Heat-shock protein 70 is associated with the entry of Marek΄s disease virus into fibroblast

Abstract

Summary. -Literature pertaining to the interactions between Marek΄s disease virus (MDV) entry-related glycoproteins and corresponding receptors is still limited. Results from a Western blot analysis of cellular proteins for virus receptors and co-immunoprecipitation suggest that heat shock protein 70 (HSP70) is a potential cellular receptor for MDV glycoprotein gH. Plaque inhibition assays confirm the involvement of HSP70 in the early stages of MDV entry into chicken embryo fibroblasts (CEF). The present work supports that HSP70 is implicated in the MDV entry process by binding to gH, and enhances the understanding of multifunctional HSP70 and the MDV infection process.

Heat shock protein 70, glutamate dehydrogenase, and angiotensin-converting enzyme of Bombyx mori mediate the cell attachment of Cypovirus 1

“…The interaction between BmACE HSP70 is a 70 kDa housekeeping protein chaperone located on the cell surface of several prokaryotes and eukaryotes cells, and it is responsible for assuring nascent protein folding, refolding misfolded proteins, and facilitating protein transportation [36]. Research indicated that HSP70 contributes to the attachment and cell entry of multiple viruses such as rotavirus [21], dengue virus [37], Japanese encephalitis virus [38], Marek's disease virus [39], Hazara virus [40], Chikungunya virus [41], grass carp reovirus [42],…”

“…HSP70 is a 70 kDa housekeeping protein chaperone located on the cell surface of several prokaryotes and eukaryotes cells, and it is responsible for assuring nascent protein folding, refolding misfolded proteins, and facilitating protein transportation [36]. Research indicated that HSP70 contributes to the attachment and cell entry of multiple viruses such as rotavirus [21], dengue virus [37], Japanese encephalitis virus [38], Marek’s disease virus [39], Hazara virus [40], Chikungunya virus [41], grass carp reovirus [42], Tembusu virus [43], enterovirus 71 [44], and echovirus 9 [45], in which HSP70 functioned as receptor, supplemental receptor, or accessory factor that facilitates viral binding to host cells and viral entry. Based on the findings of this study, we suggest that HSP70 of B. mori could be employed by DpCPV to facilitate viral attachment and cell entry.…”