Secreted in a Type III Secretion System-Dependent Manner, EsaH and EscE Are the Cochaperones of the T3SS Needle Protein EsaG of Edwardsiella piscicida

Abstract

Edwardsiella piscicida causes severe hemorrhagic septicemia in fish. Inactivation of the type III secretion system (T3SS) increases its 50% lethal dose (LD 50 ) by ~10 times.

Edwardsiella piscicida infection reshapes the intestinal microbiome and metabolome of big-belly seahorses: mechanistic insights of synergistic actions of virulence factors

“…As E. piscicida possesses virulence factors (VFs) similar to many intestinal pathogens, such as Flagella, adherence, invasion, type III and type VI secretion systems (T3SS and T6SS), quorum sensing (QS) regulators, iron uptake, two-component systems (TCS), toxins, and invasion proteins (1)(2)(3), it could be used as an attractive model organism to study the role of a single VF or a combination of VFs in pathogenic process (1)(2)(3). Unfortunately, current researches have mainly focused on revealing the functional mechanisms of single VFs in E. piscicida-induced diseases in mammals (1,4,5); the related research in fish is limited. Therefore, exploring the potential mechanisms underlying the mutual interaction of VFs to induce deep infection may not only enrich the knowledge of E. piscicida-induced enteritis in fish but also provide theoretical references for development of optimal strategies for the control and prevention of such diseases.…”

Edwardsiella tarda Attenuates Virulence upon Oxytetracycline Resistance

“…The abundance of proteins in the type VI secretion system (T6SS), type III secretion system (T3SS), and flagellum system was downregulated (Figure ). Previous studies have demonstrated that the chaperone protein EscE interacts with the apparatus EsaH and EsaG (a T3SS needle protein) and that EscE and EsaH are cochaperones of EsaG . EseC inhibits biofilm formation by sequestering the chaperone EseE .…”

“…EseC inhibits biofilm formation by sequestering the chaperone EseE . EscA and EseE are cochaperones of EseC, and EseE promotes its secretion. , The disordered region of the T6SS effector EvpP is essential for EvpC binding . FilC and FliC are flagellar filament components associated with the ability of bacteria to swim .…”

“…Previous studies have demonstrated that the chaperone protein EscE interacts with the apparatus EsaH and EsaG (a T3SS needle protein) and that EscE and EsaH are cochaperones of EsaG. 26 EseC inhibits biofilm formation by sequestering the chaperone EseE. 27 EscA and EseE are cochaperones of EseC, and EseE promotes its secretion.…”