Viroporin-like activity of the hairpin transmembrane domain of African swine fever virus B169L protein.

ABSTRACT: African swine fever virus (ASFV) is the causative agent of a contagious disease affecting wild and domestic swine. The function of B169L protein, as a potential integral structural membrane protein, remains to be experimentally characterized. Using state-of-the-art bioinformatics tools, we confirm here earlier predictions indicating the presence of an integral membrane helical hairpin, and further suggest anchoring of this protein to the ER membrane, with both terminal ends facing the lumen of the organelle. Our evolutionary analysis confirmed the importance of purifying selection in the preservation of the identified domains during the evolution of B169L in nature. Also, we address the possible function of this hairpin transmembrane domain (HTMD) as a class IIA viroporin. Expression of GF

SUBMITTER: Gladue DP 

PROVIDER: S-EPMC11334534 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature