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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface
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The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface

机译：完整的流感血凝素融合结构域在脂质：水界面处采用紧密的螺旋发夹结构

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摘要

All but five of the N-terminal 23 residues of the HA2 domain of the influenza virus glycoprotein hemagglutinin (HA) are strictly conserved across all 16 serotypes of HA genes. The structure and function of this HA2 fusion peptide (HAfp) continues to be the focus of extensive biophysical, computational, and functional analysis, but most of these analyses are of peptides that do not include the strictly conserved residues Trp~(21)-Tyr~(22)-Gly~(23). The het-eronuclear triple resonance NMR study reported here of full length HAfp of sero subtype H1, solubilized in dodecylphosphatidyl cho-line, reveals a remarkably tight helical hairpin structure, with its N-terminal α-helix (Gly~1-Gly~(12)) packed tightly against its second α-helix (Trp~(14)-Gly~(23)), with six of the seven conserved Gly residues at the interhelical interface. The seventh conserved Gly residue in position 13 adopts a positive Φ angle, enabling the hairpin turn that links the two helices. The structure is stabilized by multiple interhelical C'H to C=O hydrogen bonds, characterized by strong interhelical H~N-H~α and H~α-H~α NOE contacts. Many of the previously identified mutations that make HA2 nonfusogenic are also incompatible with the tight antiparallel hairpin arrangement of the HAfp helices. ~(15)N relaxation analysis indicates the structure to be highly ordered on the nanosecond time scale, and NOE analysis indicates HAfp is located at the water-lipid interface, with its hydrophobic surface facing the lipid environment, and the Gly-rich side of the helix-helix interface exposed to solvent.
机译：流感病毒糖蛋白血凝素（HA）的HA2结构域的N末端23个残基中，除5个外，其余所有残基在HA基因的所有16种血清型中都严格保守。这种HA2融合肽（HAfp）的结构和功能仍然是广泛的生物物理，计算和功能分析的重点，但是这些分析大多数都是不包含严格保守的Trp〜（21）-Tyr残基的肽〜（22）-Gly〜（23）。异位核三重共振NMR研究报道了H1型亚型的全长HAfp，溶于十二烷基磷脂酰胆碱中，显示出非常紧密的螺旋发夹结构，其N端α-螺旋（Gly〜1-Gly〜（ 12））紧紧堆积在其第二个α-螺旋（Trp〜（14）-Gly〜（23））上，在螺旋间界面处有七个保守的Gly残基中的六个。位置13上的第七个保守Gly残基呈正Φ角，使连接两个螺旋的发夹结构转弯。该结构通过多个螺旋C'H到C = O氢键来稳定，其特征在于牢固的螺旋H〜N-H〜α和H〜α-H〜αNOE接触。许多先前鉴定的使HA2不融合的突变也与HAfp螺旋的紧密平行的平行发夹结构不相容。 〜（15）N弛豫分析表明该结构在纳秒级时域上是高度有序的，而NOE分析表明HAfp位于水-脂质界面上，其疏水性表面面向脂质环境，且富含Gly的一面螺旋-螺旋界面暴露于溶剂。

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