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Murine norovirus capsid plasticity – Glycochenodeoxycholic acid stabilizes P-domain dimers and trigg...

Murine norovirus capsid plasticity – Glycochenodeoxycholic acid stabilizes P-domain dimers and trigg...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2505397324

Murine norovirus capsid plasticity – Glycochenodeoxycholic acid stabilizes P-domain dimers and triggers escape from antibody recognition

About this item

Full title

Murine norovirus capsid plasticity – Glycochenodeoxycholic acid stabilizes P-domain dimers and triggers escape from antibody recognition

Publisher

Cold Spring Harbor: Cold Spring Harbor Laboratory Press

Journal title

bioRxiv, 2021-02

Language

English

Formats

Publication information

Publisher

Cold Spring Harbor: Cold Spring Harbor Laboratory Press

More information

Scope and Contents

Contents

Abstract The murine norovirus (MNV) capsid protein is the target for various neutralizing antibodies binding to distal tips of its protruding (P)-domain. The bile acid glycochenodeoxycholic acid (GCDCA), an important co-factor for murine norovirus (MNV) infection, has recently been shown to induce conformational changes in surface-loops and a contr...

Alternative Titles

Full title

Murine norovirus capsid plasticity – Glycochenodeoxycholic acid stabilizes P-domain dimers and triggers escape from antibody recognition

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_journals_2505397324

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2505397324

Other Identifiers

E-ISSN

2692-8205

DOI

10.1101/2021.02.27.433148