Manczinger Máté, Kemény Lajos
Department of Dermatology and Allergology, University of Szeged, Szeged, Hungary.
MTA-SZTE Dermatological Research Group, University of Szeged, Szeged, Hungary.
PeerJ. 2018 Jul 3;6:e5118. doi: 10.7717/peerj.5118. eCollection 2018.
HLA class II proteins are important elements of human adaptive immune recognition and are associated with numerous infectious and immune-mediated diseases. These highly variable molecules can be classified into DP, DQ and DR groups. It has been proposed that in contrast with DP and DR, epitope binding by DQ variants rather results in immune tolerance. However, the pieces of evidence are limited and controversial. We found that DQ molecules bind more human epitopes than DR. Pathogen-associated epitopes bound by DQ molecules are more similar to human proteins than the ones bound by DR. Accordingly, DQ molecules bind epitopes of significantly different pathogen species. Moreover, the binding of autoimmunity-associated epitopes by DQ confers protection from autoimmune diseases. Our results suggest a special role of HLA-DQ in immune homeostasis and help to better understand the association of HLA molecules with infectious and autoimmune diseases.
人类白细胞抗原（HLA）II类蛋白是人类适应性免疫识别的重要组成部分，与多种感染性疾病和免疫介导疾病相关。这些高度可变的分子可分为DP、DQ和DR组。有人提出，与DP和DR不同，DQ变体结合表位反而会导致免疫耐受。然而，相关证据有限且存在争议。我们发现，DQ分子比DR分子能结合更多的人类表位。与DR分子结合的病原体相关表位相比，DQ分子结合的病原体相关表位与人类蛋白质更相似。因此，DQ分子结合的是明显不同病原体种类的表位。此外，DQ结合自身免疫相关表位可预防自身免疫性疾病。我们的研究结果表明HLA - DQ在免疫稳态中具有特殊作用，有助于更好地理解HLA分子与感染性疾病和自身免疫性疾病的关联。
