A Survey on Mobile Anchor Node Assisted Localization in Wireless Sensor Networks

Localization is one of the key technologies in Wireless Sensor Networks (WSNs), since it provides fundamental support for many location-aware protocols and applications. Constraints on cost and power consumption make it infeasible to equip each sensor node in the network with a Global Position System (GPS) unit, especially for large-scale WSNs. A promising method to localize unknown nodes is to use mobile anchor nodes (MANs), which are equipped with GPS units moving among unknown nodes and periodically broadcasting their current locations to help nearby unknown nodes with localization. A considerable body of research has addressed the Mobile Anchor Node Assisted Localization (MANAL) problem. However to the best of our knowledge, no updated surveys on MAAL reflecting recent advances in the field have been presented in the past few years. This survey presents a review of the most successful MANAL algorithms, focusing on the achievements made in the past decade, and aims to become a starting point for researchers who are initiating their endeavors in MANAL research field. In addition, we seek to present a comprehensive review of the recent breakthroughs in the field, providing links to the most interesting and successful advances in this research field.

LtpD is a novel legionella pneumophila effector that binds phosphatidylinositol 3-phosphate and inositol monophosphatase IMPA1

The Dot/Icm type IV secretion system (T4SS) of Legionella pneumophila is crucial for the pathogen to survive in protozoa and cause human disease. Although more than 275 effector proteins are delivered into the host cell by the T4SS, the function of the majority is unknown. Here we have characterized the Dot/Icm effector LtpD. During infection, LtpD localized to the cytoplasmic face of the membrane of the Legionella-containing vacuole (LCV). In A549 lung epithelial cells, ectopically expressed LtpD localized to large vesicular structures that contained markers of endosomal compartments. Systematic analysis of LtpD fragments identified an internal 17-kDa fragment, LtpD_471-626, which was essential for targeting ectopically expressed LtpD to vesicular structures and for the association of translocated LtpD with the LCV. LtpD_471-626 bound directly to phosphatidylinositol 3-phosphate [PtdIns(3)P] in vitro and colocalized with the PtdIns(3)P markers FYVE and SetA in cotransfected cells. LtpD was also found to bind the host cell enzyme inositol (myo)-1 (or 4)-monophosphatase 1, an important phosphatase involved in phosphoinositide production. Analysis of the role of LtpD in infection showed that LtpD is involved in bacterial replication in THP-1 macrophages, the larvae of Galleria mellonella, and mouse lungs. Together, these data suggest that LtpD is a novel phosphoinositide- binding L. pneumophila effector that has a role in intracellular bacterial replication. © 2013, American Society for Microbiology.