Yeh H Y, Luftig R B
Department of Microbiology, Immunology, Louisiana State University Medical Center, New Orleans 70112-1393.
Virology. 1991 Jul;183(1):410-4. doi: 10.1016/0042-6822(91)90156-6.
Properties of human enteric adenovirus type 41 (Ad41) binding to its receptor on the surface of HEp-2 cells were investigated. The binding was found to be temperature-dependent, saturable, and specific. Analysis of the binding data showed a single class of 4.3 x 10(4) receptor sites per cell, an equilibrium dissociation constant of 21.0 nM, and no cooperativity among receptor sites. Trypsin-treated HEp-2 cells subsequently grown in the presence of tunicamycin or 2-deoxyglucose recovered full Ad41 binding activity, but could not if subsequently grown in the presence of cycloheximide. These data indicate that a single type of virus receptor, likely protein in nature, is present on the surface of HEp-2 cells to specifically bind Ad41.
研究了人肠道腺病毒41型(Ad41)与HEp-2细胞表面受体结合的特性。发现这种结合是温度依赖性的、可饱和的且具有特异性。结合数据分析显示,每个细胞有一类4.3×10⁴个受体位点,平衡解离常数为21.0 nM,且受体位点之间无协同性。用胰蛋白酶处理过的HEp-2细胞随后在衣霉素或2-脱氧葡萄糖存在的情况下生长,可恢复完整的Ad41结合活性,但如果随后在环己酰亚胺存在的情况下生长则不能恢复。这些数据表明,HEp-2细胞表面存在一种单一类型的病毒受体,其性质可能为蛋白质,可特异性结合Ad41。