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ARS Home » Northeast Area » Beltsville, Maryland (BARC) » Beltsville Agricultural Research Center » Animal Biosciences & Biotechnology Laboratory » Research » Publications at this Location » Publication #330546
Title: Identification of Eimeria acervulina conoid antigen using chicken monoclonal antibody and liquid chromatography coupled to mass spectrometry

Author
item MATSUBAYASHI, MAKOTO - Osaka Prefecture University
item MINOURA, CHISA - Osaka Prefecture University
item SHINTAURO, KIMURA - Osaka Prefecture University
item HIROYUKI, TANI - Osaka Prefecture University
item MASARU, FURUYA - Osaka Prefecture University
item HARUO, MATSUDA - Osaka Prefecture University
item HIROSHI, NAKAGAWA - Osaka Prefecture University
item Lillehoj, Hyun
item HATTA, TAKESHI - Kitasato University
item TSUJI, NAOTOSHI - Kitasato University
item SASAI, KAZUMI - Osaka Prefecture University

Submitted to: Parasitology Research
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 6/2/2016
Publication Date: 11/2/2016
Publication URL: http://handle.nal.usda.gov/10113/5559577
Citation: Matsubayashi, M., Minoura, C., Shintauro, K., Hiroyuki, T., Masaru, F., Haruo, M., Hiroshi, N., Lillehoj, H.S., Hatta, T., Tsuji, N., Sasai, K. 2016. Identification of Eimeria acervulina conoid antigen using chicken monoclonal antibody and liquid chromatography coupled to mass spectrometry. Parasitology Research. 115(11):4123-4128.

Interpretive Summary: For the poultry industry, the disease called coccidiosis in chickens is important because it causes significant economic losses to producers when their flocks become sick. Researchers in Japan and the ARS in Beltsville, MD previously have generated a unique biological tool in the form of an antibody made in chickens that recognizes a key protein specific to the capability of the coccidiosis microbe called Eimeria acervulina to infect the cells of the chicken intestine. In the prior studies the antibody was added to cultures of chicken immune cells and to these cells was then added the parasite, the presence of the antibody in the culture significantly inhibited the invasion of host cells. To date, however, the exact molecule in Eimeria acervulina that is bound by this antibody allowing it to prevent infection remained unknown. For the work presented in this paper, we solved this question. Using molecule analysis, we found two proteins one of which was determined to be elongation factor-1 (EF-1), a molecule necessary in cells to make proteins, an EF-1-related protein. Our results suggested that EF-1a could be associated with the ability of the disease to take hold in the process of infection and may serve as a useful target towards development of strategies to limit the health and economic of this costly disease in chickens.

Technical Abstract: Protozoan parasites of the phylum Apicomplexa include a large number of medically important species. Among them, Toxoplasma gondii, Plasmodium, Cryptosporidium that cause watery diarrhea and mortality in humans and livestock, and Eimeria which induces gastrointestinal disorder in livestock and poultry. In the poultry industry, Eimeria has been recognized as the most significant economically important protozoan parasite owing to its worldwide prevalence and severity of gut damage. In this report, ARS scientist collaborated with university scientists in Osaka, Japan to identify target vaccine molecules of Eimeria as an alternative to antibiotics for coccidiosis control. In previous studies, ARS developed a chicken mAb designated 6D-12-G10 which significantly inhibited the invasion of sporozoites in vitro and recognized the target as the conoid of the sporozoites Moreover, 6D-12-G10 appears to show high cross-reactivity with related parasites, including six other apicomplexan parasites, Eimeria spp., Neospora caninum, Toxoplasma gondii, and Cryptosporidium spp. Further analyses in C. parvum revealed that the protein recognized by 6D-12-G10 is involved with the host cell invasion. Our current study identified a protein at the cytoskeleton protein located at the apical region of zoites and the elucidation of the role of this protein in future may facilitate the development of recombinant vaccine.