How the Virus Outsmarts the Host: Function and Structure of Cytomegalovirus MHC-I-Like Molecules in the Evasion of Natural Killer Cell Surveillance

<table>Amino acid sequence alignments  of the extracellular domains of classical MHC-I molecules from mouse (H-2D<sup>d</sup>) and human (HLA-A2) with MHC-I-like viral immunoevasins were generated using ClustalW module of MacVector 10.6.6. H-2D<sup>d</sup> and HLA-A2 share significant similarity at 81.7% (a). UL18 and m144 show detectable sequence similarity (21–40%) with HLA-A2 and H-2D<sup>d</sup>.  Conserved cysteine residues are in yellow (b). The alignment  of m145 family members and other MHC-I-like immunoevasins  shows 6–40%  sequence similarity to the canonical MHC-I molecules (c).</table>

BioMed Research International

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Figure 2

Figure 2: How the Virus Outsmarts the Host: Function and Structure of Cytomegalovirus MHC-I-Like Molecules in the Evasion of Natural Killer Cell Surveillance 

Figure 2 | How the Virus Outsmarts the Host: Function and Structure of Cytomegalovirus MHC-I-Like Molecules in the Evasion of Natural Killer Cell Surveillance 