Genetic control of the immune response to myoglobin. V. Analysis of the cross-reactivity of 12 myoglobins with sperm-whale myoglobin antisera of inbred mouse strains in terms of substitutions in the antigenic sites and in the environmental residues of the sites.

Genetic control of the immune response to myoglobin. V. Analysis of the cross-reactivity of 12 myoglobins with sperm-whale myoglobin antisera of inbred mouse strains in terms of substitutions in the antigenic sites and in the environmental residues of the sites.
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对肌红蛋白免疫反应的遗传控制。

DOI:
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发表时间:
1981
期刊:
Immunological Communications
影响因子:
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通讯作者:
C. David
C. David
中科院分区:
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文献类型:
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作者:
M. Atassi;Sally S. Twining;Hermann Lehmann;C. David

文献摘要

被引文献

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肌红蛋白整个抗原结构的确定,使人们有可能把注意力集中在控制和影响免疫识别的分子因素。最近,使用抗血清提出的抹香鲸肌红蛋白(Mb)在6个不同的宿主物种,并调查他们的反应与Mb从15个物种,我们表明,抗原位点的结合能力的影响,取代内的位点残基以及内的残基接近(6.0 μ m)的网站。基于这些效果,至少在定性方面,有可能关联的预期效果的替代在每个Mb和其观察到的交叉反应与抗血清抹香鲸Mb。在目前的工作中,这些相关性进行了测试,使用抹香鲸Mb抗体提出的四个近交系小鼠品系,其中针对每个抗原位点的抗体的量进行了测定。测定125I标记的抗体的量,其可以最大限度地结合12 Mb变体中的每一种。由于遗传控制,对某些抗原位点的反应没有表达,因此使我们能够以很高的置信度评估各种肌红蛋白中氨基酸替换对位点反应性的影响。根据这些考虑,预期每个Mb变体的交叉反应值与实验发现的值一致。结果明确证实,影响蛋白质交叉反应的主要因素可归因于位点内和位点环境残留物内的取代。
The determination of the entire antigenic structure of myoglobin has made it possible to focus attention on the molecular factors controlling and influencing immune recognition. Recently, using antisera raised against sperm-whale myoglobin (Mb) in six different host species and investigating their reactions with Mb from 15 species, we showed that the binding capacity of an antigenic site is influenced by substitutions within site residues as well as within the residues close (within 6.0 å) to the sites. Based on these effects it was possible to correlate, at least in qualitative terms, the expected effects of the substitutions in each Mb and its observed cross-reaction with antisera to sperm-whale Mb. In the present work, these correlations were tested using sperm-whale Mb antibodies raised in four inbred mouse strains and in which the amount of antibodies directed to each antigenic site was determined. The amounts of 125I-labelled antibodies that could be bound maximally be each of 12 Mb variants were determined. Because of genetic control, the response to some antigenic sites was not expressed and therefore permitted us to evaluate with a good degree of confidence the effects of amino acid replacements in various myoglobins upon the reactivity of the sites. The values of cross-reaction expected for each Mb variant from these considerations agreed well with the values found experimentally. The results confirm unambiguously that the major factors affecting the cross-reactions of proteins can be attributed to substitutions within the sites and within environmental residues of the sites.