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August 6, 2009PLoS PathogensOpen Access

Dimerization of Hepatitis E Virus Capsid Protein E2s Domain Is Essential for Virus–Host Interaction

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Population

Recombinant E2s domain from Hepatitis E Virus (HEV) capsid

Design

Preclinical

Authors

SLShaowei LiShandong UniversityXTXuhua TangInstitute of Molecular and Cell BiologyJSJ. SeetharamanUniversity of Tennessee Health Science Center

Discussion

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Implication

May guide HEV vaccine and inhibitor design; leaves open clinical translation pending functional validation.

Structured PICO

P
Population
Recombinant E2s domain from Hepatitis E Virus (HEV) capsid
I
Intervention
Structural and functional analysis (X-ray crystallography, mutagenesis, analytical ultracentrifugation, SDS-PAGE, Western blotting)
O
Outcome
Crystal structure of HEV capsid protein domain E2s and functional role of its dimerizationsurrogate

The crystal structure of the HEV capsid protein domain E2s reveals a homodimer essential for virus-host interaction and antibody neutralization, providing a basis for vaccine and inhibitor development.

Cite This Study

Li et al. (2009) studied this question.

synapsesocial.com/papers/6a9a1c3d63f9dbee96a0b093https://doi.org/10.1371/journal.ppat.1000537
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1The crystal structure of the emerging human-infecting hepatitis E virus E2s protein2020 · 7 citations
  2. 2Mutational Analysis of Essential Interactions Involved in the Assembly of Hepatitis E Virus Capsid2004 · 83 citations
  3. 3Structure of the hepatitis E virus-like particle suggests mechanisms for virus assembly and receptor binding2009 · 257 citations
  4. 4Dimerization: a structural feature for the protection of hepatitis E virus capsid protein against trypsinization2018 · 22 citations
  5. 5Structure of Hepatitis E Virion-sized Particle Reveals an RNA-dependent Viral Assembly Pathway*2010 · 170 citations