July 12, 2003Journal of VirologyOpen Access

A Cellular Receptor of Human Rhinovirus Type 2, the Very-Low-Density Lipoprotein Receptor, Binds to Two Neighboring Proteins of the Viral Capsid

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Population

Human rhinovirus type 2 (HRV2) and recombinant very-low-density lipoprotein receptor (VLDL-R) fragments

Design

Preclinical

Authors

ENEmmanuelle NeumannCentre National de la Recherche Scientifique RMRosita MoserUniversity of Vienna LSLuc SnyersMedical University of Vienna

Discussion

Member takes

Implication

Structural details of VLDL-R–HRV2 engagement are hypothesis-generating; extends models of viral entry but should not yet guide practice.

Structured PICO

Population

Human rhinovirus type 2 (HRV2) and recombinant very-low-density lipoprotein receptor (VLDL-R) fragments

Intervention

Binding of VLDL-R fragments to HRV2

Outcome

Binding footprints and structural resolution of the HRV2-VLDL-R complex using cryoelectron microscopysurrogate

The study reveals the structural mechanism by which the VLDL receptor binds to human rhinovirus type 2, showing that two adjacent viral proteins are stapled together by the receptor's second and third repeats.

Cite This Study

Neumann et al. (2003) studied this question.

synapsesocial.com/papers/6a70988a8031ec7bb1dc735a https://doi.org/10.1128/jvi.77.15.8504-8511.2003

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Implication

Structural details of VLDL-R–HRV2 engagement are hypothesis-generating; extends models of viral entry but should not yet guide practice.

A Cellular Receptor of Human Rhinovirus Type 2, the Very-Low-Density Lipoprotein Receptor, Binds to Two Neighboring Proteins of the Viral Capsid

Discussion

Member takes

Implication

Structured PICO

Cite This Study

A Cellular Receptor of Human Rhinovirus Type 2, the Very-Low-Density Lipoprotein Receptor, Binds to Two Neighboring Proteins of the Viral Capsid

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider