Heptad-repeat regions of respiratory syncytial virus F1 protein form a six-membered coiled-coil complex

被引：46

作者：

Lawless-Delmedico, MK ^{[1
]}

Sista, P ^{[1
]}

Sen, R ^{[1
]}

Moore, NC ^{[1
]}

Antczak, JB ^{[1
]}

White, JM ^{[1
]}

Greene, RJ ^{[1
]}

Leanza, KC ^{[1
]}

Matthews, TJ ^{[1
]}

Lambert, DM ^{[1
]}

机构：

[1] Trimeris Inc, Durham, NC 27707 USA

来源：

BIOCHEMISTRY | 2000年 / 39卷 / 38期

关键词：

D O I：

10.1021/bi000471y

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The Respiratory Syncytial Virus (RSV) fusogenic glycoprotein Fl was characterized using biochemical and biophysical techniques. Two heptad-repeat (HR) regions within Fl were shown to interact. Proteinase-K digestion experiments highlight the HR1 region (located proximal to the fusion peptide sequence) of the Fl protein to which an HR2-derived (located proximal to the membrane-spanning domain) peptide binds, thus protecting both the protein and peptide from digestion. Solution-phase analysis of HR1-derived peptides shows that these peptides adopt helical secondary structure as measured by circular dichroism. Sedimentation equilibrium studies indicate that these HR1 peptides self-associate in a monomer/trimer equilibrium with an association constant of 5.2 x 10(8) M-2. In contrast, HR2-derived peptides form random monomers in solution. CD analysis of mixtures containing peptides from the two regions demonstrate their propensity to interact and form a very stable (T-m = 87 degrees C), helical (86% helicity) complex comprised of three HR1 and three HR2 members.

引用

页码：11684 / 11695

页数：12

共 60 条

[1] Structural basis for paramyxovirus-mediated membrane fusion [J].