Identification of two distinct structural regions in a human porcine endogenous retrovirus receptor, HuPAR2, contributing to function for viral entry
2009
Understanding HuPAR2's Role in Viral Entry
Sample size: 3
publication
Evidence: high
Author Information
Author(s): Katherine T. Marcucci, Takele Argaw, Carolyn A. Wilson, Daniel R. Salomon
Primary Institution: The Scripps Research Institute
Hypothesis
What are the structural regions in HuPAR2 that contribute to its function for viral entry?
Conclusion
HuPAR2 has two distinct structural regions that influence its function for PERV-A entry.
Supporting Evidence
- HuPAR2 is 11-fold more functional for PERV-A infection than HuPAR1.
- The first 135 amino acids of HuPAR2 are critical for PERV-A entry.
- Seven residues in HuPAR2 enhance its function without affecting envelope binding.
Takeaway
Scientists studied a protein called HuPAR2 to see how it helps a virus enter cells, finding two important parts that help it work better.
Methodology
The study involved creating chimeras and performing infection assays to assess receptor function.
Statistical Information
P-Value
p < 0.001
Statistical Significance
p < 0.001
Digital Object Identifier (DOI)
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