| Description | This superfamily represents the N-terminal α-helical subdomain of VP35 IID.The C-terminal interferon inhibitory (IID) domain of VP35, also known as RNA-binding domain (RBD) IID is made of a stretch of about 120 residues that folds independently. The VP35 IID structure is organised into 2 subdomains: an N-terminal α-helical subdomain and a C-terminal β-sheet subdomain. The α-helical subdomain consists of a four helix bundle, while the β-sheet subdomain is formed by four antiparallel β-strands as well as an α-helix and a type II polyproline helix. The VP35 IID structure contains 2 basic patches that are highly conserved among members of the Filoviridae family. The first basic patch is located in the helical subdomain and its functional significance remains unknown. The second one, the so-called central basic patch, is located in the β-sheet subdomain and contains residues that are required for dsRNA binding and IFN inhibition [ , , ].The Filoviridae family of viruses, which includes marburgvirus (MARV) and ebolavirus (EBOV), can cause intermittent outbreaks that often result in highfatality rates. The family consists of five species of EBOV, Zaire, Reston, Sudan, Tai Forest, and Bundibugyo; one species of MARV; and a proposed genusCuevavirus possessing a single species Lloviu cuevavirus. MARV and EBOV share a common genome organisation but show important differences in replicationcomplex formation, cell entry, host tropism, transcriptional regulation, and immune evasion [, , , ].Filoviruses counteract innate immunity through the multifunctional viral protein (VP) 35 proteins, which perform critical roles in viral RNA synthesis,virus assembly, and virus structure. VP35 contains an N-terminal coiled-coil domain required for its oligomerisation and a C-terminal interferon (IFN)inhibitory domain (IID). Mutations within the VP35 IID result in loss of host immune suppression. The N terminus provides a critical oligomerisationfunction, which facilitates efficient IFN inhibition through elements located at the C terminus of VP35. The VP35 IID can also bind dsRNA and VP35-mediatedIFN antagonism correlates with dsRNA-binding activity [ , , , ]. | Name | Filoviruses VP35 interferon inhibitory domain, helical subdomain |
| Short Name | VP35_IID_hlx | Type | Homologous_superfamily |
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