Structural analyses of Shigella invasion proteins reveals non-conserved; intrinsically unstructured regions

Shigella is one of the most common bacterial pathogens that are isolated from patients with diarrhea. Various attempts are being made worldwide with encouraging observations; still the emergence of multidrug-resistant Shigella strains and a continuous high disease incidence imply that shigellosis is an unsolved global health problem which can probably be solved only by developing a proper vaccine and a vaccine regime for the disease. The need of the hour is to foster the development of an effective vaccine which should not only serve to improve hygiene but also should be able to curb infections by the pathogen. This goal can only be achieved by gaining proper detailed knowledge underlying Shigella pathogenesis. The analyses of the Shigella invasion proteins which have been long been targeted to be potential candidate vaccines remains an open ended problem and forms the core of this present computational study which identifies the fact that long regions in the structure of the proteins are disordered having no distinct structural conformation; multiple alignments however, did not show any conserved stretches in the disordered regions. The results probably explain the ability of these proteins to interact with multiple cellular proteins and perform a diverse array of functions leading to successful pathogenesis.