Petrella JenniElizabeth, Cohen Christopher J, Gaetz Jedidiah, Bergelson Jeffrey M
Division of Immunologic and Infectious Diseases, The Children's Hospital of Philadelphia, 3615 Civic Center Boulevard, Philadelphia, PA 19104, USA.
J Virol. 2002 Oct;76(20):10503-6. doi: 10.1128/jvi.76.20.10503-10506.2002.
In this study, a zebrafish homologue of the coxsackievirus and adenovirus receptor (CAR) protein was identified. Although the extracellular domain of zebrafish CAR (zCAR) is less than 50% identical to that of human CAR (hCAR), zCAR mediated infection of transfected cells by both adenovirus type 5 and coxsackievirus B3. CAR residues interacting deep within the coxsackievirus canyon are highly conserved in zCAR and hCAR, which is consistent with the idea that receptor contacts within the canyon are responsible for coxsackievirus attachment. In contrast, CAR residues contacting the south edge of the canyon are not conserved, suggesting that receptor interaction with the viral "puff region" is not essential for attachment.
在本研究中,鉴定出了柯萨奇病毒和腺病毒受体(CAR)蛋白的斑马鱼同源物。尽管斑马鱼CAR(zCAR)的细胞外结构域与人类CAR(hCAR)的细胞外结构域的同源性低于50%,但zCAR介导了5型腺病毒和柯萨奇病毒B3对转染细胞的感染。在柯萨奇病毒峡谷内部深处相互作用的CAR残基在zCAR和hCAR中高度保守,这与峡谷内的受体接触负责柯萨奇病毒附着的观点一致。相比之下,与峡谷南边缘接触的CAR残基并不保守,这表明受体与病毒“膨化区域”的相互作用对于附着并非必不可少。