Mus m 1.0102 is a member of the mouse Major Urinary Protein family, belonging to the Lipocalins superfamily. Major Urinary Proteins (MUPs) are characterized by highly conserved structural motifs. These include a disulphide bond, involved in protein oxidative folding and protein structure stabilization, and a free cysteine residue, substituted by serine only in the pheromonal protein Darcin (MUP20). The free cysteine is recognized as responsible for the onset of inter- or intramolecular thiol/disulphide exchange, an event that favours protein aggregation. Here we show that the substitution of selected cysteine residues modulates Mus m 1.0102 protein folding, fold stability and unfolding reversibility, while maintaining its allergenic potency. Recombinant allergens used for immunotherapy or employed in allergy diagnostic kits require, as essential features, conformational stability, sample homogeneity and proper immunogenicity. In this perspective, recombinant Mus m 1.0102 might appear reasonably adequate as lead molecule because of its allergenic potential and thermal stability. However, its modest resistance to aggregation renders the protein unsuitable for pharmacological preparations. Point mutation is considered a winning strategy. We report that, among the tested mutants, C138A mutant acquires a structure more resistant to thermal stress and less prone to aggregation, two events that act positively on the protein shelf life. Those features make that MUP variant an attractive lead molecule for the development of a diagnostic kit and/or a vaccine.

中文翻译：

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过敏原Mus m 1.0102：半胱氨酸残基和分子过敏学。

Mus m 1.0102是小鼠主要泌尿蛋白家族的成员，属于Lipocalins超家族。主要尿蛋白（MUPs）的特征是高度保守的结构基序。这些包括参与蛋白质氧化折叠和蛋白质结构稳定化的二硫键，以及仅在信息素蛋白质Darcin（MUP20）中被丝氨酸取代的游离半胱氨酸残基。游离的半胱氨酸被认为是引起分子间或分子内硫醇/二硫化物交换的原因，这种事件有利于蛋白质聚集。在这里，我们显示了所选半胱氨酸残基的取代可调节Mus m 1.0102蛋白的折叠，折叠稳定性和展开可逆性，同时保持其变应原力。用于免疫疗法或用于过敏诊断试剂盒的重组变应原，作为基本特征，构象稳定性，样品均一性和适当的免疫原性。从这个角度来看，重组Mus m 1.0102可能由于其潜在的致敏性和热稳定性而足以作为先导分子。但是，其适度的抗聚集性使该蛋白质不适合用于药物制剂。点突变被认为是制胜法宝。我们报告说，在测试的突变体中，C138A突变体获得了对热应激更具抗性且更不易于聚集的结构，这两个事件对蛋白质的保质期具有积极作用。这些特征使MUP变体成为开发诊断试剂盒和/或疫苗的有吸引力的先导分子。0102由于具有潜在的致敏性和热稳定性，因此可以合理地用作铅分子。但是，其适度的抗聚集性使该蛋白质不适合用于药物制剂。点突变被认为是制胜法宝。我们报告说，在测试的突变体中，C138A突变体获得了对热应激更具抗性且更不易于聚集的结构，这两个事件对蛋白质的保质期具有积极作用。这些特征使MUP变体成为开发诊断试剂盒和/或疫苗的有吸引力的先导分子。0102由于具有潜在的致敏性和热稳定性，因此可以合理地用作铅分子。但是，其适度的抗聚集性使该蛋白质不适合用于药物制剂。点突变被认为是制胜法宝。我们报告说，在测试的突变体中，C138A突变体获得了对热应激更具抗性且更不易于聚集的结构，这两个事件对蛋白质的保质期具有积极作用。这些特征使MUP变体成为开发诊断试剂盒和/或疫苗的有吸引力的先导分子。我们报告说，在测试的突变体中，C138A突变体获得了对热应激更具抗性且更不易于聚集的结构，这两个事件对蛋白质的保质期具有积极作用。这些特征使MUP变体成为开发诊断试剂盒和/或疫苗的有吸引力的先导分子。我们报告说，在测试的突变体中，C138A突变体获得了对热应激更具抗性且更不易于聚集的结构，这两个事件对蛋白质的保质期具有积极作用。这些特征使MUP变体成为开发诊断试剂盒和/或疫苗的有吸引力的先导分子。