Clostridium perfringens-induced host-pathogen transcriptional changes in the small intestine of broiler chickens

Authors: QU, GUANGGANG - Shandong Binzhou Academy Of Animal Science And Veterinary Medicine; XU, ZHIYANG - Nanjing University; Tuo, Wenbin; Li, Charles; WAN, GEN - Jiangxi Agricultural University; Lillehoj, Hyun; GONG, HAIWEI - Jiangxi Agricultural University; HUANG, JINXIN - Jiangxi Agricultural University; TIAN, GUICHUAN - Jiangxi Agricultural University; LI, SHANXIN - Jiangxi Agricultural University; LIU, YUXIN - Jiangxi Agricultural University; LIU, LIHENG - Jiangxi Agricultural University

Submitted to: Frontiers in Veterinary Science
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 12/23/2021
Publication Date: 12/25/2021
Citation: Qu, G., Xu, Z., Tuo, W., Li, C.Z., Wan, G., Lillehoj, H.S., Gong, H., Huang, J., Tian, G., Li, S., Liu, Y., Liu, L. 2021. Clostridium perfringens-induced host-pathogen transcriptional changes in the small intestine of broiler chickens. Frontiers in Veterinary Science. https://doi.org/10.1016/j.vetpar.2021.109642.
DOI: https://doi.org/10.1016/j.vetpar.2021.109642

Interpretive Summary: A protozoa parasite called Eimeria necatrix causes intestinal coccidiosis that can reduce growth performance of poultry and result in high mortality in older chickens. The components of the growth or sporozoite stage of this parasite that cause immune responses in chickens remains unclear. In this study, the whole sporozoite proteins of E. necatrix were analyzed by two-dimensional electrophoresis (2-DE) and Western blotting using hyperimmune chicken serum containing E. necatrix-specific antibodies. Approximately 680 E. necatrix sporozoite proteins were detected and 98 of these proteins were recognized by E. necatrix-specific antibodies. Fifty-six proteins were further evaluated by mass spectrometry. Of those 56 samples, 50 proteins were identified, including proteins of nuclear location and function; multifunctional- or multifunctional motifs-containing proteins; cellular transport and structure-related proteins; and proteins of known or predicted enzymatic activities. There are two proteins which may be involved in mediating parasite interactions with the host immune system and two organelle-related proteins. There is one hypothetical protein with no apparent functions and one heat-shock-related protein. Three motor-related proteins were also detected as immunogenic proteins. Our study has identified nine groups of antigens which were never characterized previously. These new findings will enhance our understanding of parasite immunogenicity and immune evasion mechanisms of E. necatrix, and facilitate the discovery phase of highly effective candidate vaccines.

Technical Abstract: Eimeria necatrix, an apicomplexan protozoa of the genus Eimeria, causes intestinal coccidiosis that can reduces growth performance of poultry and high mortality in older chickens. In this study, the whole sporozoite proteins of E. necatrix were analyzed by two-dimensional electrophoresis (2-DE) and Western blotting using hyperimmune chicken serum containing E. necatrix-specific antibodies. Approximately 680 E. necatrix sporozoite protein spots were detected by 2-DE with silver staining, among which 98 protein spots were recognized by E. necatrix-specific immune sera. Out of fifty-six spots that were selected for MALDI-TOF-MS/MS analysis, 50 proteins were identified using the “MASCOT” server including proteins of nuclear location & function, multifunctional- or multifunctional motifs-containing proteins, cellular transport and structure-related proteins and proteins of known or predicted enzymatic activities. There are 2 SAG family proteins which may be involved in mediating parasite interactions with the host immune system and 2 organelle-related proteins. There is one hypothetical protein with no apparent functions and one heat-shock-related protein. Three motor related proteins were also detected as immunogenic proteins. Our study has identified 9 groups of antigens which were never characterized previously except 8 out of 56 spots identified as known proteins of E. necatrix. These new findings will enhance our understanding of parasite immunogenicity and immune evasion mechanisms of E. necatrix, and facilitate the discovery phase of highly effective candidate vaccines.