Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding
LC Walters, K Harlos, S Brackenridge… - Nature …, 2018 - nature.com
Through major histocompatibility complex class Ia leader sequence-derived (VL9) peptide
binding and CD94/NKG2 receptor engagement, human leucocyte antigen E (HLA-E) reports
cellular health to NK cells. Previous studies demonstrated a strong bias for VL9 binding by
HLA-E, a preference subsequently supported by structural analyses. However, Mycobacteria
tuberculosis (Mtb) infection and Rhesus cytomegalovirus-vectored SIV vaccinations
revealed contexts where HLA-E and the rhesus homologue, Mamu-E, presented diverse …
binding and CD94/NKG2 receptor engagement, human leucocyte antigen E (HLA-E) reports
cellular health to NK cells. Previous studies demonstrated a strong bias for VL9 binding by
HLA-E, a preference subsequently supported by structural analyses. However, Mycobacteria
tuberculosis (Mtb) infection and Rhesus cytomegalovirus-vectored SIV vaccinations
revealed contexts where HLA-E and the rhesus homologue, Mamu-E, presented diverse …
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