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Comparative analysis of the L, M, and S RNA segments of Crimean–Congo haemorrhagic fever virus isolates from southern Africa
Author(s) -
Goedhals Dominique,
Bester Phillip A.,
Paweska Janusz T.,
Swanepoel Robert,
Burt Felicity J.
Publication year - 2015
Publication title -
journal of medical virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 121
eISSN - 1096-9071
pISSN - 0146-6615
DOI - 10.1002/jmv.24079
Subject(s) - biology , virology , glycoprotein , transmembrane domain , conserved sequence , genetics , orfs , sequence alignment , genome , bunyaviridae , virus , transmembrane protein , peptide sequence , amino acid , gene , open reading frame , receptor
Crimean–Congo haemorrhagic fever virus (CCHFV) is a member of the Bunyaviridae family with a tripartite, negative sense RNA genome. This study used predictive software to analyse the L (large), M (medium), and S (small) segments of 14 southern African CCHFV isolates. The OTU‐like cysteine protease domain and the RdRp domain of the L segment are highly conserved among southern African CCHFV isolates. The M segment encodes the structural glycoproteins, G N and G C, and the non‐structural glycoproteins which are post‐translationally cleaved at highly conserved furin and subtilase SKI‐1 cleavage sites. All of the sites previously identified were shown to be conserved among southern African CCHFV isolates. The heavily O‐glycosylated N‐terminal variable mucin‐like domain of the M segment shows the highest sequence variability of the CCHFV proteins. Five transmembrane domains are predicted in the M segment polyprotein resulting in three regions internal to and three regions external to the membrane across the G N , NS M and G C glycoproteins. The corroboration of conserved genome domains and sequence identity among geographically diverse isolates may assist in the identification of protein function and pathogenic mechanisms, as well as the identification of potential targets for antiviral therapy and vaccine design. As detailed functional studies are lacking for many of the CCHFV proteins, identification of functional domains by prediction of protein structure, and identification of amino acid level similarity to functionally characterised proteins of related viruses or viruses with similar pathogenic mechanisms are a necessary step for selection of areas for further study. J. Med. Virol. 87:717–724, 2015 . © 2015 Wiley Periodicals, Inc.