Recruitment of Hsp70 chaperones: a crucial part of viral survival strategies.
Virus proliferation depends on the successful recruitment of host cellular components for their own replication, protein synthesis, and virion assembly. In the course of virus particle production a large number of proteins are synthesized in a relatively short time, whereby protein folding can become a limiting step. Most viruses therefore need cellular chaperones during their life cycle. In addition to their own protein folding problems viruses need to interfere with cellular processes such as signal transduction, cell cycle regulation and induction of apoptosis in order to create a favorable environment for their proliferation and to avoid premature cell death. Chaperones are involved in the control of these cellular processes and some viruses reprogram their host cell by interacting with them. Hsp70 chaperones, as central components of the cellular chaperone network, are frequently recruited by viruses. This review focuses on the function of Hsp70 chaperones at the different stages of the viral life cycle emphasizing mechanistic aspects.
Mayer
M P
MP
Zentrum für Molekulare Biologie, Universität Heidelberg, Im Neuenheimer Feld 282, 69120, Heidelberg, Germany. M.Mayer@zmbh.uni-heidelberg.de
D000818:Animals; D017209:Apoptosis; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D017510:Protein Folding; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism; D014771:Virion / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D014779:Virus Replication / Q000235:genetics / Q000502:physiology*
D018840:HSP70 Heat-Shock Proteins; D014764:Viral Proteins