Polymorphism of Filovirus Glycoproteins

• Published in: Advances in Virus Research Vol. 64; pp. 359 - 381
• Main Authors: Volchkov, Viktor E., Volchkova, Valentina A., Dolnik, Olga, Feldmann, Heinz, Klenk, Hans‐Dieter
• Format: Book Chapter Journal Article
• Language: English
• Published: United States Elsevier Science & Technology 2005
• Subjects: Animals; Antigens, Viral - analysis; Filoviridae - chemistry; Filoviridae - genetics; Filoviridae - immunology; Filovirus; Glycoproteins - chemistry; Glycoproteins - genetics; Glycoproteins - immunology; Humans; Polymorphism, Genetic; Virion - chemistry; Virion - genetics; Virology
• ISBN: 012039863X; 9780120398638
• ISSN: 0065-3527; 1557-8399
• DOI: 10.1016/S0065-3527(05)64011-0

Filoviral glycoproteins are encoded by gene 4 (GP gene) of the nonsegmented negative-strand RNA genome. Nonstructural glycoprotein (sGP) as well as Ebola virus (EBOV) and Marburgvirus (MBGV) GP undergo several posttranslational processing steps giving rise to a whole series of different glycoproteins. Comparison of the GP sequences of Marburg virus (MBGV) and Ebola virus (EBOV) shows conservation at the amino-terminal and carboxy-terminal ends, whereas the middle region is variable. GP can be subdivided into a large ectodomain, a lipid membrane-spanning domain of approximately 30 amino acids, and a short cytoplasmic tail of 4 (EBOV) and 8 (MBGV) amino acids, respectively. Sequence comparison has revealed several striking similarities between GP2 of filoviruses and the transmembrane glycoprotein of retroviruses. According to data, GP2 contains a hydrophobic fusion peptide at a distance of 22 (EBOV) or 91 (MBGV) amino acids from the amino terminus. Between the fusion domain, which is flanked by two cysteines, and the transmembrane domain there are two amphipathic helices separated by a CX6CC motif. It is indicated that maturation and release of GP in membrane-bound form does not depend on other viral proteins.