A dual controllability analysis of influenza virus-host protein-protein interaction networks for antiviral drug target discovery

Ackerman, Emily E.; Alcorn, John F.; Hase, Takeshi; Shoemaker, Jason E.

While none of the proteins change robust classification between networks, the aforementioned replacement of 11 host driver proteins with viral proteins after the addition of virus interactions creates a small change in robust type distribution for driver proteins. Of the displaced host proteins (deemed "robust proteins", found in Table 1 ), seven are neutral and four are dispensable in the HIN, meaning that their removal from the network does not change the number of driver proteins and reduces the number of driver proteins needed, respectively. All IAV proteins are classified as dispensable in the VIN. Of the five robust proteins that are both driver and IAV interacting proteins, four are neutral and one is dispensable. The most notable change in degree and betweenness between the HIN and VIN is PRMT5, with an increase of 9 and 2250, respectively. Overall, robust controllability results suggest that the HIN is stable against potential changes in the control structure that could be caused by the addition of IAV interactions.