Janvier B, Constantinidou C, Aucher P, Marshall Z V, Penn C W, Fauchère J L
Microbiologie A, CHU la Milétrie, Poitiers, France.
Res Microbiol. 1998 Feb;149(2):95-107. doi: 10.1016/s0923-2508(98)80025-9.
In order to study a 19-kDa protein (p19) of Campylobacter jejuni, we purified this protein to homogeneity from C. jejuni strain 81,176 by anion exchange chromatography. The molecular weight of the native protein is 19,000 daltons. P19 was found to be acidic with an isoelectric point of 4.8 and was located in the periplasmic space of the bacteria. The 20 N-terminal amino acids were sequenced and no significant similarities with known proteins were shown. A monoclonal antibody showed that p19 is conserved in the 2 species C. jejuni and C. coli. Analysis of sera from 23 patients with a Campylobacter-related infection indicated that p19 is not immunogenic during natural infection in man. The gene encoding p19 was cloned and no strong homologies with known sequences were identified. The preparation of a knockout mutant in p19 will enable the investigation of the function of this cell wall component of Campylobacter.
为了研究空肠弯曲菌的一种19-kDa蛋白（p19），我们通过阴离子交换色谱法从空肠弯曲菌81176菌株中纯化该蛋白至均一状态。天然蛋白的分子量为19,000道尔顿。发现p19呈酸性，等电点为4.8，位于细菌的周质空间。测定了其N端20个氨基酸的序列，未显示与已知蛋白有明显相似性。一种单克隆抗体表明p19在空肠弯曲菌和大肠弯曲菌这两个菌种中是保守的。对23例空肠弯曲菌相关感染患者的血清分析表明，p19在人类自然感染期间不具有免疫原性。克隆了编码p19的基因，未发现与已知序列有强同源性。制备p19基因敲除突变体将有助于研究空肠弯曲菌这种细胞壁成分的功能。
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