Geurtsen Jeroen, Steeghs Liana, Hamstra Hendrik-Jan, Ten Hove Jan, de Haan Alex, Kuipers Betsy, Tommassen Jan, van der Ley Peter
Netherlands Vaccine Institute, P.O. Box 457, 3720 AL Bilthoven, The Netherlands.
Infect Immun. 2006 Oct;74(10):5574-85. doi: 10.1128/IAI.00834-06.
Lipopolysaccharide (LPS) is one of the major constituents of the gram-negative bacterial cell envelope. Its endotoxic activity causes the relatively high reactogenicity of whole-cell vaccines. Several bacteria harbor LPS-modifying enzymes that modulate the endotoxic activity of the LPS. Here we evaluated whether two such enzymes, i.e., PagP and PagL, could be useful tools for the development of an improved and less reactogenic whole-cell pertussis vaccine. We showed that expression of PagP and PagL in Bordetella pertussis leads to increased and decreased endotoxic activity of the LPS, respectively. As expected, PagP activity also resulted in increased endotoxic activity of whole bacterial cells. However, more unexpectedly, this was also the case for PagL. This paradoxical result may be explained, in part, by an increased release of LPS, which we observed in the PagL-expressing cells.
脂多糖（LPS）是革兰氏阴性菌细胞壁包膜的主要成分之一。其内毒素活性导致全细胞疫苗具有相对较高的反应原性。几种细菌含有可调节LPS内毒素活性的LPS修饰酶。在此，我们评估了两种这样的酶，即PagP和PagL，是否可作为开发改良的、反应原性较低的全细胞百日咳疫苗的有用工具。我们发现，PagP和PagL在百日咳博德特氏菌中的表达分别导致LPS内毒素活性增加和降低。正如预期的那样，PagP活性也导致全细菌细胞的内毒素活性增加。然而，更出乎意料的是，PagL的情况也是如此。这一矛盾的结果可能部分是由于我们在表达PagL的细胞中观察到的LPS释放增加所致。
