Amino acid sequences in the alpha 1 domain and not glycosylation are important in HLA-A2/beta 2-microglobulin association and cell surface expression.

J Santos-Aguado; P A Biro; U Fuhrmann; J L Strominger; J A Barbosa

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Amino acid sequences in the alpha 1 domain and not glycosylation are important in HLA-A2/beta 2-microglobulin association and cell surface expression.

机译：α1结构域中的氨基酸序列和不是糖基化在HLA-A2 /β2-微球蛋白结合和细胞表面表达中是重要的。

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The role of the single carbohydrate moiety present on the HLA-A2 molecule was studied by introducing several amino acid substitutions (by site-directed mutagenesis of the HLA-A2 gene) in the consensus glycosylation sequence Asn-X-Ser. Two different amino acid substitutions of the asparagine residue at position 86 (glutamine and aspartic acid) resulted in the synthesis of ca. 39,000-molecular-weight nonglycosylated heavy chains that were detected in the cytoplasm but not on the surface of mouse L-cell transfectants. However, a low level of surface expression was detected following transfection of human (rhabdomyosarcoma) cells or mouse L cells containing human beta 2-microglobulin. The defect in surface expression was not due to the absence of the glycan moiety, since the substitution of a glycine for a serine at amino acid 88 did not have the same drastic effect in the presence of human beta 2-microglobulin. These and other data suggest that the asparagine residue may play a critical role in the conformation of the HLA heavy chain and its interaction with beta 2-microglobulin. Immunofluorescence microscopy following permeabilization of the transfectants demonstrated that the unglycosylated HLA heavy chains are sequestered in an unidentified cellular compartment that is different from the Golgi structure.

机译：通过在共有糖基化序列Asn-X-Ser中引入几个氨基酸取代（通过HLA-A2基因的点定向诱变）来研究单一碳水化合物部分在HLA-A2分子上的作用。在86（谷氨酰胺和天冬氨酸）的两种不同氨基酸取代物在86（谷氨酰胺和天冬氨酸）中导致了CA的合成。在细胞质中检测到39,000分子量的核心化重链，但不在小鼠L细胞转染子表面上。然而，在含有人β2-微球蛋白的人（横纹肌肉瘤）细胞或小鼠L细胞转染后检测到低水平的表面表达。表面表达的缺陷不是由于甘共部分的存在，因为在氨基酸88处取代甘氨酸的丝氨酸在人β2-微球蛋白存在下没有相同的剧烈效果。这些和其他数据表明天冬酰胺残留物可以在HLA重链的构象中发挥关键作用及其与β2-微球蛋白的相互作用。转染剂的透明度后的免疫荧光显微镜表明，在不同于Golgi结构的未识别的细胞室中，将不缩粒子化的HLA重链隔离。

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《Molecular and Cellular Biology》 |1987年第3期|共9页
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J Santos-Aguado; P A Biro; U Fuhrmann; J L Strominger; J A Barbosa;
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1. Amino acid sequences in the alpha 1 domain and not glycosylation are important in HLA-A2/beta 2-microglobulin association and cell surface expression. [J] . J Santos-Aguado, P A Biro, U Fuhrmann, Molecular and Cellular Biology . 1987,第3期

机译：α1结构域中的氨基酸序列和不是糖基化在HLA-A2 /β2-微球蛋白结合和细胞表面表达中是重要的。
2. Amino acid sequences in the alpha 1 domain and not glycosylation are important in HLA-A2/beta 2-microglobulin association and cell surface expression. [J] . J Santos-Aguado, P A Biro, U Fuhrmann, Molecular and Cellular Biology . 1987,第3期

机译：α1结构域中的氨基酸序列和不是糖基化在HLA-A2 /β2-微球蛋白结合和细胞表面表达中是重要的。
3. Identification of amino acids within the second alpha helical domain of the human immunodeficiency virus type 1 Vpu that are critical for preventing CD4 cell surface expression. [J] . Hill MS, Ruiz A, Schmitt Virology . 2010,第1期

机译：鉴定人类免疫缺陷病毒1型Vpu的第二个alpha螺旋结构域内的氨基酸，这些氨基酸对于防止CD4细胞表面表达至关重要。
4. Designing of structures of peptides and proteins by introducing alpha , beta -dehydro-residues in the amino acid sequences [C] . Patel, H.C., Narula, Engineering in Medicine and Biology Society, 1989. Images of the Twenty-First Century., Proceedings of the Annual International Conference of the IEEE Engineering in . 1989

机译：通过在氨基酸序列中引入α，β-脱氢残基来设计肽和蛋白质的结构
5. Regulation of alpha7 nicotinic acetylcholine receptor function and pharmacology by amino acid sequence in the second transmembrane domain. [D] . Placzek, Andon Nicholas. 2005

机译：通过第二跨膜结构域中的氨基酸序列调节α7烟碱型乙酰胆碱受体功能和药理作用。
6. Amino acid sequences in the alpha 1 domain and not glycosylation are important in HLA-A2/beta 2-microglobulin association and cell surface expression. [O] . J Santos-Aguado, P A Biro, U Fuhrmann, 1987

机译：在HLA-A2 /β2-微球蛋白缔合和细胞表面表达中α1结构域中的氨基酸序列而不是糖基化非常重要。
7. Amino acid sequences in the alpha 1 domain and not glycosylation are important in HLA-A2/beta 2-microglobulin association and cell surface expression. [O] . Santos-Aguado, J, Biro, P A, Fuhrmann, U, 1987

机译：在HLA-A2 /β2-微球蛋白缔合和细胞表面表达中，α1结构域中的氨基酸序列而不是糖基化非常重要。

Amino acid sequences in the alpha 1 domain and not glycosylation are important in HLA-A2/beta 2-microglobulin association and cell surface expression.

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