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The order Mononegavirales harbors numerous viruses of significant relevance to human health, including both established and emerging infections. Currently, vaccines are only available for a small subset of these viruses, and antiviral therapies remain limited. Being obligate cellular parasites, viruses must utilize the cellular machinery for their replication and spread. Therefore, targeting cellular pathways used by viruses can provide novel therapeutic approaches. One of the key challenges confronted by both hosts and viruses alike is the successful folding and maturation of proteins. In cells, this task is faced by cellular molecular chaperones, a group of conserved and abundant proteins that oversee protein folding and help maintain protein homeostasis. In this review, we summarize the current knowledge of how the Mononegavirales interact with cellular chaperones, highlight key gaps in our knowledge, and discuss the potential of chaperone inhibitors as antivirals.
Protein Folding, respiratory syncytial virus, Hsp90, Review, Respiratory syncytial virus, Virus Replication, Microbiology, Antiviral Agents, Hsp70, Ebola virus, antivirals, Virology, Chaperones, chaperones, Humans, rabies virus, HSP70 Heat-Shock Proteins, HSP90 Heat-Shock Proteins, Biology and Life Sciences, <i>Mononegavirales</i>, Antivirals, QR1-502, CCT, Respiratory Syncytial Viruses, Mumps virus, Rabies virus, Measles virus, measles virus, Host-Pathogen Interactions, mumps virus, Mononegavirales, Molecular Chaperones
Protein Folding, respiratory syncytial virus, Hsp90, Review, Respiratory syncytial virus, Virus Replication, Microbiology, Antiviral Agents, Hsp70, Ebola virus, antivirals, Virology, Chaperones, chaperones, Humans, rabies virus, HSP70 Heat-Shock Proteins, HSP90 Heat-Shock Proteins, Biology and Life Sciences, <i>Mononegavirales</i>, Antivirals, QR1-502, CCT, Respiratory Syncytial Viruses, Mumps virus, Rabies virus, Measles virus, measles virus, Host-Pathogen Interactions, mumps virus, Mononegavirales, Molecular Chaperones
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