Intrinsically Disordered Proteins in Host Function and Subversion by Pathogens

Dear Colleagues,

Many proteins critical to cell function as well as pathogenic conditions are intrinsically disordered proteins (IDPs) or contain intrinsically disordered regions (IDRs). These IDP/IDRs lack persistent structure in solution, and their inherent plasticity enables them to bind to multiple partners. This is integral to host processes such as transport into and out of the nucleus, which in turn is central to cell signalling in innate immune responses. The ability to bind to multiple partners is also key to the strategies pathogens use to circumvent the innate immune response. Clearly, delineating the relationship between IDP/IDR structure and function is central to understanding the host–pathogen interface.
This relationship is complicated, however, by the fact that inherent lack of structure hampers high-resolution structure determination. Innovative approaches are required to give insight into the molecular detail and dynamics of IDPs/IDRs, how this impacts host cell function and how it is exploited by pathogens.
This Special Issue will focus on the basic biology of host- and pathogen-derived IDRs and IDPs, as well as their contribution to innate immunity and infection.

Dr. Natalie Borg
Prof. David A. Jans
Guest Editors

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