Intrinsically disordered proteins (IDPs) and proteins with long intrinsically disordered protein regions (IDPRs) lack ordered
structure but are involved in a multitude of biological processes, where they often serve as major regulators and controllers of various
functions of their binding partners. Furthermore, IDPs/IDPRs are often related to the pathogenesis of various diseases, including cancer.
Intrinsic disorder confers multiple functional advantages to its carriers. As a result, due to their functional versatility and structural plasticity,
IDPs and IDPRs are common in various proteomes, including proteomes of different pathological organisms. Viruses are “welleducated”
users of various aspects of intrinsic disorder for their advantage. These small but highly efficient invaders broadly use intrinsic
disorder to overrun the host organism’s defense system, as well as to seize and overrun host systems and pathways forcing them to work
for the virus needs, to ensure accommodation of viruses to their variable and often hostile habitats, and to promote and support the economic
usage of the viral genetic material. Human papillomaviruses (HPVs), with their tiny proteomes (the entire HPV genome includes
just eight open reading frames), intricate life cycle, and ability to either cause benign papillomas/warts or promote the development of
carcinomas of the genital tract, head and neck and epidermis, attracted considerable attention of researchers. This review analyzes the
plentitude and demeanor of intrinsic disorder in proteins from HPVs and their cellular targets.
Intrinsically disordered protein, protein function, protein-protein interaction, protein-nucleic acid interaction, human
Department of Molecular Medicine, University of South Florida, 12901 Bruce B. Downs Blvd. MDC07, Tampa, Florida 33612, USA.