Comparison of antiviral responses in two bat species reveals conserved and divergent innate immune pathways.

When looking at the substitution rate of amino acids across paralogs of bat TNFRSF14, we observe an interesting trend: The residues whose homologs in human TNFRSF14 were shown to form an interface with herpes glycoprotein D (gD) (based on the crystal structure of the human-herpes virus complex), are significantly more divergent in comparison with other surface residues of the TNFRSF14 protein.

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