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. 2018 Oct;3(10):1084-1089.
doi: 10.1038/s41564-018-0227-2. Epub 2018 Aug 27.

The Discovery of Bombali Virus Adds Further Support for Bats as Hosts of Ebolaviruses

Free PMC article

The Discovery of Bombali Virus Adds Further Support for Bats as Hosts of Ebolaviruses

Tracey Goldstein et al. Nat Microbiol. .
Free PMC article

Erratum in

  • Author Correction: The discovery of Bombali virus adds further support for bats as hosts of ebolaviruses.
    Goldstein T, Anthony SJ, Gbakima A, Bird BH, Bangura J, Tremeau-Bravard A, Belaganahalli MN, Wells HL, Dhanota JK, Liang E, Grodus M, Jangra RK, DeJesus VA, Lasso G, Smith BR, Jambai A, Kamara BO, Kamara S, Bangura W, Monagin C, Shapira S, Johnson CK, Saylors K, Rubin EM, Chandran K, Lipkin WI, Mazet JAK. Goldstein T, et al. Nat Microbiol. 2018 Dec;3(12):1486. doi: 10.1038/s41564-018-0315-3. Nat Microbiol. 2018. PMID: 30410089


Here we describe the complete genome of a new ebolavirus, Bombali virus (BOMV) detected in free-tailed bats in Sierra Leone (little free-tailed (Chaerephon pumilus) and Angolan free-tailed (Mops condylurus)). The bats were found roosting inside houses, indicating the potential for human transmission. We show that the viral glycoprotein can mediate entry into human cells. However, further studies are required to investigate whether exposure has actually occurred or if BOMV is pathogenic in humans.


Figure 1.
Figure 1.
Phylogenetic tree comparing the relationship of BOMV to other known filoviruses. Each protein presented separately (i-vii) and as a complete genome (viii). Genbank accession numbers for reference sequences included in Supplemental Data.
Figure 2.
Figure 2.
BOMV GP-mediated entry and infection is NPC1-dependent. (A) BOMV GP1,2 is incorporated in the rVSV particles detected by immunoblotting using ebolavirus anti-GP1 (B) Infectivity of rVSVs bearing BOMV, EBOV or VSV GP1 on WT or NPC1-KO U2OS cells complemented with or without human NPC1 cDNA. (C) GP1 alignment of the known human- infecting ebolaviruses (EBOV, SUDV, RESTV, BDBV, TAFV) and BOMV. Displayed regions pertain to the GP1 interface based on the GP1-human NPC1 crystal structure (PDB: 5F1B). Conserved residues in blue; viral-specific residues in yellow. Squared positions correspond to residues whose side chain heavy atoms are within 5 Â of any heavy atom in the human NPC1 receptor. (D) Left panel: Atomic representation of the interaction between the human NPC1 (red) and the EBOV GPi protein (blue) (PDB: 5F1B). Middle panel: Close-up view of the interface. Right panel: Close-up view of the modeled interface between the human NPC1 crystal structure (red) and the BOMV GP1 atomic model (blue). Displayed viral residues (in yellow) correspond to interfacial positions with different amino acids in the BOMV GP1 protein. Displayed residues on the human NPC1 (in white) correspond to residues with side chain heavy atoms within 5 Å of residues 146 and/or 148 in the EBOV or BOMV GP1.

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