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Fig. 2 | BMC Veterinary Research

Fig. 2

From: An insight into the transmission role of insect vectors based on the examination of gene characteristics of African swine fever virus originated from non-blood sucking flies in pig farm environments

Fig. 2

Detailed view of the A179L:BH3 peptide interfaces. a Beclin-BH3 peptide (light blue) binds to a groove formed by α-helices of ASFV A179L (brown) from M. domestica flies. b ASFV A179L from Georgia/2007 is shown in grey on the molecular surface, with the floor of the binding groove shown in brown. Beclin-BH3 is shown in light blue. c-d Hydrophobicity of ASFV A179L-BH3 protein structure. Different colors represent different degrees of hydrophobicity, ranging from + 3 to− 3. c Hydrophobic residues in yellow are distributed in the binding groove of ASFV A179L-BH3 from M. domestica flies. d Hydrophilic residues in blue are distributed in the binding groove of A179L-BH3from the Georgia/2007 strain. e–f The six conserved hydrophobic residues of Beclin-BH3 (Tyr46, Glu64, Asn83, Gly85, Arg80, and Asp86) are involved in binding grooves, but with different directions of interaction. Different colors represent amino acids from different species. Amino acids in ASFV A179L from Georgia/2007 and M. domestica flies are shown in light blue or light purple, respectively

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BMC Veterinary Research

ISSN: 1746-6148

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