Defining the structural basis for human alloantibody binding to human leukocyte antigen allele HLA-A*11:01

Yue Gu, Yee Hwa Wong, Chong Wai Liew, Conrad E. Z. Chan, Tanusya M. Murali, Jiawei Yap, Chien Tei Too, Kiren Purushotorman, Maryam Hamidinia, Abbas El Sahili, Angeline T. H. Goh, Rachel Z. C. Teo, Kathryn J. Wood, Brendon J. Hanson, Nicholas R. J. Gascoigne, Julien Lescar (), Anantharaman Vathsala () and Paul A. MacAry ()
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Yue Gu: National University of Singapore
Yee Hwa Wong: Nanyang Technological University
Chong Wai Liew: Nanyang Technological University
Conrad E. Z. Chan: DSO National Laboratories
Tanusya M. Murali: National University of Singapore
Jiawei Yap: National University of Singapore
Chien Tei Too: National University of Singapore
Kiren Purushotorman: National University of Singapore
Maryam Hamidinia: National University of Singapore
Abbas El Sahili: Nanyang Technological University
Angeline T. H. Goh: National University Hospital
Rachel Z. C. Teo: National University Hospital
Kathryn J. Wood: University of Oxford
Brendon J. Hanson: DSO National Laboratories
Nicholas R. J. Gascoigne: National University of Singapore
Julien Lescar: Nanyang Technological University
Anantharaman Vathsala: National University Hospital
Paul A. MacAry: National University of Singapore

Nature Communications, 2019, vol. 10, issue 1, 1-11

Abstract: Abstract Our understanding of the conformational and electrostatic determinants that underlie targeting of human leukocyte antigens (HLA) by anti-HLA alloantibodies is principally based upon in silico modelling. Here we provide a biochemical/biophysical and functional characterization of a human monoclonal alloantibody specific for a common HLA type, HLA-A*11:01. We present a 2.4 Å resolution map of the binding interface of this antibody on HLA-A*11:01 and compare the structural determinants with those utilized by T-cell receptor (TCR), killer-cell immunoglobulin-like receptor (KIR) and CD8 on the same molecule. These data provide a mechanistic insight into the paratope−epitope relationship between an alloantibody and its target HLA molecule in a biological context where other immune receptors are concomitantly engaged. This has important implications for our interpretation of serologic binding patterns of anti-HLA antibodies in sensitized individuals and thus, for the biology of human alloresponses.

Date: 2019
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DOI: 10.1038/s41467-019-08790-1

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