Minocha H C, Xue W, Reddy J R
Department of Diagnostic Medicine/Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan 66506, USA.
Adv Exp Med Biol. 1997;412:145-8. doi: 10.1007/978-1-4899-1828-4_22.
A 50 kDa cell surface protein from MDBK cells has been identified as a putative receptor for bovine viral diarrhea virus (BVDV) by using a BVDV specific anti-idiotypic antibody (Anti-D89). This study delineates further characterization of the receptor protein. Protease treatment of cultured MDBK cells adversely affected the receptor thus abolishing the binding of anti-D89 to the cells. However, pretreatment of the cells with either phospholipases or glycosidases did not signficantly alter the extent of anti-D89 binding. Additionally, pretreatment of cell monolayers with proteases decreased BVDV attachment and replication in the cells. These results suggested that the receptor for BVDV is a protein in nature, and glycosylation and phosphorylation of the receptor protein may not play a direct role in BVDV attachment to cells. The BVDV receptor protein gradually regenerated on cells when they were maintained in culture following protease treatment. The purified 50 kDa receptor protein also significantly inhibited BVDV infection in a plaque reduction assay.
利用牛病毒性腹泻病毒（BVDV）特异性抗独特型抗体（抗-D89），已鉴定出MDBK细胞表面一种50 kDa的蛋白质为BVDV的假定受体。本研究进一步阐述了该受体蛋白的特性。用蛋白酶处理培养的MDBK细胞会对受体产生不利影响，从而消除抗-D89与细胞的结合。然而，用磷脂酶或糖苷酶预处理细胞并不会显著改变抗-D89的结合程度。此外，用蛋白酶预处理细胞单层会降低BVDV在细胞中的附着和复制。这些结果表明，BVDV的受体本质上是一种蛋白质，并且受体蛋白的糖基化和磷酸化可能在BVDV与细胞的附着过程中不发挥直接作用。蛋白酶处理后，当细胞在培养中维持时，BVDV受体蛋白会在细胞上逐渐再生。在蚀斑减少试验中，纯化的50 kDa受体蛋白也显著抑制了BVDV感染。
