Development of two murine antibodies against Neospora caninum using phage display technology and application on the detection of N. caninum.
Neosporosis, caused by an intracellular parasite, Neospora caninum, is an infectious disease primarily of cattle and dogs. It occurs worldwide and causes huge damages to dairy farms. In this study, we immunized mice with recombinant surface-associated protein 1 of N. caninum (rNcSAG1) and developed...
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doaj-46cf78438c764f91a4f8d3643cc089042020-11-24T22:06:47ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0181e5326410.1371/journal.pone.0053264Development of two murine antibodies against Neospora caninum using phage display technology and application on the detection of N. caninum.Jinhua DongTakahiro OtsukiTatsuya KatoTetsuya KohsakaKazunori IkeEnoch Y ParkNeosporosis, caused by an intracellular parasite, Neospora caninum, is an infectious disease primarily of cattle and dogs. It occurs worldwide and causes huge damages to dairy farms. In this study, we immunized mice with recombinant surface-associated protein 1 of N. caninum (rNcSAG1) and developed two novel monoclonal antibodies, A10 and H3, against NcSAG1 using phage-display technology. Both clones bound to purified rNcSAG1 and the half maximal inhibitory concentrations of A10 and H3 are 50 and 72 nM of rNcSAG1, respectively. In immunofluorescence assays, both A10 and H3 Fabs bound to N. caninum parasites. Direct detection of N. caninum parasites was developed firstly using an enzyme-linked immunosorbent assay (ELISA) with A10 and H3. Binding of A10 and H3 antibodies to rNcSAG1 was also inhibited by some certain anti-N. caninum antibodies in the neosporosis-positive cattle sera, suggesting they might bind to the same epitopes of NcSAG1 with those anti-N. caninum antibodies of bovine. These antibodies were demonstrated to have a potential for monitoring the N. caninum parasites in a dairy farm, which may lead to protect livestock from parasite-infection.http://europepmc.org/articles/PMC3540087?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Jinhua Dong Takahiro Otsuki Tatsuya Kato Tetsuya Kohsaka Kazunori Ike Enoch Y Park |
spellingShingle |
Jinhua Dong Takahiro Otsuki Tatsuya Kato Tetsuya Kohsaka Kazunori Ike Enoch Y Park Development of two murine antibodies against Neospora caninum using phage display technology and application on the detection of N. caninum. PLoS ONE |
author_facet |
Jinhua Dong Takahiro Otsuki Tatsuya Kato Tetsuya Kohsaka Kazunori Ike Enoch Y Park |
author_sort |
Jinhua Dong |
title |
Development of two murine antibodies against Neospora caninum using phage display technology and application on the detection of N. caninum. |
title_short |
Development of two murine antibodies against Neospora caninum using phage display technology and application on the detection of N. caninum. |
title_full |
Development of two murine antibodies against Neospora caninum using phage display technology and application on the detection of N. caninum. |
title_fullStr |
Development of two murine antibodies against Neospora caninum using phage display technology and application on the detection of N. caninum. |
title_full_unstemmed |
Development of two murine antibodies against Neospora caninum using phage display technology and application on the detection of N. caninum. |
title_sort |
development of two murine antibodies against neospora caninum using phage display technology and application on the detection of n. caninum. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2013-01-01 |
description |
Neosporosis, caused by an intracellular parasite, Neospora caninum, is an infectious disease primarily of cattle and dogs. It occurs worldwide and causes huge damages to dairy farms. In this study, we immunized mice with recombinant surface-associated protein 1 of N. caninum (rNcSAG1) and developed two novel monoclonal antibodies, A10 and H3, against NcSAG1 using phage-display technology. Both clones bound to purified rNcSAG1 and the half maximal inhibitory concentrations of A10 and H3 are 50 and 72 nM of rNcSAG1, respectively. In immunofluorescence assays, both A10 and H3 Fabs bound to N. caninum parasites. Direct detection of N. caninum parasites was developed firstly using an enzyme-linked immunosorbent assay (ELISA) with A10 and H3. Binding of A10 and H3 antibodies to rNcSAG1 was also inhibited by some certain anti-N. caninum antibodies in the neosporosis-positive cattle sera, suggesting they might bind to the same epitopes of NcSAG1 with those anti-N. caninum antibodies of bovine. These antibodies were demonstrated to have a potential for monitoring the N. caninum parasites in a dairy farm, which may lead to protect livestock from parasite-infection. |
url |
http://europepmc.org/articles/PMC3540087?pdf=render |
work_keys_str_mv |
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