Rai Tia, Caffrey Michael, Rong Lijun
Department of Microbiology and Immunology, College of Medicine, University of Illinois at Chicago, Chicago, IL 60612, USA.
J Virol. 2005 Dec;79(23):14962-6. doi: 10.1128/JVI.79.23.14962-14966.2005.
Avian sarcoma and leukosis virus subgroup A (ASLV-A) entry is mediated by interactions between the viral glycoprotein EnvA and its cognate receptor Tva. Previously, some interesting mutants of ASLV-A have been selected by others which can use chicken Tva, but not quail Tva, for efficient entry. The mutant phenotypes are caused by two point mutations within the surface subunit of EnvA (S. L. Holmen, D. C. Melder, and M. J. Federspiel, J. Virol. 75:726-737, 2001). In this study, we have shown that the altered receptor specificity maps to the LDL-A module of Tva. Further, we have identified two residues in the chicken LDL-A module that allow more efficient viral entry by the mutant viruses. These results demonstrate that the altered receptor specificity of the mutant viruses is determined by specific interactions with residues in the LDL-A module of Tva.
禽肉瘤和白血病病毒A亚群(ASLV-A)的进入是由病毒糖蛋白EnvA与其同源受体Tva之间的相互作用介导的。此前,其他人已筛选出一些有趣的ASLV-A突变体,这些突变体可以利用鸡的Tva,但不能利用鹌鹑的Tva进行有效进入。这些突变体表型是由EnvA表面亚基内的两个点突变引起的(S. L. 霍尔门、D. C. 梅尔德和M. J. 费德尔斯皮尔,《病毒学杂志》75:726 - 737,2001年)。在本研究中,我们已表明,改变的受体特异性定位于Tva的低密度脂蛋白A(LDL-A)模块。此外,我们已在鸡的LDL-A模块中鉴定出两个残基,这两个残基能使突变病毒更有效地进入。这些结果表明,突变病毒改变的受体特异性是由与Tva的LDL-A模块中的残基的特异性相互作用决定 的。