D-alanine modification of a protease-susceptible outer membrane component by the Bordetella pertussis dra locus promotes resistance to antimicrobial peptides and polymorphonuclear leukocyte-mediated killing.
D-alanine modification of a protease-susceptible outer membrane component by the Bordetella pertussis dra locus promotes resistance to antimicrobial peptides and polymorphonuclear leukocyte-mediated killing.
复制标题
百日咳博德特氏菌 dra 位点对蛋白酶敏感的外膜成分进行 D-丙氨酸修饰，可促进对抗菌肽的耐药性和多形核白细胞介导的杀伤作用。
DOI：
10.1128/jb.00510-13
复制
发表时间：
2013
影响因子：
3.2
通讯作者：
Deora,Rajendar
中科院分区：
文献类型：
--
作者：
Taneja,NeetuKumra;Ganguly,Tridib;Bakaletz,LaurenO;Nelson,KimberlyJ;Dubey,Purnima;Poole,LeslieB;Deora,Rajendar
Bordetella pertussis is the causative agent of pertussis, a highly contagious disease of the human respiratory tract. Despite very high vaccine coverage, pertussis has reemerged as a serious threat in the United States and many developing countries. Thus, it is important to pursue research to discover unknown pathogenic mechanisms of B. pertussis. We have investigated a previously uncharacterized locus in B. pertussis, thedralocus, which is homologous to thedltoperons of Gram-positive bacteria. The absence of thedralocus resulted in increased sensitivity to the killing action of antimicrobial peptides (AMPs) and human phagocytes. Compared to the wild-type cells, the mutant cells bound higher levels of cationic proteins and peptides, suggesting thatdracontributes to AMP resistance by decreasing the electronegativity of the cell surface. The presence ofdraled to the incorporation ofd-alanine into an outer membrane component that is susceptible to proteinase K cleavage. We conclude thatdraencodes a virulence-associated determinant and contributes to the immune resistance of B. pertussis. With these findings, we have identified a new mechanism of surface modification in B. pertussis which may also be relevant in other Gram-negative pathogens.
