Aims:  The focus of this study was to evaluate the potential use of the predatory bacteria Bdellovibrio bacteriovorus and Micavibrio aeruginosavorus to control the pathogens associated with human infection. Methods and Results:  By coculturing B. bacteriovorus 109J and M. aeruginosavorus ARL‐13 with selected pathogens, we have demonstrated that predatory bacteria are able to attack bacteria from the genus Acinetobacter, Aeromonas, Bordetella, Burkholderia, Citrobacter, Enterobacter, Escherichia, Klebsiella, Listonella, Morganella, Proteus, Pseudomonas, Salmonella, Serratia, Shigella, Vibrio and Yersinia. Predation was measured in single and multispecies microbial cultures as well as on monolayer and multilayer preformed biofilms. Additional experiments aimed at assessing the optimal predation characteristics of M. aeruginosavorus demonstrated that the predator is able to prey at temperatures of 25–37°C but is unable to prey under oxygen‐limiting conditions. In addition, an increase in M. aeruginosavorus ARL‐13 prey range was also observed. Conclusions:  Bdellovibrio bacteriovorus and M. aeruginosavorus have an ability to prey and reduce many of the multidrug‐resistant pathogens associated with human infection. Significance and Impact of the Study:  Infectious complications caused by micro‐organisms that have become resistant to drug therapy are an increasing problem in medicine, with more infections becoming difficult to treat using traditional antimicrobial agents. The work presented here highlights the potential use of predatory bacteria as a biological‐based agent for eradicating multidrug‐resistant bacteria, with the hope of paving the way for future studies in animal models.

Large-gap peripheral nerve injuries present a significant challenge for nerve regeneration due to lack of suitable grafts, insufficient cell penetration, and repair. Biomimetic nanofibrous scaffolds, functionalized on the surface with extracellular matrix proteins, can lead to novel therapies for repair and regeneration of damaged peripheral nerves. Here, nanofibrous scaffolds electrospun from blends of poly(caprolactone) (PCL) and chitosan were fabricated. Taking advantage of the amine groups on the chitosan, the surface of the scaffolds were functionalized with laminin by carbodiimide based crosslinking. Crosslinking allowed laminin to be attached to the surfaces of the PCL-chitosan nanofibers at relatively high concentrations that were not possible using conventional adsorption methods. The nanofibrous meshes were tested for wettability, mechanical properties and cell attachment and proliferation. Blending of chitosan with PCL provided more favorable surfaces for attachment of Schwann cells due to the reduction of the contact angle in comparison to neat PCL. Proliferation rates of Schwann cells grown on PCL-chitosan scaffolds with crosslinked laminin were significantly higher than the rates for PCL-chitosan nanofibrous matrices with adsorbed laminin. PCL-chitosan scaffolds with modified surfaces via crosslinking of laminin could potentially serves as versatile substrates with excellent mechanical and surface properties for in vivo cell delivery for nerve tissue engineering applications.

Receptor protein-tyrosine phosphatase RPTPσ has important functions in modulating neural development and regeneration. Compelling evidence suggests that both heparan sulfate (HS) and chondroitin sulfate (CS) glycosaminoglycans (GAGs) bind to a series of Lys residues located in the first Ig domain of RPTPσ. However, HS promotes and CS inhibits axonal growth. Mutation of these Lys residues abolished binding and signal transduction of RPTPσ to CS, whereas HS binding was reduced, and signaling persisted. This activity was mediated through novel heparin-binding sites identified in the juxtamembrane region. Although different functional outcomes of HS and CS have been previously attributed to the differential oligomeric state of RPTPσ upon GAG binding, we found that RPTPσ was clustered by both heparin and CS GAG rich in 4,6--disulfated disaccharide units. We propose an additional mechanism by which RPTPσ distinguishes between HS and CS through these novel binding sites.

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