Bentley G A
Unité d'Immunologie Structurale, C.N.R.S. URA 1961, Department d'Immunologie, Institut Pasteur, Paris, France.
EXS. 1996;75:301-19. doi: 10.1007/978-3-0348-9225-4_16.
Type c lysozymes, and hen egg lysozyme in particular, have been extensively used to study the immune response because of their strong immunogenicity, the availability of many natural variants to study cross-reactivity, and the possibility to correlate these results with the known three-dimensional structure of lysozymes from several species. To date, the structure of six different murine monoclonal anti-lysozyme antibodies has been studied as a complex between the Fab fragment and antigen. In some cases, the structure of the uncomplexed Fab is also available, giving detail at the atomic level of the changes which take place during the formation of the antibody-antigen complex. The bacterially-expressed Fv molecule, the simplest fragment of an immunoglobulin retaining an intact antigen-binding site, has been studied for three of the monoclonal anti-lysozyme antibodies. Recombinant Fv fragments have opened up the possibility of using site-directed mutagenesis to study the effect of amino acid changes at the antibody-antigen interface. The six monoclonal antibodies appear to recognize epitopes which are localised on three different regions of the lysozyme surface.
C型溶菌酶，尤其是鸡蛋清溶菌酶，因其强大的免疫原性、存在许多可用于研究交叉反应性的天然变体，以及能够将这些结果与几种物种溶菌酶已知的三维结构相关联，而被广泛用于研究免疫反应。迄今为止，已研究了六种不同的鼠源单克隆抗溶菌酶抗体与Fab片段和抗原形成的复合物的结构。在某些情况下，也可获得未结合抗原的Fab的结构，这在原子水平上详细揭示了抗体-抗原复合物形成过程中发生的变化。已对三种单克隆抗溶菌酶抗体研究了细菌表达的Fv分子，它是免疫球蛋白中保留完整抗原结合位点的最简单片段。重组Fv片段为利用定点诱变研究抗体-抗原界面氨基酸变化的影响开辟了可能性。这六种单克隆抗体似乎识别位于溶菌酶表面三个不同区域的表位。
