Anti-Salmonella typhimurium LPS antibody [1E6]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Salmonella typhimurium LPS also known as lipopolysaccharide forms a vital component of the outer membrane of Gram-negative bacteria such as Salmonella. This complex molecule consists of a lipid A domain a core oligosaccharide and an O-antigen polysaccharide chain. The lipid A component with an estimated mass of roughly 10 kDa is the main contributor to LPS endotoxin activity. In Salmonella the LPS is expressed in the bacterial cell wall providing structural integrity and defense against environmental stresses. Its composition varies among different Salmonella strains influencing the bacterium's virulence and interaction with host immune systems.

Biological function summary

Salmonella typhimurium LPS engages in stimulating immune responses. An important part of the LPS structure the lipid A moiety activates the innate immune system by binding to Toll-like receptor 4 (TLR4) on host immune cells. This interaction triggers a cascade of pro-inflammatory cytokine production. As part of the outer membrane of Salmonella LPS works in synergy with other membrane proteins to form the protective barrier for the bacteria. The variability in the O-antigen portion aids in evasion of host immune responses allowing different Salmonella serotypes to survive and cause infection.

Pathways

The response of TLR4 to Salmonella typhimurium LPS forms a central axis in innate immune signaling. This pathway activates NF-kB a transcription factor pivotal in inducing cytokine genes thereby intensifying the antibacterial response. LPS interactions not only involve TLR4 but also influence pathways such as the MAPK signaling cascade further regulating immune responses. These pathways ensure rapid immune mobilization to control bacterial infections highlighting the significant role LPS plays in pathogen-host interactions.

Associated diseases and disorders

Salmonella typhimurium LPS remains an important factor in the pathogenesis of salmonellosis and septic shock. LPS as a potent endotoxin contributes to systemic inflammation during septicemia by over-activating the immune system. Its interaction with TLR4 leads to high levels of inflammatory cytokines resulting in symptoms associated with both intestinal and systemic infections. The molecular attributes of LPS particularly lipid A connect to disease outcomes and also offer potential targets for therapeutic intervention in controlling severe inflammatory responses during Salmonella infections.