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首页> 美国卫生研究院文献>Proceedings of the National Academy of Sciences of the United States of America >Naturally processed peptides from two disease-resistance-associated HLA-DR13 alleles show related sequence motifs and the effects of the dimorphism at position 86 of the HLA-DR beta chain.
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Naturally processed peptides from two disease-resistance-associated HLA-DR13 alleles show related sequence motifs and the effects of the dimorphism at position 86 of the HLA-DR beta chain.

机译：来自两个与疾病抗性相关的HLA-DR13等位基因的天然加工肽显示相关的序列基序并且在HLA-DR beta链的86位具有双态性。

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摘要

HLA-DR13 has been associated with resistance to two major infectious diseases of humans. To investigate the peptide binding specificity of two HLA-DR13 molecules and the effects of the Gly/Val dimorphism at position 86 of the HLA-DR beta chain on natural peptide ligands, these peptides were acid-eluted from immunoaffinity-purified HLA-DRB1*1301 and -DRB1*1302, molecules that differ only at this position. The eluted peptides were subjected to pool sequencing or individual peptide sequencing by tandem MS or Edman microsequencing. Sequences were obtained for 23 peptides from nine source proteins. Three pool sequences for each allele and the sequences of individual peptides were used to define binding motifs for each allele. Binding specificities varied only at the primary hydrophobic anchor residue, the differences being a preference for the aromatic amino acids Tyr and Phe in DRB1*1302 and a preference for Val in DRB1*1301. Synthetic analogues of the eluted peptides showed allele specificity in their binding to purified HLA-DR, and Ala-substituted peptides were used to identify the primary anchor residues for binding. The failure of some peptides eluted from DRB1*1302 (those that use aromatic amino acids as primary anchors) to bind to DRB1*1301 confirmed the different preferences for peptide anchor residues conferred by the Gly-->Val change at position 86. These data suggest a molecular basis for the differential associations of HLA-DRB1*1301 and DRB1*1302 with resistance to severe malaria and clearance of hepatitis B virus infection.
机译：HLA-DR13与人类两种主要传染病的抗性相关。为了研究两个HLA-DR13分子的肽结合特异性以及HLA-DRβ链第86位的Gly / Val二态性对天然肽配体的影响，从免疫亲和纯化的HLA-DRB1 *中酸洗脱了这些肽1301和-DRB1 * 1302是仅在此位置不同的分子。通过串联MS或Edman微测序对洗脱的肽进行合并测序或单个肽测序。从九种来源蛋白中获得了23种肽的序列。每个等位基因的三个合并序列和单个肽的序列用于定义每个等位基因的结合基序。结合特异性仅在主要的疏水锚残基处变化，差异是在DRB1 * 1302中优先选择芳香族氨基酸Tyr和Phe，在DRB1 * 1301中优先选择Val。洗脱肽的合成类似物在与纯化的HLA-DR的结合中显示等位基因特异性，Ala取代的肽用于鉴定结合的主要锚残基。从DRB1 * 1302洗脱的某些肽（那些使用芳香族氨基酸作为主要锚点的肽）未能结合到DRB1 * 1301，这证实了在86位的Gly-> Val改变赋予了肽锚点残基的不同偏好。这些数据提示HLA-DRB1 * 1301和DRB1 * 1302与对严重疟疾的抵抗力和清除乙型肝炎病毒感染的差异关联的分子基础。

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