Structural flexibility and functional valence of CD4-IgG2 (PRO 542): potential for cross-linking human immunodeficiency virus type 1 envelope spikes.
Structural flexibility and functional valence of CD4-IgG2 (PRO 542): potential for cross-linking human immunodeficiency virus type 1 envelope spikes.
复制标题
CD4-IgG2 (PRO 542) 的结构灵活性和功能价:交联人类免疫缺陷病毒 1 型包膜刺突的潜力。
DOI:
10.1128/jvi.75.14.6682-6686.2001
复制
发表时间:
2001
影响因子:
5.4
通讯作者:
Roux,KH
中科院分区:
文献类型:
--
作者:
Zhu,P;Olson,WC;Roux,KH
CD4-immunoglobulin G2 (CD4-IgG2) incorporates four copies of the D1D2 domains of CD4 into an antibody-like molecule that potently neutralizes primary human immunodeficiency virus type 1. Here electron microscopy was used to explore the structure and functional valence of CD4-IgG2 in complex with gp120. CD4-γ2, a divalent CD4-immunoglobulin fusion protein, was evaluated in parallel. Whereas CD4-γ2–gp120 complexes adopted a simple Y-shaped structure, CD4-IgG2–gp120 complexes consisted of four gp120s arrayed about a central CD4-IgG2 molecule, a structure more reminiscent of complement C1q. Molecular modeling corroborated the electron microscopy data and further indicated that CD4-IgG2 but not CD4-γ2 has significant potential to cross-link gp120-gp41 trimers on the virion surface, suggesting a mechanism for the heightened antiviral activity of CD4-IgG2.