Table 4 shows that these interaction modules were associated with biological processes related to ligase activity, ubiquitination, protein modification, transcription and translation, immune response, signaling, cytoskeleton organization, development, and mRNA processing.

Table 2 shows that these virulence factors interacted with a statistically significant number of human proteins that were associated with 1) protein ubiquitination and ubiquitin ligase activity, 2) vesicle organization, and 3) protein complexes located in the cytoskeleton , in lysosomes, and in the nuclear lumen.

These results were consistent with the experimentally observed pathogen interference with host cytoskeleton organization and ubiquitination levels [2, 3, 19—21, 24].

One of the most prominently recurring results across all of our analyses was the link between B. mallei pathogenicity and host cytoskeleton organization.

It has been shown that a number of bacterial pathogens, including Yersinia, Salmonella, Shigella, Listeria, and Barkholderia, interfere with host signaling pathways to stimulate the host’s cytoskeleton rearrangement [2, 33].

4 shows host proteins that interacted with known and putative B. mallei Virulence factors that can be directly associated with cytoskeleton organization.

In addition, the analysis revealed specific host processes relevant to B. mallei virulence factors’ pathogenicity, e.g., signaling and communication, protein modification and regulation, and cytoskeleton organization, and suggested that virulence factors preferentially targeted multifunctional host proteins, thereby affecting multiple host cellular processes simultaneously.

The majority of these molecular interactions belonged to a connected sub-pathway located at the beginning of the pathway (the probability of observing such connectivity at random is < 106), and they provided a link between membrane receptors and signaling events that led to reorganization of the actin cytoskeleton .

We introduce a new type of traction force microscopy that in contrast to traditional methods uses additional image data for cytoskeleton and adhesion structures and a biophysical model to improve the robustness of the inverse procedure and abolishes the need for regularization.

If accomplished, however, such studies then will yield new mechanical insight into the mechanisms of global force transmission and sensing in the actin cytoskeleton of adherent cells.

This model represents several typical mechanical properties of the actin cytoskeleton .

Actin cytoskeleton and traction force microscopy.