Spasticity is a known muscular tonus velocity dependent alteration which quantification in clinical practice is still based on subjective perception and scale grading through procedures that lack controlled protocols. In the research field, both physician’s and engineer’s researches have pointed the potentialities in the use of biomechanical magnitudes and their physiological meanings as much lesser subjective means of quantifying spasticity as well as its effects on patient daily life. Last, but not less important, this scientific and clinic urge is also justified by the high costs of treatments as well as the very tight relation they express between effectiveness and applied dose. As a consequence, this team of developers has been focused in creating a device to detect spasticity. During the validation of a first prototype with a small set of subjects, the obtained results were satisfyingly good as the device correctly detected 89% of the spastic subjects and 82% of the non-spastic subjects. Even so, the limitations found in the prototype concept itself led to a new development phase that resulted on a very different approach. SpastiMed, a motorized and electronically controlled device which is still on its validation phase but already showing an immense potential.

The formation of nurse cells in host muscle cells during Trichinella spiralis infection is a key step in the infective mechanism. Collagen trimerization is set up via disulphide bond formation, catalysed by protein disulphide isomerase (PDI). In T. spiralis, some PDI family members have been identified but no localization is described and no antibodies specific for T. spiralis PDIs are available. In this work, computational approaches were used to search for non-described PDIs in the T. spiralis genome database and to check the cross-reactivity of commercial anti-human antibodies with T. spiralis orthologues. In addition to a previously described PDI (PDIA2), endoplasmic reticulum protein (ERp57/PDIA3), ERp72/PDIA4, and the molecular chaperones calreticulin (CRT), calnexin (CNX) and immunoglobulin-binding protein/glucose-regulated protein (BIP/GRP78), we identified orthologues of the human thioredoxin-related-transmembrane proteins (TMX1, TMX2 and TMX3) in the genome protein database, as well as ERp44 (PDIA10) and endoplasmic reticulum disulphide reductase (ERdj5/PDIA19). Immunocytochemical staining of paraffin sections of muscle infected by T. spiralis enabled us to localize some orthologues of the human PDIs (PDIA3 and TMX1) and the chaperone GRP78. A theoretical three-dimensional model for T. spiralis PDIA3 was constructed. The localization and characteristics of the predicted linear B-cell epitopes and amino acid sequence of the immunogens used for commercial production of anti-human PDIA3 antibodies validated the use of these antibodies for the immunolocalization of T. spiralis PDIA3 orthologues. These results suggest that further study of the role of the PDIs and chaperones during nurse cell formation is desirable.