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首页> 美国卫生研究院文献>Journal of Virology >Glycoprotein B of Herpes Simplex Virus 2 Has More than One Intracellular Conformation and Is Altered by Low pH
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Glycoprotein B of Herpes Simplex Virus 2 Has More than One Intracellular Conformation and Is Altered by Low pH

机译：单纯疱疹病毒2的糖蛋白B具有一种以上的细胞内构型并被低pH值改变

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摘要

The crystal structure of herpes simplex virus (HSV) gB identifies it as a class III fusion protein, and comparison with other such proteins suggests this is the postfusion rather than prefusion conformation, although this is not proven. Other class III proteins undergo a pH-dependent switch between pre- and postfusion conformations, and a low pH requirement for HSV entry into some cell types suggests that this may also be true for gB. Both gB and gH undergo structural changes at low pH, but there is debate about the extent and significance of the changes in gB, possibly due to the use of different soluble forms of the protein and different assays for antigenic changes. In this study, a complementary approach was taken, examining the conformations of full-length intracellular gB by quantitative confocal microscopy with a panel of 26 antibodies. Three conformations were distinguished, and low pH was found to be a major influence. Comparison with previous studies indicates that the intracellular conformation in low-pH environments may be the same as that of the soluble form known as s-gB at low pH. Interestingly, the antibodies whose binding was most affected by low pH both have neutralizing activity and consequently must block either the function of a neutral pH conformation or its switch from an inactive form to an activated form. If one of the intracellular conformations is the fusion-active form, another factor required for fusion is presumably absent from wherever that conformation is present in infected cells so that inappropriate fusion is avoided.
机译：单纯疱疹病毒（HSV）gB的晶体结构将其鉴定为III类融合蛋白，与其他此类蛋白的比较表明，这是融合后而不是融合前的构象，尽管尚未得到证实。其他III类蛋白质在融合前和融合后构象之间经历了pH依赖性转换，并且HSV进入某些细胞类型的低pH要求表明，这对于gB也可能是正确的。 gB和gH都在低pH值下发生结构变化，但是关于gB变化的程度和重要性存在争议，这可能是由于使用了蛋白质的不同可溶性形式和抗原变化的不同测定所致。在这项研究中，采取了一种补充方法，通过使用共26种抗体的定量共聚焦显微镜检查全长细胞内gB的构象。区分了三种构象，发现低pH是主要影响。与先前研究的比较表明，在低pH环境中的细胞内构象可能与在低pH条件下称为s-gB的可溶性形式的构象相同。有趣的是，其结合受低pH影响最大的抗体都具有中和活性，因此必须阻断中性pH构象的功能或其从无活性形式转变为活化形式的功能。如果细胞内构象之一是融合活性形式，则无论受感染细胞中该构象存在于何处，都可能不存在融合所需的另一因素，从而避免了不适当的融合。

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