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Structural and Molecular Evidence Suggesting Coronavirus-driven Evolution of Mouse Receptor.

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Mice evolved a variant receptor, mCEACAM1b, to evade mouse hepatitis coronavirus (MHV) infection. Structural and residue differences in mCEACAM1b reduce viral binding, illustrating pathogen-driven host receptor evolution.

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Area of Science:

  • Virology
  • Structural Biology
  • Evolutionary Biology

Background:

  • Hosts and pathogens engage in an evolutionary arms race.
  • Mouse hepatitis coronavirus (MHV) uses mouse CEACAM1a (mCEACAM1a) as its receptor for infection.
  • A variant receptor, mCEACAM1b, evolved from the Ceacam1a gene, exhibits reduced MHV binding.

Purpose of the Study:

  • To elucidate the detailed structural and molecular mechanisms behind the differential MHV receptor activities of mCEACAM1a and mCEACAM1b.
  • To understand how structural and residue variations in mCEACAM1b contribute to its poor MHV receptor function.

Main Methods:

  • Determined the crystal structure of mCEACAM1b.
  • Identified structural and residue differences between mCEACAM1a and mCEACAM1b affecting MHV binding.
  • Utilized pseudovirus entry and protein-protein binding assays to assess receptor activity.

Main Results:

  • Identified conformational alterations in the CC' loop and residue variations in other MHV-binding regions (β-strands C', C'', loop C'C'') between mCEACAM1a and mCEACAM1b.
  • Demonstrated that introducing mCEACAM1b features into mCEACAM1a reduces viral receptor activity.
  • Showed that introducing mCEACAM1a features into mCEACAM1b enhances viral receptor activity.

Conclusions:

  • Elucidated the detailed molecular mechanism for differential MHV receptor activity.
  • Provided insight into pathogen-driven evolution of host receptor proteins.
  • Highlighted how structural and residue changes in mCEACAM1b allow mice to counter MHV infection.