Disease relevance of sGP

• When sGP expressed from vaccinia virus vectors was analyzed by pulse-chase experiments using SDS-PAGE under reducing conditions, the mature form and two different precursors have been identified [1].

Psychiatry related information on sGP

• Whether the soluble glycoproteins GP1 and sGP interfere with the humoral immune response and other defense mechanisms remains to be determined [2].

High impact information on sGP

• Protection was achieved and correlated with antibody titer and antigen-specific T-cell responses to sGP or GP [3].
• The mutant was significantly more cytotoxic than wild-type virus, indicating that cytotoxicity caused by GP is down-regulated by the virus through transcriptional RNA editing and expression of sGP [4].
• Ebola virus secretory glycoprotein (sGP) diminishes Fc gamma RIIIB-to-CR3 proximity on neutrophils [5].
• In contrast, the soluble glycoproteins sGP and delta-peptide did not activate endothelial cells or change the endothelial barrier function [6].
• Delta-peptide is the carboxy-terminal cleavage fragment of the nonstructural small glycoprotein sGP of Ebola virus [1].

Biological context of sGP

• It is unlikely that sGP plays a role in the Ebola virus pathogenesis through interfering with the innate immunity by targeting neutrophils [7].
• Studies employing site-directed mutagenesis revealed that sGP was cleaved at a multibasic amino acid motif at positions 321 to 324 of the open reading frame [1].
• Formic acid hydrolysis of sGP demonstrated that sGP dimers consist of monomers in antiparallel orientation [8].

Anatomical context of sGP

• First, the endoplasmic reticulum form sGP(er), full-length sGP with oligomannosidic N-glycans, was detected, sGP(er) was then replaced by the Golgi-specific precursor pre-sGP, full-length sGP containing complex N-glycans [1].

Associations of sGP with chemical compounds

• Another editing product of the GP gene of Ebola virus (ssGP), which shares 295 amino-terminal amino acid residues with sGP, is secreted from cells in a monomeric form due to the lack of the carboxyl-terminal part (present in sGP), including cysteine at position 306 [8].

References