Cross-reactivity characterization

Beineke, A. et al., Immunohistochemical investigation of the cross-reactivity of selected cell markers from various species for characterization of lymphatic tissues in the harbour porpoise (Phocoena phocoena), J. Comp. Pathol., 125, 311, 2001. 

Asturias, J. A., Gomez-Bayon, N., AriUa, M. C., Martinez, A., Palacios, R., Sanchez-Gascon, F., and Martinez, J. (1999). Molecular characterization of American cockroach tropomyosin (Periplaneta americana allergen 7), a cross-reactive aUergen. /. Immunol. 162, 4342 348. 

Binder, M. Mahler, V. Hayek, B. Sperr, W.R. Scholler, M. Prozell, S. Wie-dermann, G. Valent, P. Valenta, R. Duchene, M. Molecular and immunological characterization of arginine kinase from the Indianmeal moth, Plo-dia interpunctella, a novel cross-reactive invertebrate pan-allergen. J. Immunol., 167, 5470-5477 (2001)... 

Avenacinase, an enzyme from G. graminis var. avenae, is related to tomatinase from S. lycopersici because is able to deglucosilate tomatine by identical mode of action. However, the activity is very low and corresponds to approximately 2% of its activity towards avenacin A-1 [32]. Tomatinase form S. lycopersici, also can cleave avenacin A-l but has less than 0.01% of activity towards it in comparison to its activity towards tomatine [32]. Therefore, the two enzymes are highly specific for their respective host plant saponins. Purification and characterization of S. lycopersici tomatinase revealed that this enzyme shares many properties (including immunological cross-reactivity) with avenacinase... 

HSP27 and Tau protein, respectively. 2D immunoblotting combined with mass spectrometry-based identification methods has been widely applied to the characterization of 2D electrophoretic cross-reactive isoforms of the same protein, e.g., resulting from alternative splicing, co- and/or posttranslational modifications and proteolytic cleavages (15-19). 

Turiel, E., C. Perez-Conde, and A. Martin-Esteban (2003). Assessment of the cross-reactivity and binding sites characterization of a pro-pazine-imprinted polymer using the Langmiur-Freundlich isotherm. Analyst, 128 137-141. 

Inghirami, G., Foitl, D. R., Sabichi, A., Zhu, B. Y., and Knowles, D. M., Autoantibody-associated cross-reactive idiotype-bearing human B lymphocytes Distribution and characterization, including Ig VH gene and CD5 antigen expression. Blood 78,1503-1515 (1991). 

Bohle, B., Radakovics, A., Luttkopf, D., Jahn-Schmid, B., Vieths, S., and Ebner, C. 2005. Characterization of the T cell response to the major hazelnut allergen, Cor a 1.04 Evidence for a relevant T cell epitope not cross-reactive with homologous pollen allergens. Clin Exp Allergy 35(10) 1392-1399. 

In the tissue cross-reactivity studies, the antibody has equal access to all tissues and all cell components (membrane, cytosol, nucleus) of the tissues on the section. This is not true in vivo where access to the tissues is governed by passive diffusion of the antibody to the tissue. Moreover, unless uptake by tissues is receptor-mediated, cell membranes preclude entrance of an antibody into the cells. In addition there are blood-brain, blood-nerve, blood-eye, and blood-testis barriers characterized by specialized endothelium that reduce movement of immunoglobulin into these protected spaces. Thus, some tissues have relatively little access by antibodies compared to others. Likewise, antigens within cells have little chance of access to the antibody compared to cell membrane or transmembrane antigens. 

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