Empirical Evaluation of the Reliability of Photogrammetry Software in the Recovery of Three-Dimensional Footwear Impressions.

This paper examines the reliability of Structure from Motion (SfM) photogrammetry as a tool in the capture of forensic footwear marks. This is applicable to photogrammetry freeware DigTrace but is equally relevant to other SfM solutions. SfM simply requires a digital camera, a scale bar, and a selection of oblique photographs of the trace in question taken at the scene. The output is a digital three-dimensional point cloud of the surface and any plastic trace thereon. The first section of this paper examines the reliability of photogrammetry to capture the same data when repeatedly used on one impression, while the second part assesses the impact of varying cameras. Using cloud to cloud comparisons that measure the distance between two-point clouds, we assess the variability between models. The results highlight how little variability is evident and therefore speak to the accuracy and consistency of such techniques in the capture of three-dimensional traces. Using this method, 3D footwear impressions can, in many substrates, be collected with a repeatability of 97% with any variation between models less than ~0.5 mm

T-cell recognition of chemicals, protein allergens and drugs: towards the development of in vitro assays

Chemicals can elicit T-cell-mediated diseases such as allergic contact dermatitis and adverse drug reactions. Therefore, testing of chemicals, drugs and protein allergens for hazard identification and risk assessment is essential in regulatory toxicology. The seventh amendment of the EU Cosmetics Directive now prohibits the testing of cosmetic ingredients in mice, guinea pigs and other animal species to assess their sensitizing potential. In addition, the EU Chemicals Directive REACh requires the retesting of more than 30,000 chemicals for different toxicological endpoints, including sensitization, requiring vast numbers of animals. Therefore, alternative methods are urgently needed to eventually replace animal testing. Here, we summarize the outcome of an expert meeting in Rome on 7 November 2009 on the development of T-cell-based in vitro assays as tools in immunotoxicology to identify hazardous chemicals and drugs. In addition, we provide an overview of the development of the field over the last two decades

Components of the ligand for a Ni⁺⁺ reactive human T cell clone

The major histocompatibility complex (MHC) restriction element for a human Ni2+ reactive T cell, ANi-2.3, was identified as DR52c. A series of experiments established that the functional ligand for this T cell was a preformed complex of Ni2+ bound to the combination of DR52c and a specific peptide that was generated in human and mouse B cells, but not in fibroblasts nor other antigen processing-deficient cells. In addition, ANi-2.3 recognition of this complex was dependent on βHis81 of the MHC β chain, suggesting a role for this amino acid in Ni2+ binding to MHC. We propose a general model for Ni2+ recognition in which β His81 and two amino acids from the NH2-terminal part of the MHC bound peptide coordinate Ni2+ which then interacts with some portion of the Vα CDR1 or CDR2 region

A recombinant rubella virus E1 glycoprotein as a rubella vaccine candidate.

A recombinant rubella virus E1 (rE1) glycoprotein was produced and some of its chemical and immunological features were characterized. Two animal models were then used to establish that the rE1 glycoprotein and rubella virus particles shared antigenic and immunogenic properties. In the first one, sera from rE1 glycoprotein-immunized BALB/c mice neutralized in vitro rubella virus infection. In the second model, severe combined immune deficient (SCID) mice implanted with tonsil fragments from rubella immune donors and immunized with rE1 glycoprotein produced human anti-rubella virus antibodies. Altogether, these results showed that immunization with rE1 glycoprotein elicited neutralizing anti-rubella virus antibodies. This study thus indicated that the rE1 glycoprotein could constitute a non-replicating rubella vaccine