推荐原始出处：
Biology Direct 2009, 4:18doi:10.1186/1745-6150-4-18
Mapping the sequence mutations of the 2009 H1N1 influenza A virus neuraminidase relative to drug and antibody binding sites
Sebastian Maurer-Stroh , Jianmin Ma , Raphael Tze Chuen Lee , Fernanda L Sirota and Frank Eisenhaber
In this work, we study the consequences of sequence variations of the "2009 H1N1" (swine or Mexican flu) influenza A virus strain neuraminidase for drug treatment and vaccination. We find that it is phylogenetically more closely related to European H1N1 swine flu and H5N1 avian flu rather than to the H1N1 counterparts in the Americas. Homology-based 3D structure modeling reveals that the novel mutations are preferentially located at the protein surface and do not interfere with the active site. The latter is the binding cavity for 3 currently used neuraminidase inhibitors: oseltamivir (Tamiflu(R)), zanamivir (Relenza(R)) and peramivir; thus, the drugs should remain effective for treatment. However, the antigenic regions of the neuramidase relevant for vaccine development, serological typing and passive antibody treatment can differ from those of previous strains and already vary among patients. Reviewers: This article was reviewed by Sandor Pongor and Aravind Lakshminarayanan Iyer.
 |
甲型H1N1流感3D结构模型
（生物化学资料网注：红点代表药物及其他原子，蓝色点代表甲型H1N1病毒相比1918年流感病毒新变异点，黄点代表甲型H1N1流感出现在不同病例中的变异点，橙色点代表只在一个甲型H1N1流感病例中出现的变异）
新加坡科研人员在新一期《生物学指南》杂志上发表论文说，他们在获得首例人感染甲型H1N1流感病毒样本后，用两周时间研制出了与该病毒有关的一种关键蛋白质的三维结构模型。这一研究成果将有助于科研人员开发防治甲型H1N1流感的药物和疫苗。
甲型H1N1流感病毒表面密布两种蛋白质——血细胞凝集素（H）和神经氨酸酶（N）。新加坡生物信息研究所的科研人员通过分子三维结构计算等方法，研制出了该病毒表面的神经氨酸酶的三维结构模型。
通过分析上述三维模型，研究人员发现，与H5N1型禽流感病毒以及1918年西班牙流感病毒相比，目前正在蔓延的甲型H1N1流感病毒表面的神经氨酸酶的结构已发生重大变化，而且它更接近于H5N1型禽流感病毒的神经氨酸酶结构。以前针对神经氨酸酶开发的流感疫苗对预防目前的甲型H1N1流感病毒效果不大，而达菲和乐感清对甲型H1N1流感病毒有一定疗效。
新加坡生物信息研究所所长弗兰克·艾森哈贝尔认为，利用“计算生物学”方法了解甲型H1N1流感病毒变异对免疫系统和药物的影响意义重大，这将帮助科研人员开发出有效治疗甲型H1N1流感的方法和药物。