Abstract
Human septins comprise a family of 13 genes that encode conserved GTP-binding proteins. They form nonpolar complexes, which assemble into higher-order structures, such as bundles, scaffolding structures, or rings. Septins are counted among the cytoskeletal elements. They interact with the actin and microtubule networks and can bind to membranes. Many cellular functions with septin participation have been described in the literature, including cytokinesis, motility, forming of scaffolding platforms or lateral diffusion barriers, vesicle transport, exocytosis, and recognition of micron-scale curvature. Septin dysfunction has been implicated in diverse human pathologies, including neurodegeneration and tumorigenesis. Moreover, septins are thought to affect the outcome of host–microbe interactions. Implication of septins has been demonstrated in fungal, bacterial, and viral infections. Knowledge on the precise function of a particular septin in the different steps of the virus infection and replication cycle is still limited. Published data for vaccinia virus (VACV), hepatitis C virus (HCV), influenza A virus (H1N1 and H5N1), human herpesvirus 8 (HHV-8), and Zika virus (ZIKV), all of major concern for public health, will be discussed here.
Highlights
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The human genome encodes 13 septin genes classified into four homology groups based on sequence similarity (SEPT2, SEPT3, SEPT6, and SEPT7)
The SETP2 group comprises SEPTIN1, SEPTIN2, SEPTIN4, and SEPTIN5; the SEPT3 group SEPTIN3, SEPTIN9, and SEPTIN12; the SEPT6 group SEPTIN6, SEPTIN8, SEPTIN10, SEPTIN11, and SEPTIN14, while SEPTIN7 is the only member of the SEPT7 group [3]
Summary
Septins are a family of conserved GTPases belonging to the GTPase superclass of P-loop NTPases [1]. Septin complexes polymerize end-to-end to form apolar filaments, which can associate to form higher-order structures, such as bundles, scaffolding structures, or rings. Because of their filamentous appearance and their association with cellular membranes, actin filaments and microtubules, septins are considered as the fourth component of the cytoskeleton [3]. Higher-order septin ring-like structures, tightly associated with the plasma membrane, are located at the base of these processes. By interacting with the nucleotide-binding pocket of septins, FCF interferes with the GTP-binding dynamics and turnover leading to changes in polymerization and stability of septin filaments [38]. Modification of the chemical structure of FCF might lead to the development of new analogues with improved therapeutic potential and less side effects [42,43]
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