IgG4和IgG1经过共同的酸诱导压实成交替折叠状态。

IF 3.5 4区生物学 Q1 Biochemistry, Genetics and Molecular Biology

FEBS Letters Pub Date : 2025-03-17 DOI:10.1002/1873-3468.70031

Hiroshi Imamura, Shinya Honda

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引用次数: 0

摘要

免疫球蛋白G1 （IgG1）抗体在酸性条件下变性，导致选择性折叠状态（AFS）。AFS结构比原生态结构更紧凑。然而，AFS在其他亚类中的患病率仍未得到充分研究。本研究证明人源化的IgG4也可以采用AFS结构，通过粒径排除色谱-小角度x射线散射（SEC-SAXS）分析证实了这一点。这些发现表明免疫球蛋白G （igg）的异常压实对亚类之间序列和结构的变化具有弹性。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

IgG4 and IgG1 undergo common acid-induced compaction into an alternatively folded state

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IgG4 and IgG1 undergo common acid-induced compaction into an alternatively folded state

Immunoglobulin G1 (IgG1) antibodies undergo denaturation in acidic conditions, resulting in an alternatively folded state (AFS). The AFS structure is more compact than the native state. However, the prevalence of AFS in other subclasses remains largely unexplored. This study provides evidence that humanized IgG4 can also adopt the AFS structure, as demonstrated through size-exclusion chromatography coupled with small-angle X-ray scattering (SEC-SAXS) analysis. These findings suggest that the anomalous compaction of immunoglobulins G (IgGs) is resilient to variations in sequence and structure among subclasses.

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来源期刊

FEBS Letters 生物-生化与分子生物学

CiteScore

7.00

自引率

2.90%

发文量

303

审稿时长

1.0 months

期刊介绍： FEBS Letters is one of the world''s leading journals in molecular biology and is renowned both for its quality of content and speed of production. Bringing together the most important developments in the molecular biosciences, FEBS Letters provides an international forum for Minireviews, Research Letters and Hypotheses that merit urgent publication.