Fig. 10

Protein-protein interactions. Stronger associations are represented by blue thick lines. The predicted functional partners for our query protein adeK are a family of adeA, adeJ, adeI, multidrug ABC transporter and multidrug efflux pump. Pili assembly chaperone and P Pilus assembly protein, which are responsible for pili assembly have interaction with a fimbrial protein. Outer membrane protein OmpA interacts with TolB (involved in TonB-independent uptake of colicins) and peptidoglycan associated lipoprotein. ponA (penicillin binding protein 1a) and general secretion pathway protein D interacts with a group of Type IV pili proteins, including Tfp pilus assembly protein PilP, type IV fimbrial biogenesis protein PilO and type IV pilus assembly protein PilM. These interactions show that the bacteria possess flagellum independent surface associated motility, and ponA and general secretion pathway protein D assist the type IV pili multi-protein in exhibiting this property in A. baumannii. These associations aid bacteria to adhere to biotic and abiotic surfaces and facilitate in enhanced virulence, colonization and subsequently to disease