Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 699 - 707 |
| Number of pages | 9 |
| Journal | Nature Immunology |
| Volume | 14 |
| Issue number | 7 |
| DOIs | |
| Publication status | Published - 2013 |
Cite this
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Targeting of a natural killer cell receptor family by a viral immunoevasin. / Berry, Richard; Ng, Natasha May-Yoke; Saunders, Philippa M; Vivian, Julian; Lin, Jie; Deuss, Felix; Corbett, Alexandra; Forbes, Catherine A; Widjaja, Jacqueline ML; Sullivan, Lucy Catherine; McAlister, Adrian Dale; Perugini, Matthew Anthony; Call, Melissa J; Scalzo, Anthony A; Degli-Esposti, Mariapia; Coudert, Jerome D; Beddoe, Travis Clarke; Brooks, Andrew; Rossjohn, Jamie.
In: Nature Immunology, Vol. 14, No. 7, 2013, p. 699 - 707.Research output: Contribution to journal › Article › Research › peer-review
TY - JOUR
T1 - Targeting of a natural killer cell receptor family by a viral immunoevasin
AU - Berry, Richard
AU - Ng, Natasha May-Yoke
AU - Saunders, Philippa M
AU - Vivian, Julian
AU - Lin, Jie
AU - Deuss, Felix
AU - Corbett, Alexandra
AU - Forbes, Catherine A
AU - Widjaja, Jacqueline ML
AU - Sullivan, Lucy Catherine
AU - McAlister, Adrian Dale
AU - Perugini, Matthew Anthony
AU - Call, Melissa J
AU - Scalzo, Anthony A
AU - Degli-Esposti, Mariapia
AU - Coudert, Jerome D
AU - Beddoe, Travis Clarke
AU - Brooks, Andrew
AU - Rossjohn, Jamie
PY - 2013
Y1 - 2013
N2 - Activating and inhibitory receptors on natural killer (NK) cells have a crucial role in innate immunity, although the basis of the engagement of activating NK cell receptors is unclear. The activating receptor Ly49H confers resistance to infection with murine cytomegalovirus by binding to the immunoevasin m157. We found that m157 bound to the helical stalk of Ly49H, whereby two m157 monomers engaged the Ly49H dimer. The helical stalks of Ly49H lay centrally across the m157 platform, whereas its lectin domain was not required for recognition. Instead, m157 targeted an aromatic peg motif present in stalks of both activating and inhibitory receptors of the Ly49 family, and substitution of this motif abrogated binding. Furthermore, ligation of m157 to Ly49H or Ly49C resulted in intracellular signaling. Accordingly, m157 has evolved to tackle the legs of a family of NK cell receptors.
AB - Activating and inhibitory receptors on natural killer (NK) cells have a crucial role in innate immunity, although the basis of the engagement of activating NK cell receptors is unclear. The activating receptor Ly49H confers resistance to infection with murine cytomegalovirus by binding to the immunoevasin m157. We found that m157 bound to the helical stalk of Ly49H, whereby two m157 monomers engaged the Ly49H dimer. The helical stalks of Ly49H lay centrally across the m157 platform, whereas its lectin domain was not required for recognition. Instead, m157 targeted an aromatic peg motif present in stalks of both activating and inhibitory receptors of the Ly49 family, and substitution of this motif abrogated binding. Furthermore, ligation of m157 to Ly49H or Ly49C resulted in intracellular signaling. Accordingly, m157 has evolved to tackle the legs of a family of NK cell receptors.
UR - http://www.nature.com/ni/journal/v14/n7/pdf/ni.2605.pdf
U2 - 10.1038/ni.2605
DO - 10.1038/ni.2605
M3 - Article
VL - 14
SP - 699
EP - 707
JO - Nature Immunology
JF - Nature Immunology
SN - 1529-2908
IS - 7
ER -