Burton Dennis R, Stanfield Robyn L, Wilson Ian A
Department of Immunology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Proc Natl Acad Sci U S A. 2005 Oct 18;102(42):14943-8. doi: 10.1073/pnas.0505126102. Epub 2005 Oct 11.
HIV has evolved many strategies to avoid neutralizing antibody responses, particularly to conserved regions on the external glycoprotein spikes of the virus. Nevertheless, a small number of antibodies have been evolved by the human immune system to recognize conserved parts of the glycoproteins, and therefore, have broadly neutralizing cross-strain activities. These antibodies constitute important tools in the quest to design immunogens that can elicit broadly neutralizing antibodies in humans and hence contribute to an effective HIV vaccine. Crystallographic analyses of the antibodies, in many cases in an antigen-complexed form, have revealed novel and, in some instances, remarkable structural adaptations to attain virus recognition. Antibodies, like HIV, can evolve relatively rapidly through mutation and selection. It seems that the structures of these broadly neutralizing antibodies bear witness to a heroic struggle between two titans of rapid evolution.
人类免疫缺陷病毒（HIV）已经进化出许多策略来逃避中和抗体反应，尤其是针对该病毒外部糖蛋白刺突上的保守区域。然而，人类免疫系统已经进化出少数抗体来识别糖蛋白的保守部分，因此具有广泛的中和跨毒株活性。这些抗体是设计能在人类中引发广泛中和抗体从而有助于研发有效HIV疫苗的免疫原过程中的重要工具。对这些抗体的晶体学分析，在许多情况下是抗原复合形式的分析，揭示了为实现病毒识别而出现的新颖且在某些情况下引人注目的结构适应性变化。抗体，就像HIV一样，可以通过突变和选择相对快速地进化。这些广泛中和抗体的结构似乎见证了两个快速进化巨头之间的一场英勇斗争。
