Recruitment of PI4KIIIβ to coxsackievirus B3 replication organelles is independent of ACBD3, GBF1, and Arf1

作者: C. M. Dorobantu , H. M. van der Schaar , L. A. Ford , J. R. P. M. Strating , R. Ulferts

DOI: 10.1128/JVI.03650-13

关键词:

摘要: Members of the Enterovirus (poliovirus [PV], coxsackieviruses, and human rhinoviruses) Kobuvirus (Aichi virus) genera in Picornaviridae family rely on PI4KIIIβ (phosphatidylinositol-4-kinase IIIβ) for efficient replication. The small membrane-anchored enteroviral protein 3A recruits to replication organelles, yet underlying mechanism has remained elusive. Recently, it was shown that kobuviruses recruit through interaction with ACBD3 (acyl coenzyme A [acyl-CoA]-binding domain 3), a novel partner PI4KIIIβ. Therefore, we investigated possible role recruiting enterovirus organelles. Although interacted directly coxsackievirus B3 (CVB3) 3A, its depletion from cells by RNA interference did not affect recruitment organelles impair CVB3 previously also proposed via GBF1/Arf1, based known GBF1, an important regulator secretory pathway transport guanine nucleotide exchange factor (GEF) Arf1. However, our results demonstrate inhibition GBF1 or Arf1 either pharmacological interfering (siRNA) treatment ability Furthermore, show mutant no longer binds capable PI4KIIIβ, even ACBD3-depleted cells. Together, findings indicate unlike originally envisaged, independently GBF1/Arf1. IMPORTANCE hallmark infection is generation new membranous structures support viral functionality these “replication organelles” depends concerted actions both nonstructural proteins co-opted host factors. It thus essential understand how are formed which cellular components key players this process. GBF1/Arf1 have been contribute lipid-modifying enzyme Here independent ACBD3. This study shows strategy employed far more complex than initially anticipated.

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