Norrby E, Mufson M A, Alexander H, Houghten R A, Lerner R A
Proc Natl Acad Sci U S A. 1987 Sep;84(18):6572-6. doi: 10.1073/pnas.84.18.6572.
A set of 23 nested 15-amino-acid-long peptides with overlaps of 5 amino acids, representing the complete extramembranous part of the large glycoprotein G of respiratory syncytial (RS) virus, was analyzed in ELISA against different sera containing virus-specific antibodies. Seven of the peptides reacted with rabbit hyperimmune sera against purified virions. In contrast, only one of these seven peptides reacted with murine monoclonal antibodies specific for G. In connection with RS virus infections in humans, increase of antibody titers against three peptides was found in about one-third of the cases. These three peptides were included among those identified by both murine and rabbit antibodies. The present findings may open possibilities for site-directed clinical serology in the case of RS virus infections.
一组23个嵌套的、长度为15个氨基酸且有5个氨基酸重叠的肽段,代表呼吸道合胞(RS)病毒大糖蛋白G的完整膜外部分,针对含有病毒特异性抗体的不同血清进行了ELISA分析。其中七个肽段与抗纯化病毒粒子的兔超免疫血清发生反应。相比之下,这七个肽段中只有一个与针对G的鼠单克隆抗体发生反应。关于人类RS病毒感染,约三分之一的病例中发现针对三种肽段的抗体滴度升高。这三种肽段包含在鼠抗体和兔抗体都识别的肽段之中。目前的研究结果可能为RS病毒感染情况下的定点临床血清学研究开辟可能性。