/10.13039/501100003086; 2-s2.0-85164233401; https://api.elsevier.com/content/abstract/scopus_id/85164233401
DOI: 10.1128/jvi.00350-23
DOI: 10.13039/501100003086
الاتاحة: http://hdl.handle.net/10261/339033
https://doi.org/10.1128/jvi.00350-23
https://doi.org/10.13039/501100003086
https://api.elsevier.com/content/abstract/scopus_id/85164233401
Rights: none
رقم الانضمام: edsbas.DD60F953
قاعدة البيانات: BASE
الوصف
تدمد:0022538X
10985514
DOI:10.1128/jvi.00350-23