sGP seems to possess an anti-inflammatory activity as it can reverse the barrier-decreasing effects of TNF alpha. Might therefore contribute to the lack of inflammatory reaction seen during infection in spite the of extensive necrosis and massive virus production. Does not seem to be involved in activation of primary macrophages. Does not seem to interact specifically with neutrophils. Viroporin that permeabilizes mammalian cell plasma membranes. It acts by altering permeation of ionic compounds and small molecules. This activity may lead to viral enterotoxic activity. sGP is a homodimer; disulfide-linked. The homodimers are linked by two disulfide bonds in a parallel orientation. Delta-peptide is a monomer (By similarity). Pre-sGP is N-glycosylated. This precursor is processed into mature sGP and delta-peptide by host furin or furin-like proteases. The cleavage site corresponds to the furin optimal cleavage sequence [KR]-X-[KR]-R. Both cleavage fragments contain sialic acid, but only the delta-peptide is O-glycosylated (By similarity). Partially edited. RNA editing at this position consists of an insertion of one adenine nucleotide. The sequence displayed here is the small secreted glycoprotein, derived from the unedited RNA. The edited RNA gives rise to the full-length transmembrane glycoprotein (AC Q89853). Belongs to the filoviruses glycoprotein family.