一种登革2型特异性单克隆抗体与包膜蛋白结构域3上的登革病毒复合反应性抗原位点结合。
A DENV-2-type-specific monoclonal antibody binds to the DENV-complex-reactive antigenic site on envelope protein domain 3.
作者信息
Sarathy Vanessa V, Pitcher Trevor J, Gromowski Gregory D, Roehrig John T, Barrett Alan D T
机构信息
Sealy Center for Vaccine Development, University of Texas Medical Branch, Galveston TX 77555, USA.
Department of Pathology, University of Texas Medical Branch, Galveston, TX 77555, USA.
出版信息
J Gen Virol. 2017 Jun;98(6):1299-1304. doi: 10.1099/jgv.0.000785. Epub 2017 Jun 20.
The Dengue virus (DENV) envelope (E) protein is the major component of the viral surface and is structurally subdivided into three domains, ED1, ED2 and ED3. ED3 elicits potent neutralizing antibodies and contains two major antigenic sites: the DENV-type-specific and DENV-complex-reactive antigenic sites. Each site is composed of a limited subset of residues that are required for monoclonal antibody (mAb) binding. Here we show that DENV-2-type-specific mAb 9A3D-8 utilizes the functionally critical residues K307, V308, K310, I312, P332, L387, L389 and N390 for ED3 binding. Surprisingly, this DENV-type-specific epitope is predicted to overlap with the ED3 DENV-complex-reactive antigenic site on the viral surface. Further, this unique binding site enables mAb 9A3D-8 to neutralize virus infectivity at relatively low occupancy of virions compared to other ED3 mAbs identified to date. Together, the data in this study indicate that this is a new DENV-2-type-specific antigenic site on ED3.
登革病毒（DENV）包膜（E）蛋白是病毒表面的主要成分，在结构上可细分为三个结构域，即ED1、ED2和ED3。ED3可诱导产生强效中和抗体，并包含两个主要抗原位点：登革病毒型特异性和登革病毒复合体反应性抗原位点。每个位点均由单克隆抗体（mAb）结合所需的有限数量的残基组成。在此，我们表明登革病毒2型特异性单克隆抗体9A3D - 8利用功能关键残基K307、V308、K310、I312、P332、L387、L389和N390与ED3结合。令人惊讶的是，这个登革病毒型特异性表位预计与病毒表面的ED3登革病毒复合体反应性抗原位点重叠。此外，与迄今鉴定的其他ED3单克隆抗体相比，这个独特的结合位点使单克隆抗体9A3D - 8能够在相对较低的病毒体占有率下中和病毒感染性。总之，本研究中的数据表明这是ED3上一个新的登革病毒2型特异性抗原位点。
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