Mazmanian S K, Liu G, Ton-That H, Schneewind O
Department of Microbiology and Immunology, UCLA School of Medicine, University of California, 10833 Le Conte Avenue, Los Angeles, CA 90095, USA.
Science. 1999 Jul 30;285(5428):760-3. doi: 10.1126/science.285.5428.760.
Surface proteins of Gram-positive bacteria are linked to the bacterial cell wall by a mechanism that involves cleavage of a conserved Leu-Pro-X-Thr-Gly (LPXTG) motif and that occurs during assembly of the peptidoglycan cell wall. A Staphylococcus aureus mutant defective in the anchoring of surface proteins was isolated and shown to carry a mutation in the srtA gene. Overexpression of srtA increased the rate of surface protein anchoring, and homologs of srtA were found in other pathogenic Gram-positive bacteria. The protein specified by srtA, sortase, may be a useful target for the development of new antimicrobial drugs.
革兰氏阳性菌的表面蛋白通过一种机制与细菌细胞壁相连,该机制涉及保守的亮氨酸 - 脯氨酸 - X - 苏氨酸 - 甘氨酸(LPXTG)基序的切割,且发生在肽聚糖细胞壁组装过程中。分离出一株表面蛋白锚定存在缺陷的金黄色葡萄球菌突变体,并显示其srtA基因发生了突变。srtA的过表达提高了表面蛋白锚定的速率,并且在其他致病性革兰氏阳性菌中也发现了srtA的同源物。由srtA指定的蛋白质分选酶可能是开发新型抗菌药物的一个有用靶点。