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Research Article

Structure of the HCMV UL16-MICB Complex Elucidates Select Binding of a Viral Immunoevasin to Diverse NKG2D Ligands

  • Steffen Müller,

    Affiliation: Interfaculty Institute for Biochemistry, University of Tuebingen, Tuebingen, Germany

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  • Georg Zocher,

    Affiliation: Interfaculty Institute for Biochemistry, University of Tuebingen, Tuebingen, Germany

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  • Alexander Steinle,

    Affiliation: Department of Immunology, Interfaculty Institute for Cell Biology, University of Tuebingen, Tuebingen, Germany

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  • Thilo Stehle mail

    thilo.stehle@uni-tuebingen.de

    Affiliations: Interfaculty Institute for Biochemistry, University of Tuebingen, Tuebingen, Germany, Department of Pediatrics, Vanderbilt University School of Medicine, Nashville, Tennessee, United States of America

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  • Published: January 15, 2010
  • DOI: 10.1371/journal.ppat.1000723

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Publisher's Note: Correction to Figure S1

Posted by PLoS_Pathogens on 21 Jan 2010 at 19:41 GMT

Schematic view of the structural mimicry of UL16. The blue regions highlight the five UL16 and NKG2D footprint residues participating in structural mimicry. UL16 residues are shown in white, the corresponding NKG2D residues are shown in black. MICA and MICB residues that are contacted by the footprint are placed in yellow circles, at the approximate position of interaction. Also shown are the amino acids at corresponding positions in ULBP1, ULBP5/6, ULBP2, ULBP3 and ULBP4. In ULBP3 [28], a kink in the α3-helix starting at position 162 (Figure 6B) causes a one-residue shift towards the N-terminus. In these cases, the shifted ULBP3 residue that corresponds to the MICBpf residue is given by a superscript number following the ULBP3 one letter code. As an example, ULBP3 position Met168 and not Val169 corresponds to MICBpf position Ala159. Also as a result of the helix kink, no ULPB3 residue corresponds in space to the MICBpf residue in position 155, indicated by (#). Interactions between residues are represented with arrows, accompanied by green text for hydrogen bonds, red text for salt bridges, and magenta text for hydrophobic contacts; the blue text indicates the clash of ULBP3 Arg162 (Figure 3A) with Leu100 of UL16 or Met184 of NKG2D as observed in the MICA/NKG2D complex structure [26] (Figure 6B).
http://plospathogens.org/article/info:doi/10.1371/journal.ppat.1000723#article1.body1.sec5.supplementary-material2.caption1.p1

The incorrect legend was published for Figure S1, the correct legend should read: Kinetic and equilibrium SPR analyses of UL16 interactions with ULBP1 and ULBP2. (A, B) Kinetic analyses of UL16 binding to Protein A G captured (A) ULBP2 Fc and (B) ULBP1 Fc ectodomains. Each individual analyte concentration was injected twice and data are representative of at least two separate experiments with similar results. Double-referenced sensorgrams (shown in color) are overlaid with fits of a “1:1 binding with mass transfer” model (black lines). Corresponding residual plots below the sensorgrams show the kinetic-fit range and absolute deviation (∆) of data points from curve fit values. The red arrow and the red highlighted area of the sensorgram series indicate data used to determine averaged (AVG) equilibrium (Eq) response values (Eq-Response AVG) for equilibrium analysis. (C), Equilibrium analysis of UL16 binding to the ULBP2-Fc ectodomain. Averaged equilibrium response values (red squares) are plotted against injected UL16 concentrations and fitted to a “1:1 Langmuir isotherm” model (black line). The shaded boxes contain additional information about setup details (black font) and results from kinetic (blue font) and equilibrium analysis (red font).

No competing interests declared.