英美科學(xué)家通過聯(lián)合研究發(fā)現(xiàn),，綠茶所含的一種成分能阻止艾滋病病毒附著到免疫細(xì)胞上,。
據(jù)英國媒體３１日?qǐng)?bào)道，研究人員發(fā)現(xiàn),，綠茶含有一種多酚類化合物ＥＧＣＧ,，一旦這種成分先附著在免疫細(xì)胞上，艾滋病病毒就不再有機(jī)會(huì)附著上去了,。
英國謝菲爾德大學(xué)的威廉姆森教授說：“我們的研究顯示,，喝綠茶可能有助于減少感染艾滋病病毒的危險(xiǎn)，并有助于減緩艾滋病病毒的擴(kuò)散,。”
但他同時(shí)強(qiáng)調(diào)說,，喝綠茶不是治療艾滋病的方法，也不是預(yù)防艾滋病的安全手段,，但對(duì)一些感染者來說,，這種方法可以與傳統(tǒng)藥物相配合，緩解他們的病情,。
威廉姆森說,，有關(guān)的研究還處于初級(jí)階段，還要進(jìn)一步研究,，看綠茶飲用量是否影響綠茶成分抵御艾滋病病毒的效果,。
這項(xiàng)聯(lián)合研究成果刊登在最新一期美國《過敏與臨床免疫學(xué)》雜志上。
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
