Structural Characterization of Cuta- and Tusavirus : Insight into Protoparvoviruses Capsid Morphology

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Mietzsch , M , McKenna , R , Väisänen , E , Yu , J C , Ilyas , M , Hull , J A , Kurian , J , Smith , J K , Chipman , P , Lasanajak , Y , Smith , D , Söderlund-Venermo , M & Agbandje-McKenna , M 2020 , ' Structural Characterization of Cuta- and Tusavirus : Insight into Protoparvoviruses Capsid Morphology ' , Viruses-Basel , vol. 12 , no. 6 , 653 . https://doi.org/10.3390/v12060653

Title: Structural Characterization of Cuta- and Tusavirus : Insight into Protoparvoviruses Capsid Morphology
Author: Mietzsch, Mario; McKenna, Robert; Väisänen, Elina; Yu, Jennifer C.; Ilyas, Maria; Hull, Joshua A.; Kurian, Justin; Smith, J. Kennon; Chipman, Paul; Lasanajak, Yi; Smith, David; Söderlund-Venermo, Maria; Agbandje-McKenna, Mavis
Contributor: University of Helsinki, Department of Virology
University of Helsinki, Human Parvoviruses: Epidemiology, Molecular Biology and Clinical Impact
Date: 2020-06
Language: eng
Number of pages: 19
Belongs to series: Viruses-Basel
ISSN: 1999-4915
URI: http://hdl.handle.net/10138/319108
Abstract: Several members of theProtoparvovirusgenus, capable of infecting humans, have been recently discovered, including cutavirus (CuV) and tusavirus (TuV). To begin the characterization of these viruses, we have used cryo-electron microscopy and image reconstruction to determine their capsid structures to similar to 2.9 angstrom resolution, and glycan array and cell-based assays to identify glycans utilized for cellular entry. Structural comparisons show that the CuV and TuV capsids share common features with other parvoviruses, including an eight-stranded anti-parallel beta-barrel, depressions at the icosahedral 2-fold and surrounding the 5-fold axes, and a channel at the 5-fold axes. However, the viruses exhibit significant topological differences in their viral protein surface loops. These result in three separated 3-fold protrusions, similar to the bufaviruses also infecting humans, suggesting a host-driven structure evolution. The surface loops contain residues involved in receptor binding, cellular trafficking, and antigenic reactivity in other parvoviruses. In addition, terminal sialic acid was identified as the glycan potentially utilized by both CuV and TuV for cellular entry, with TuV showing additional recognition of poly-sialic acid and sialylated Lewis X (sLeXLeXLeX) motifs reported to be upregulated in neurotropic and cancer cells, respectively. These structures provide a platform for annotating the cellular interactions of these human pathogens.
Subject: parvovirus
protoparvovirus
cryo-EM
capsid
human pathogen
glycan receptor
sialic acid
SIALIC-ACID BINDING
MINUTE VIRUS
CANINE PARVOVIRUS
TRANSFERRIN RECEPTOR
PORCINE PARVOVIRUS
DIARRHEA
AFFINITY
TRANSDUCTION
BUFAVIRUS
LEUCINE
11832 Microbiology and virology
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