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Published on: March 2, 2016
Echovirus 6 strains derived from a clinical isolate show differences in haemagglutination ability and cell entry
Nicolas Lévêque1, Helene Norder, Youssef Zreik
1Centre National de Référence des Entérovirus, Laboratoire de Virologie, Centre de Biologie et de Pathologie Est, Institut de Microbiologie, Hospices Civils de Lyon, 69677 Bron, France. nicolas.leveque@chu-lyon.fr
Virus Research
|June 15, 2007
Summary
Two echovirus 6 strains were isolated, one retaining haemagglutination (HAEV6) and the other losing it (NHAEV6). HAEV6 uses DAF and caveolae pathways, while NHAEV6 uses clathrin-mediated pathways.
Area of Science:
- Virology
- Cell Biology
- Molecular Biology
Background:
- Echovirus 6 (EV6) is a significant human pathogen.
- Viral entry mechanisms dictate host cell tropism and pathogenesis.
- Understanding viral adaptation and evolution is crucial for disease control.
Purpose of the Study:
- To investigate the mechanisms underlying echovirus 6 adaptation and altered cell entry.
- To characterize the role of DAF (decay-accelerating factor) in EV6 haemagglutination.
- To elucidate the distinct cellular pathways utilized by different EV6 strains.
Main Methods:
- Isolation and characterization of EV6 strains with differing haemagglutinating properties.
- Virus binding assays using DAF-expressing cells.
- Coinfection experiments to assess viral competition.
- Analysis of cellular entry pathways (caveolae-dependent vs. clathrin-mediated).
- Sequence analysis of viral capsid proteins (VP1, VP2, VP3).
Main Results:
- Two EV6 strains were isolated: HAEV6 (haemagglutinating) and NHAEV6 (non-haemagglutinating).
- HAEV6 binding to DAF-expressing cells confirmed DAF's role in haemagglutination.
- HAEV6 preferentially utilized lipid raft-dependent caveolae pathways for entry.
- NHAEV6 utilized the clathrin-mediated pathway for entry.
- Five amino acid changes in capsid proteins (VP1, VP2, VP3) were identified between strains.
Conclusions:
- EV6 can adapt to utilize distinct cellular entry pathways, influencing its biological properties.
- DAF is a key receptor for HAEV6 haemagglutination and cell binding.
- Changes in viral capsid proteins are associated with altered receptor binding, entry mechanisms, and potentially pathogenicity.
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