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Structural Insights into the Human Metapneumovirus Glycoprotein Ectodomain

DOI: 10.1128/JVI.01726-14 DOI Help
PMID: 25031352 PMID Help

Authors: C. Leyrat (University of Oxford) , G. C. Paesen (University of Oxford) , J. Charleston (University of Oxford) , M. Renner (University of Oxford) , J. M. Grimes (Division of Structural Biology, University of Oxford, Diamond Light Source)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Virology , VOL 88 (19) , PAGES 11611 - 11616

State: Published (Approved)
Published: September 2014

Open Access Open Access

Abstract: Human metapneumovirus is a major cause of respiratory tract infections worldwide. Previous reports have shown that the viral attachment glycoprotein (G) modulates innate and adaptive immune responses, leading to incomplete immunity and promoting reinfection. Using bioinformatics analyses, static light scattering, and small-angle X-ray scattering, we show that the extracellular region of G behaves as a heavily glycosylated, intrinsically disordered polymer. We discuss potential implications of these findings for the modulation of immune responses by G.

Subject Areas: Biology and Bio-materials

Facility: ESRF

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