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2 Archivum Immunologiae et Therapiae Experimentalis

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Advanced glycation end-products prepared in solution under high pressure contain epitopes distinct from those formed in the dry reaction at high temperature

100%

Staniszewska M. , Jarosz J. , Jon M. , Gamian A.

tom 53

nr 1

71-78

Advanced glycation end-products play an important role in diseases related to diabetes and aging processes. Model compounds are synthesized in order to prepare the diagnostic and experimental tools for studying the mechanisms of pathogenesis. The objective of the present study was to accelerate glycation and upgrade its efficiency under high-pressure conditions.Aqueous solutions of proteins were kept with carbohydrates under a pressure of up to 850 MPa for several hours. Then the high-pressure glycation (HPG) products were fractionated on a Sephadex G-200 column and characterized with SDS-PAGE and MALDI-TOF mass spectrometry. The low-molecular-mass fraction of glycated proteins was separated from the two fractions containing high- and intermediate-molecular-mass cross-linked products of glycation. The products were then compared with those obtained with the high-temperature glycation (HTG) procedure carried out in dry conditions with a lyophilized mixture of substrates. The fractionated products were used to prepare rabbit sera. The immunoblotting experiments showed that the epitopes on the cross-linked glycation products formed in solution under high pressure differed from those originating in dry conditions at high temperature. Sera against the HPG products were specific to homologous material and did not interact with the fractions obtained by HTG. The antibodies against HTG products recognized HTG but not HPG products.

Serological classification and epitope specificity of Proteus vulgaris TG 251 from Proteus serogroup O65

88%

Zych K. , Kolodziejska K. , Drzewiecka D. , Perepelov A. V. , Knirel Y. A. , Sidorczyk Z.

nr 3

187-191

Introduction: Proteus rods are currently subdivided into five named species, i.e. Proteus mirabilis, P. vulgaris, P. penneri, P. hauseri, and P. myxofaciens, and three unnamed Proteus genomospecies 4 to 6. Based on the serospecificity of the lipopolysaccharide (LPS; O-antigen), strains of P. mirabilis and P. vulgaris were divided into 49 O-serogroups and 11 additional O-serogroups were proposed later. About 15 further O-serogroups have been proposed for the third medically important species, P. penneri. Here the serological classification of P. vulgaris strain TG 251, which does not belong to these serogroups, is reported. Serological investigations also allowed characterization of the epitope specificity of its LPS. Materials and Methods: Purified LPSs from five Proteus strains were used as antigens in enzyme immunosorbent assay (EIA), SDS/PAGE, and Western blot and alkali-treated LPSs in the passive immunohemolysis (PIH) test, inhibition of PIH and EIA, and absorption of the rabbit polyclonal O-antisera with the respective LPS. Results: The serological studies of P. vulgaris TG 251 LPS indicated the identity of its O-polysaccharide with that of P. penneri O65. The antibody specificities of P. vulgaris TG 251 and P. penneri O65 O-antisera, were described. Conclusions: P. vulgaris TG 251 was classified to the Proteus O65 serogroup. Two disaccharide-associated epitopes present in P. vulgaris TG 251 and P. penneri O65 LPSs are suggested to be responsible for cross-reactions with three heterologous Proteus strains.