英美科学家通过联合研究发现，绿茶所含的一种成分能阻止艾滋病病毒附着到免疫细胞上。
据英国媒体３１日报道，研究人员发现，绿茶含有一种多酚类化合物ＥＧＣＧ，一旦这种成分先附着在免疫细胞上，艾滋病病毒就不再有机会附着上去了。
英国谢菲尔德大学的威廉姆森教授说：“我们的研究显示，喝绿茶可能有助于减少感染艾滋病病毒的危险，并有助于减缓艾滋病病毒的扩散。”
但他同时强调说，喝绿茶不是治疗艾滋病的方法，也不是预防艾滋病的安全手段，但对一些感染者来说，这种方法可以与传统药物相配合，缓解他们的病情。
威廉姆森说，有关的研究还处于初级阶段，还要进一步研究，看绿茶饮用量是否影响绿茶成分抵御艾滋病病毒的效果。
这项联合研究成果刊登在最新一期美国《过敏与临床免疫学》杂志上。
部分英文原文：
Volume 113, Issue 2 (Supplement), Page S256 (February 2004)
Green tea polyphenol epigallocatechin gallate binding to CD4 as a model for the inhibition of HIV-1-gp120 binding to CD4+ T cells
Abstract
Rationale
The catechin, epigallocatechin gallate (EGCG), the active component of green tea, has anti-inflammatory, anti-tumorigenic, and anti-oxidative as well as anti-viral properties. In vitro, EGCG inhibits HIV-1 replication by the inhibition of HIV-1 reverse transcriptase with a resultant lowered p24 antigenemia. Recently, EGCG has been linked with interference of gp120 binding to CD4. We propose a model of EGCG binding to the CD4 molecule with competitive inhibition of HIV-1-gp120 binding.
Methods
Previously generated NMR spectroscopy and time-averaged nuclear Overhauser effects of EGCG protein chemistry were utilized in the development of multiple EGCG molecular conformations. Using the protein database file 1CDJ, the molecular structure of CD4 was illustrated via electron density mapping at 3A. Modeling of EGCG binding to CD4 was achieved by computer-generated docking programs.
Results
Specific residues of the D1 domain of the CD4 molecule involved in HIV-1-gp120 binding were demonstrated to be potential sites of EGCG binding. Analysis of the residues involved in the binding of HIV-1-gp120 to the CD4 molecule revealed a binding pocket of amino acids, flanked by Phe43 and Arg59. The inherent conformational flexibility of EGCG lends itself to binding with this region of critical residues.
Conclusions
Mechanisms that interfere with the interaction of HIV-1-gp120 and CD4+ T cells have been purported as potential targets in HIV-1 treatment. We present a model of EGCG binding to a pocket of the CD4 molecule that might result in the interference of HIV-1-gp120 binding and subsequent inhibition of HIV-1 infection of CD4+ T cells
