據(jù)2月27日的《科學(xué)》雜志報(bào)道說(shuō)，美國(guó)斯克利普斯研究所(TSRI)的Damian Ekiert及其同事披露了有關(guān)如何將一個(gè)人類的抗體與某一關(guān)鍵性流感蛋白結(jié)合的細(xì)節(jié),，該結(jié)合能夠幫助人們研發(fā)針對(duì)季節(jié)性和大規(guī)模流行性感冒病毒的廣譜疫苗,。
這種叫做CR6261的抗體會(huì)與流感病毒血凝素蛋白的一個(gè)高度保守（即其結(jié)構(gòu)在許多不同的流感病毒株中都非常相似）的區(qū)域結(jié)合。這一發(fā)現(xiàn)對(duì)那些希望設(shè)計(jì)一種較為“通用型”的流感疫苗的研究人員來(lái)說(shuō)是一個(gè)好消息,，因?yàn)樵撏ㄓ眯鸵呙缈梢灾泻投喾N流感病毒株并減弱新的流感大流行所造成的影響,。
目前，人們對(duì)流感病毒的設(shè)計(jì)需要每年都進(jìn)行猜測(cè),，以決定在流行季節(jié)中哪種病毒株將會(huì)流行,。 Ekiert及其同僚對(duì)與CR6261結(jié)合的造成1918年致命性流感的病毒的血凝素蛋白的晶體結(jié)構(gòu)以及該抗體與最近在亞洲造成禽流感爆發(fā)有關(guān)的病毒株的血凝素蛋白結(jié)合的晶體結(jié)構(gòu)進(jìn)行了檢測(cè)。 在這兩種情況下,，該抗體似乎都阻止了血凝素發(fā)生使病毒與一個(gè)健康細(xì)胞融合所需要的那些變化,。（生物谷Bioon.com）
生物谷推薦原始出處：
Science，DOI: 10.1126/science.1171491,，Damian C. Ekiert,，Ian A. Wilson
Antibody Recognition of a Highly Conserved Influenza Virus Epitope
Damian C. Ekiert 1, Gira Bhabha 1, Marc-André Elsliger 1, Robert H. E. Friesen 2, Mandy Jongeneelen 2, Mark Throsby 2, Jaap Goudsmit 2, Ian A. Wilson 3*
1 Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
2 Crucell Holland BV, Archimedesweg 4-6, 2301 CA Leiden, The Netherlands.
3 Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.; The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Influenza virus presents a significant and persistent threat to public health worldwide, and current vaccines provide immunity to viral isolates similar to the vaccine strain. High-affinity antibodies against a conserved epitope could provide immunity to the diverse influenza subtypes and protection against future pandemic viruses. Co-crystal structures were determined at 2.2 and 2.7 ? resolutions for broadly neutralizing human antibody CR6261 Fab in complexes with the major surface antigen (hemagglutinin, HA) from viruses responsible for the 1918 H1N1 influenza pandemic and a recent lethal case of H5N1 avian influenza. In contrast to other structurally characterized influenza antibodies, CR6261 recognizes a highly conserved helical region in the membrane-proximal stem of HA1/HA2. The antibody neutralizes the virus by blocking conformational rearrangements associated with membrane fusion. The CR6261 epitope identified here should accelerate the design and implementation of improved vaccines that can elicit CR6261-like antibodies, as well as antibody-based therapies for the treatment of influenza.
