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This article presents an accurate analytical model (AM) for synchronous reluctance machine (SynRM) that incorporates the effect of stator slots on the air gap flux density and torque waveforms. From the formulation of magnetic potential in the air gap for both the stator and rotor, the flux density is obtained, considering the first harmonic of the flux density and the electric loading, the average torque is calculated using the Lorentz’s force. The ripple torque is obtained from the energy stored in magnetic circuit. The method is developed for a rotor with one flux barrier per pole and then extended to a larger number of barriers. To validate the results obtained by the AM proposed finite element analysis have been carried out. Several comparisons have been derived considering different rotor positions as well as different harmonic orders, and the pros and cons of the method are highlighted. The model performs fast and can predict results with high accuracy, and can be adopted to speed up the preliminary design and optimizations of this type of motors, with respect to finite element. In addition, from the analytical expressions it is possible to obtain all the correlations between electrical, magnetic, and geometrical characteristics of the machine, with the advantage of enabling a faster machine design. [ABSTRACT FROM AUTHOR]

The role of second messengers in the diversion of cellular processes by pathogens remains poorly studied despite their importance. Among these, Ca2+ virtually regulates all known cell processes, including cytoskeletal reorganization, inflammation, or cell death pathways. Under physiological conditions, cytosolic Ca2+ increases are transient and oscillatory, defining the so-called Ca2+ code that links cell responses to specific Ca2+ oscillatory patterns. During cell invasion, Shigella induces atypical local and global Ca2+ signals. Here, we show that by hydrolyzing phosphatidylinositol-(4,5)bisphosphate, the Shigella type III effector IpgD dampens inositol-(1,4,5)trisphosphate (InsP3) levels. By modifying InsP3 dynamics and diffusion, IpgD favors the elicitation of long-lasting local Ca2+ signals at Shigella invasion sites and converts Shigella-induced global oscillatory responses into erratic responses with atypical dynamics and amplitude. Furthermore, IpgD eventually inhibits InsP3-dependent responses during prolonged infection kinetics. IpgD thus acts as a pathogen regulator of the Ca2+ code implicated in a versatility of cell functions. Consistent with this function, IpgD prevents the Ca2+-dependent activation of calpain, thereby preserving the integrity of cell adhesion structures during the early stages of infection. [ABSTRACT FROM AUTHOR]

The actin cytoskeleton is key to the barrier function of epithelial cells, by permitting the establishment and maintenance of cell-cell junctions and cell adhesion to the basal matrix. Actin exists under monomeric and polymerized filamentous form and its polymerization following activation of nucleation promoting factors generates pushing forces, required to propel intracellular microorganisms in the host cell cytosol or for the formation of cell extensions that engulf bacteria. Actin filaments can associate with adhesion receptors at the plasma membrane via cytoskeletal linkers. Membrane anchored to actin filaments are then subjected to the retrograde flow that may pull membrane-bound bacteria inside the cell. To induce its internalization by normally non-phagocytic cells, bacteria need to establish adhesive contacts and trick the cell into apply pulling forces, and/or to generate protrusive forces that deform the membrane surrounding its contact site. In this review, we will focus on recent findings on actin cytoskeleton reorganization within epithelial cells during invasion and cell-to-cell spreading by the enteroinvasive pathogen S higella, the causative agent of bacillary dysentery. [ABSTRACT FROM AUTHOR]

The Shigella type III effector IpaA contains three binding sites for the focal adhesion protein vinculin (VBSs), which are involved in bacterial invasion of host cells. Here, we report that IpaA VBS3 unexpectedly binds to talin. The 2.5 Å resolution crystal structure of IpaA VBS3 in complex with the talin H1-H4 helices shows a tightly folded α-helical bundle, which is in contrast to the bundle unraveling upon vinculin interaction. High-affinity binding to talin H1-H4 requires a core of hydrophobic residues and electrostatic interactions conserved in talin VBS H46. Remarkably, IpaA VBS3 localizes to filopodial distal adhesions enriched in talin, but not vinculin. In addition, IpaA VBS3 binding to talin was required for filopodial adhesions and efficient capture of Shigella. These results point to the functional diversity of VBSs and support a specific role for talin binding by a subset of VBSs in the formation of filopodial adhesions., (Copyright © 2018 The Author(s). Published by Elsevier Inc. All rights reserved.)

The role of second messengers in the diversion of cellular processes by pathogens remains poorly studied despite their importance. Among these, Ca 2+ virtually regulates all known cell processes, including cytoskeletal reorganization, inflammation, or cell death pathways. Under physiological conditions, cytosolic Ca 2+ increases are transient and oscillatory, defining the so-called Ca 2+ code that links cell responses to specific Ca 2+ oscillatory patterns. During cell invasion, Shigella induces atypical local and global Ca 2+ signals. Here, we show that by hydrolyzing phosphatidylinositol-(4,5)bisphosphate, the Shigella type III effector IpgD dampens inositol-(1,4,5)trisphosphate (InsP 3 ) levels. By modifying InsP 3 dynamics and diffusion, IpgD favors the elicitation of long-lasting local Ca 2+ signals at Shigella invasion sites and converts Shigella -induced global oscillatory responses into erratic responses with atypical dynamics and amplitude. Furthermore, IpgD eventually inhibits InsP 3 -dependent responses during prolonged infection kinetics. IpgD thus acts as a pathogen regulator of the Ca 2+ code implicated in a versatility of cell functions. Consistent with this function, IpgD prevents the Ca 2+ -dependent activation of calpain, thereby preserving the integrity of cell adhesion structures during the early stages of infection., (© 2017 The Authors.)

Internalization of Shigella into host epithelial cells, where the bacteria replicates and spreads to neighboring cells, requires a type 3 secretion system (T3SS) effector coined IpaA. IpaA binds directly to and activates the cytoskeletal protein vinculin after injection in the host cell cytosol, and this was previously thought to be directed by two amphipathic α-helical vinculin-binding sites (VBS) found in the C-terminal tail domain of IpaA. Here, we report a third VBS, IpaA-VBS3, that is located N-terminal to the other two VBSs of IpaA and show that one IpaA molecule can bind up to three vinculin molecules. Biochemical in vitro Shigella invasion assays and the 1.6 Å crystal structure of the vinculin·IpaA-VBS3 complex showed that IpaA-VBS3 is functionally redundant with the other two IpaA-VBSs in cell invasion and in activating the latent F-actin binding functions of vinculin. Multiple VBSs in IpaA are reminiscent of talin, which harbors 11 VBSs. However, most of the talin VBSs have low affinity and are buried in helix bundles, whereas all three of the VBSs of IpaA are high affinity, readily available, and in close proximity to each other in the IpaA structure. Although deletion of IpaA-VBS3 has no detectable effects on Shigella invasion of epithelial cells, deletion of all three VBSs impaired bacterial invasion to levels found in an ipaA null mutant strain. Thus, IpaA-directed mimicry of talin in activating vinculin occurs through three high affinity VBSs that are essential for Shigella pathogenesis.