Przemysław Knysz
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Przemysław Knysz has a total of 15 co-authors. Here are the top co-authors by number of shared publications:
- Michał Gondek
Department of Food Hygiene of Animal Origin, Faculty of Veterinary Medicine, University of Life Sciences in Lublin, Akademicka 12, 20-033 Lublin, Poland
2 shared publications - Adam Lepczyński
Department of Physiology, Cytobiology and Proteomics, West Pomeranian University of Technology, Szczecin, Poland
1 shared publication - Agnieszka Herosimczyk
Department of Physiology, Cytobiology and Proteomics, Faculty of Biotechnology and Animal Husbandry, West Pomeranian University of Technology Szczecin, Klemensa Janickiego 29, 71-270 Szczecin, Poland
1 shared publication - Justyna Bień-Kalinowska
The Witold Stefański Institute of Parasitology, Polish Academy of Sciences, Twarda 51/55, 00-818 Warsaw, Poland
1 shared publication Krzysztof Szkucik
Uniwersytet Przyradniczy Lublinie, Wydzial Med Weterynaryjnej, Katedra Higieny Zywnosci Zwierzecego Pochodzenia, Ul Akad 12, PL-20033 Lublin, Poland
1 shared publication- Krzysztof Szkucik
Department of Food Hygiene of Animal Origin, Faculty of Veterinary Medicine, University of Life Sciences in Lublin, Akademicka 12, 20-950 Lublin, Poland
1 shared publication
Latest Publications
- Open Access
Insight into Trichinella britovi Infection in Pigs: Effect of Various Infectious Doses on Larvae Density and Spatial Larvae Distribution in Carcasses and Comparison of the Detection of Anti-T. britovi IgG of Three Different Commercial ELISA Tests and Immunoblot Assay
There is limited information available on the Trichinella britovi (T. britovi) muscle larvae (ML) distribution in pig muscle and the humoral immune response of pigs infected with moderate doses of this parasite; therefore, this study investigated the infectivity of a Polish strain of T. britovi for pigs, the antibody response of this host to various doses of T. britovi, and the efficiency of three different commercial ELISA kits and an immunoblot assay at detecting anti-T. britovi IgG. No significant differences in terms of the infection level of particular muscles or of whole carcasses between pigs infected with 3000 and those infected with 5000 ML of T. britovi were observed. The highest intensity of T. britovi infection was reported in the diaphragm pillars. The larvae of T. britovi showed homogeneous distribution with respect to the muscle side. Statistically, specific IgG antibodies against excretory–secretory (ES) antigens of Trichinella ML were first detected by all ELISA protocols on day 36 post infection; however, individual pig results showed some differences between the three tests applied. A significant increase in the level of anti-T. britovi IgG was observed between days 36 and 41 post infection, and from day 45 until day 62 after T. britovi infection, production of these antibodies reached its plateau phase. No positive correlation was found between the anti-T. britovi IgG level and the larvae density in 15 different muscles. Sera of T. britovi-infected pigs showed reactivity with T. britovi ML ES antigens of 62, 55, and 52 kDa. The results provide novel information on spatial larvae distribution in muscles and the humoral immune response of pigs exposed to two different doses of a Polish strain of T. britovi, extend knowledge on serological diagnostic tools which may be introduced in veterinary practice for the detection of T. britovi infections in pig production, and offer practical solutions for meat hygiene inspectors in the field at sampling sites when examining pig carcasses for Trichinella.
Open AccessInsight into Trichinella britovi Infection in Pigs: Effect of Various Infectious Doses on Larvae Density and Spatial Larvae Distribution in Carcasses and Comparison of the Detection of Anti-T. britovi IgG of Three Different Commercial ELISA Tests and Immunoblot Assay
There is limited information available on the Trichinella britovi (T. britovi) muscle larvae (ML) distribution in pig muscle and the humoral immune response of pigs infected with moderate doses of this parasite; therefore, this study investigated the infectivity of a Polish strain of T. britovi for pigs, the antibody response of this host to various doses of T. britovi, and the efficiency of three different commercial ELISA kits and an immunoblot assay at detecting anti-T. britovi IgG. No significant differences in terms of the infection level of particular muscles or of whole carcasses between pigs infected with 3000 and those infected with 5000 ML of T. britovi were observed. The highest intensity of T. britovi infection was reported in the diaphragm pillars. The larvae of T. britovi showed homogeneous distribution with respect to the muscle side. Statistically, specific IgG antibodies against excretory–secretory (ES) antigens of Trichinella ML were first detected by all ELISA protocols on day 36 post infection; however, individual pig results showed some differences between the three tests applied. A significant increase in the level of anti-T. britovi IgG was observed between days 36 and 41 post infection, and from day 45 until day 62 after T. britovi infection, production of these antibodies reached its plateau phase. No positive correlation was found between the anti-T. britovi IgG level and the larvae density in 15 different muscles. Sera of T. britovi-infected pigs showed reactivity with T. britovi ML ES antigens of 62, 55, and 52 kDa. The results provide novel information on spatial larvae distribution in muscles and the humoral immune response of pigs exposed to two different doses of a Polish strain of T. britovi, extend knowledge on serological diagnostic tools which may be introduced in veterinary practice for the detection of T. britovi infections in pig production, and offer practical solutions for meat hygiene inspectors in the field at sampling sites when examining pig carcasses for Trichinella.
