Recombinant Partial Conglutinin of Buffalo and Nilgai In Vitro Can Mimic the Functions of Native Conglutinin In Vivo
2019
Ramēṣ, Ta. | Chandra Mohan, S. | Saini, Mohini | Barik, Sasmita | Shynu, M. | Das, Asit | Sharma, Anil Kumar | Chaturvedi, Vinod Kumar | Gupta, Praveen Kumar
Conglutinin, a high molecular weight protein detected in bovine serum, belongs to the family of innate immunity markers called collectins. It plays a key role as antimicrobial agent against all kinds of micro-organisms by binding to sugar moieties present on them. In the present study, partial recombinant conglutinin consisting neck and carbohydrate recognition domain of buffalo and nilgai was expressed in prokaryotic system and found to be of 27 kDa through SDS-PAGE and western blotting using antiserum raised against buffalo conglutinin. In the presence of calcium, protein showed high binding activity towards mannan coated to microtitre plate but in contrast, binding activity towards lipopolysaccharide was calcium independent, which needs to be explored further. The partial protein was unable to inhibit haemagglutination by Newcastle disease virus; this could be attributed to lack of complete protein, as complete protein forms tetramer which can cross link the virus. The protein was also found to reduce bovine herpes virus-1 titre propagated in MDBK cells. This paves path to check the effect of complete conglutinin protein on different enveloped viruses, which will provide insight into protein’s importance in innate immunity. Since the concentration of serum conglutinin is found to be hereditary dependent, this could be also helpful in better parentage selection.
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