Complexity of lipopolysaccharide modifications in Salmonella enterica: Its effects on endotoxin activity, membrane permeability, and resistance to antimicrobial peptides
- 作者：Kiyoshi Kawasaki ; kkawasak@dwc.doshisha.ac.jp
- 关键词：S. Typhimurium ; Salmonella enterica serovar Typhimurium ; TLR ; toll-like receptor ; LPS ; lipopolysaccharide ; MD2 ; myeloid differentiation factor 2 ; CAMPs ; cationic antimicrobial peptides ; Aminoarabinose ; 4-amino-4-deoxy-L-arabinose ; MPL ; 4&prime ; -monophospo
- 刊名：Food Research International
- 出版年：2012
- 期刊代码：53_09639969
- 类别：abs
- 出版时间：March, 2012
- 卷：45
- 期：2
- 页码：493-501
- 文件大小：475 K
摘要
Pathogenic bacteria must adapt to host tissues to establish a persistent infection and cause disease. Salmonella enterica serovar Typhimurium remodels its lipopolysaccharide, including the lipid A portion, to adapt to its environment, including host tissues. This remodeling is beneficial for Salmonella because it increases resistance to antimicrobial peptides, produces a robust permeation barrier in the outer membrane, and evades host immune surveillance. Lipid A modifications are regulated at both the transcriptional level and post-translational level. Regulations at the transcriptional level are studied well, and the two-component signal transduction system PhoP-PhoQ plays a central role. Most genes involved in lipid A modifications are under the control of PhoP-PhoQ. In contrast, post-translational regulations are poorly understood, but lipid A modifications appear to affect the enzymes that catalyze other lipid A modifications. Several post-translational regulations, including lipid A deacylation by the outer membrane enzyme PagL, can occur and these complex regulations constitute an emerging notion of the complexity of lipid A modifications. This review aims to describe the role of lipid A modifications in Salmonella pathogenesis and examine how their complexity affects pathogenesis.