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Cellular expression and crystal structure of the murine cytomegalovirus major histocompatibility complex class I-like

Janet Mans1, Kannan Natarajan, Andrea Balbo

  • 1Molecular Biology Section, Laboratory of Immunology, NIAID, National Institutes of Health, Bethesda, Maryland 20892-1892, USA.

The Journal of Biological Chemistry
|September 28, 2007
PubMed

Insights

Mouse cytomegalovirus (MCMV) protein m153, a novel MHC-I-like molecule, is expressed on infected cells. Its structure reveals unique dimerization and an extended N terminus, aiding study of MCMV immune evasion strategies.

Area of Science:

  • Virology
  • Immunology
  • Structural Biology

Background:

  • Mouse cytomegalovirus (MCMV) is a beta-herpesvirus used to model virus-host interactions.
  • MCMV encodes the m145 family of immunoevasins with predicted Major Histocompatibility Complex, Class I (MHC-I) structures.
  • Some m145 family members modulate host MHC-I and NKG2D ligands, and interact with NK cell receptors.

Purpose of the Study:

  • To characterize the cellular, biochemical, and structural properties of the MCMV m153 protein.
  • To understand the structural basis of m153 function within the m145 family and its interaction with the host immune system.

Main Methods:

  • Cellular expression analysis of m153 in MCMV-infected cells.
  • Biochemical characterization including glycosylation and dimerization.
  • X-ray crystallography to determine the 2.4-A crystal structure of m153.

Main Results:

  • m153 is a heavily glycosylated homodimer expressed on the surface of MCMV-infected cells.
  • m153 does not require beta2-microglobulin or peptide for its structure or expression.
  • The crystal structure reveals an MHC-I-like fold with a novel dimerization mode and a disulfide-stabilized extended N terminus.

Conclusions:

  • The determined structure of m153 provides a framework for understanding the m145 family of MCMV immunoevasins.
  • m153 represents a distinct MHC-I-like molecule involved in MCMV immune evasion.
  • Further studies can utilize this structural information to explore MCMV-host interactions and develop therapeutic strategies.

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