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首页> 外文期刊>Infection and immunity >Synthetic Peptide Immunogens Elicit Polyclonal and Monoclonal Antibodies Specific for Linear Epitopes in the D Motifs ofStaphylococcus aureus Fibronectin-Binding Protein, Which Are Composed of Amino Acids That Are Essential for Fibronectin Binding
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Synthetic Peptide Immunogens Elicit Polyclonal and Monoclonal Antibodies Specific for Linear Epitopes in the D Motifs ofStaphylococcus aureus Fibronectin-Binding Protein, Which Are Composed of Amino Acids That Are Essential for Fibronectin Binding

机译：合成肽免疫原引起对金黄色葡萄球菌纤连蛋白结合蛋白D母题的线性表位特异的多克隆和单克隆抗体，这些蛋白由纤连蛋白结合必不可少的氨基酸组成

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A fibronectin (Fn)-binding adhesin of Staphylococcus aureus contains three tandem 37- or 38-amino-acid motifs (D1, D2, and D3), which function to bind Fn. Plasma from patients with S. aureus infections contain antibodies that preferentially recognize ligand induced binding sites in the D motifs and do not inhibit Fn binding (F. Casolini, L. Visai, D. Joh, P. G. Conaldi, A. Toniolo, M. H??k, and P. Speziale, Infect. Immun. 66:5433–5442, 1998). To eliminate the influence of Fn binding on antibody development, we used synthetic peptide immunogens D121–34 and D320–33, which each contain a conserved pattern of amino acids that is essential for Fn binding but which cannot bind Fn without N- or C-terminal extensions. The D320–33 immunogen promoted the production of polyclonal antibodies that were 10-fold more effective as inhibitors of Fn-binding to the D3 motif than antibodies obtained by immunizing with an extended peptide D316–36, which exhibits functional Fn binding. The D320–33 immunogen also facilitated the production of a monoclonal antibody, 9C3, which was highly specific for the epitope SVDFEED, and abolished Fn binding by the D3 motif. When mixed with polyclonal anti-D121–34 immunoglobulin G, 70% inhibition of Fn binding to the three tandem D motifs was achieved compared to no more than 30% inhibition with either antibody preparation alone. Therefore, by immunizing with short synthetic peptides that are unable to bind Fn, we have effectively stimulated the production of antibodies specific for epitopes comprised of amino acids that are essential for Fn binding. Although these epitopes occur within a conserved pattern of amino acids that is required for Fn binding, the antibodies recognized specific linear epitope sequences and not a conserved structure common to all repeated motifs.
机译：金黄色葡萄球菌的纤连蛋白（Fn）结合粘附素包含三个串联的37或38个氨基酸基序（D1，D2和D3），其功能是结合Fn。来自金黄色葡萄球菌感染患者的血浆包含的抗体可优先识别D基序中配体诱导的结合位点，并且不抑制Fn结合（F.Casolini，L.Viasi，D.Joh，PG Conaldi，A.Toniolo，M.H K，和P. Speziale，《感染免疫》 66：5433-5442，1998年）。为了消除Fn结合对抗体发育的影响，我们使用了合成肽免疫原D121-34和D320-33，它们各自包含保守的氨基酸模式，这对于Fn结合是必不可少的，但是如果没有N-或C-就不能结合Fn终端扩展。 D320-33免疫原促进了多克隆抗体的产生，这种抗体比起用功能性Fn结合的扩展肽D316-36进行免疫获得的抗体，其作为Fn结合D3基序的抑制剂的效力高10倍。 D320-33免疫原还促进了单克隆抗体9C3的产生，该抗体对表位SVDFEED具有高度特异性，并通过D3基序消除了Fn的结合。当与多克隆抗D121-34免疫球蛋白G混合时，与任何一种抗体制剂相比，对Fn结合三个串联D基序的抑制作用达到70％的抑制率。因此，通过用不能结合Fn的短的合成肽进行免疫，我们有效地刺激了特异性针对由Fn结合必不可少的氨基酸组成的表位的抗体的产生。尽管这些表位出现在Fn结合所需的氨基酸保守模式内，但抗体识别特定的线性表位序列，而不是所有重复基序共有的保守结构。

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