- Open Access
Comparative Proteomic Analysis of Serum from Pigs Experimentally Infected with Trichinella spiralis, Trichinella britovi, and Trichinella pseudospiralis
Although the available proteomic studies have made it possible to identify and characterize Trichinella stage-specific proteins reacting with infected host-specific antibodies, the vast majority of these studies do not provide any information about changes in the global proteomic serum profile of Trichinella-infested individuals. In view of the above, the present study aimed to examine the protein expression profile of serum obtained at 13 and 60 days postinfection (d.p.i.) from three groups of pigs experimentally infected with Trichinella spiralis, Trichinella britovi, and Trichinella pseudospiralis and from uninfected, control pigs by two-dimensional gel electrophoresis (2-DE) followed by matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry. The comparative proteomic analysis of the T. spiralis group vs. the control group revealed 5 differently expressed spots at both 13 and 60 d.p.i. Experimental infection with T. britovi induced significant expression changes in 3 protein spots at 13 d.p.i. and in 6 protein spots at 60 d.p.i. in comparison with the control group. Paired analyses between the group infected with T. pseudospiralis and the uninfected control group revealed 6 differently changed spots at 13 d.p.i. and 2 differently changed spots at 60 d.p.i. Among these 27 spots, 15 were successfully identified. Depending on the Trichinella species triggering the infection and the time point of serum collection, they were IgM heavy-chain constant region, antithrombin III-precursor, immunoglobulin gamma-chain, clusterin, homeobox protein Mohawk, apolipoprotein E precursor, serum amyloid P-component precursor, Ig lambda chains, complement C3 isoform X1, and apolipoprotein A-I. Our results demonstrate that various Trichinella species and different phases of the invasion produce a distinct, characteristic proteomic pattern in the serum of experimentally infected pigs.
Open AccessComparative Proteomic Analysis of Serum from Pigs Experimentally Infected with Trichinella spiralis, Trichinella britovi, and Trichinella pseudospiralis
Although the available proteomic studies have made it possible to identify and characterize Trichinella stage-specific proteins reacting with infected host-specific antibodies, the vast majority of these studies do not provide any information about changes in the global proteomic serum profile of Trichinella-infested individuals. In view of the above, the present study aimed to examine the protein expression profile of serum obtained at 13 and 60 days postinfection (d.p.i.) from three groups of pigs experimentally infected with Trichinella spiralis, Trichinella britovi, and Trichinella pseudospiralis and from uninfected, control pigs by two-dimensional gel electrophoresis (2-DE) followed by matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry. The comparative proteomic analysis of the T. spiralis group vs. the control group revealed 5 differently expressed spots at both 13 and 60 d.p.i. Experimental infection with T. britovi induced significant expression changes in 3 protein spots at 13 d.p.i. and in 6 protein spots at 60 d.p.i. in comparison with the control group. Paired analyses between the group infected with T. pseudospiralis and the uninfected control group revealed 6 differently changed spots at 13 d.p.i. and 2 differently changed spots at 60 d.p.i. Among these 27 spots, 15 were successfully identified. Depending on the Trichinella species triggering the infection and the time point of serum collection, they were IgM heavy-chain constant region, antithrombin III-precursor, immunoglobulin gamma-chain, clusterin, homeobox protein Mohawk, apolipoprotein E precursor, serum amyloid P-component precursor, Ig lambda chains, complement C3 isoform X1, and apolipoprotein A-I. Our results demonstrate that various Trichinella species and different phases of the invasion produce a distinct, characteristic proteomic pattern in the serum of experimentally infected pigs.
- 1 January 2018
- Published by Medycyna Weterynaryjna - Redakcja in Medycyna Weterynaryjna
- Vol. 74 (10) , 5971-2018
Chemical composition and nutritional quality of short-ripened rennet cheeses produced by traditional methods
- 1 January 2018
- Published by Medycyna Weterynaryjna - Redakcja in Medycyna Weterynaryjna
- Vol. 74 (10) , 5971-2018
Chemical composition and nutritional quality of short-ripened rennet cheeses produced by traditional methods