• 我要登录|
  • 免费注册
    |
  • 我的丁香通
    • 企业机构:
    • 成为企业机构
    • 个人用户:
    • 个人中心
  • 移动端
    移动端
丁香通 logo丁香实验_LOGO
搜实验

    大家都在搜

      大家都在搜

        0 人通过求购买到了急需的产品
        免费发布求购
        发布求购
        点赞
        收藏
        wx-share
        分享

        Inhibition of HIV Infection by Lectin Binding to gp120

        互联网

        796
        Human immunodeficiency virus (HIV) is the causative agent of AIDS (acquired immunodeficiency syndrome). The polypeptide precursor gp160 of HIV-1 forms the external glycoprotein, gp120 and the transmembrane glycoprotein, gp41 (1 ). Sequence variability is a feature of HIV viruses that have been classified into several subtypes (2 ). There are 22–31 potential N -linked glycosylation sites on gp120 depending on the HIV-1 isolate and thus, approximately half of its molecular weight is composed of carbohydrate. Gp120 oligosaccharides are a mixture of high mannose-, hybrid-, and complex-type N -glycans (3 -5 ). The proportion of these N -glycan substituents on the envelope glycoprotein varies on different HIV-2 isolates propagated in different cell lines (6 ). The less-processed oligosaccharides are primarily located on conserved N -linked glycosylation sites on the recombinant gp120s produced in CHO cells and by a baculovirus expression system (4 ,7 ). This points to the high mannose and hybridtype oligosaccharides as being important in the structure and/or function of the envelope glycoprotein.
        ad image
        提问
        扫一扫
        丁香实验小程序二维码
        实验小助手
        丁香实验公众号二维码
        扫码领资料
        反馈
        TOP
        打开小程序