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Cloning, monoclonal antibody production, and bodily distribution pattern of a bovine lipocalin
Tamar Japaridze1, Akitsugu Senda, Hirofumi Nozaki
1Department of Animal and Food Hygiene, Obihiro University of Agriculture and Veterinary Medicine, Obihiro, Hokkaido, Japan.
Insights
Bovine lipocalin (bcOBP) is secreted in milk and other bodily fluids, suggesting a role as a pheromone carrier in cattle. This protein, found in various farm animals, may facilitate communication through scent.
Area of Science:
- Biochemistry
- Animal Science
- Molecular Biology
Background:
- A bovine lipocalin, identified as a putative odorant-binding protein in bovine colostrum (bcOBP), was investigated.
- Previous research suggested bcOBP's role in olfaction.
Purpose of the Study:
- To clone and express bcOBP.
- To develop a monoclonal antibody for bcOBP detection.
- To investigate the distribution and potential function of bcOBP in bovines.
Main Methods:
- Cloning and expression of bcOBP.
- Development of a monoclonal antibody against bcOBP.
- Quantification of bcOBP in various bovine bodily fluids using the antibody.
- Sequence analysis for conserved motifs.
Main Results:
- bcOBP was successfully cloned, expressed, and its monoclonal antibody established.
- bcOBP was consistently secreted into milk postpartum (181±39 µg/L) and found in nasal mucus, saliva, amniotic fluid, vaginal discharge, and blood plasma.
- bcOBP contains a conserved CxxxC motif, characteristic of pheromone-binding proteins.
- Homologous proteins were detected in the colostrum of other Cetartiodactyla species.
Conclusions:
- The distribution pattern and conserved motif suggest bcOBP functions as a pheromone carrier in bovines.
- bcOBP is secreted into milk from blood, with concentrations varying by lactation stage.
- The findings indicate a potential role for bcOBP in pheromonal communication within and between bovine individuals and related species.
Abstract:
A bovine lipocalin, previously identified as a putative odorant-binding protein in bovine colostrum (bcOBP), was cloned and expressed, and its monoclonal antibody was established. bcOBP was constantly secreted into milk on day of parturition until at least 10 d postpartum at a concentration of 181±39 µg/L. Besides milk, bcOBP occurred in the nasal mucus, saliva, amniotic fluid, vaginal discharge, and blood plasma. Despite its low concentration, the distribution pattern and the finding that bcOBP harbored a characteristic sequence motif, CxxxC, which is conserved among insect and mammal pheromone binding proteins, suggest that bcOBP functions as a pheromone carrier. The presence of bcOBP in the plasma at varied concentrations depending on the lactation period does not exclude the possibility that bcOBP is secreted into milk from the blood. Cross-reactivity of the monoclonal antibody indicated presence of proteins homologous to bcOBP in the colostrum of farm animals of Cetartiodactyla.
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