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Article

Harnessing an RNA-mediated chaperone for the assembly of influenza hemagglutinin in an immunologically relevant conformation.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology - 1 May 2018

Yang Seung Won, Jang Yo Han, Kwon Soon Bin, Lee Yoon Jae, Chae Wonil, Byun Young Ho, Kim Paul, Park Chan, Lee Young Jae, Kim Choon Kang, Kim Young Seok, Choi Seong Il, Seong Baik Lin

Abstract excerpt

A novel protein-folding function of RNA has been recognized, which can outperform previously known molecular chaperone proteins. The RNA as a molecular chaperone (chaperna) activity is intrinsic to some ribozymes and is operational during viral infections. Our purpose was to test whether influenza hemagglutinin (HA) can be assembled in a soluble, trimeric, and immunologically activating conformation by means of...

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Share to Antibodies, Neutralizing
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hemagglutinin Glycoproteins, Influenza Virus

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Share to Influenza A virus

Share to Molecular Chaperones

Share to Protein Multimerization

Share to RNA, Transfer

Source

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Identifiers

PMID: 29295864
DOI: 10.1096/fj.201700747RR
PMCID: PMC5901386

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

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