Lipooligosaccharide (LOS Sample Clauses

Lipooligosaccharide (LOS. In Gram-negative bacteria, lipopolysaccharide (LPS) is a major component of the outer membrane that contributes to the stability of the cell membrane, increases the overall net negative charge of the organism, and protects the membrane from certain types of chemical attack. Gonococcoal lipooligosaccharide (LOS) is anchored to the bacterial cell wall membrane via lipid A and differs from LPS in that it lacks the long repeating O antigen; instead, the side chain consists of three short chains named α, β, and γ (28). The 7 gonococcal glycosyltransferases encoded by 3 chromosomal loci comprise the genes involved in LOS biosynthesis. The highly conserved gonococcal glycosyltransferase genes lgtA, lgtC, lgtD, and lgtG undergo phase variation due to slipped-strand base mispairing that occurs at homopolymeric G tracts, and as a result, gonococci can express more than one antigenically distinct LOS on their cell surface at one time (11, 217, 221). Variations in sialylation of LOS by the lst gene, which encodes for α-2,3-sialyltransferase, also lead to mutability among gonococcal LOS types, leading to improved protection from polymorphonuclear leukocyte (PMN) killing (124). It has been well established that phase and antigenic variation along with sialylation of gonococcal LOS plays an important role in establishment of an infection and immune evasion (11, 172, 193). Variations in gonococcal LOS can result in a less effective adaptive immune response by limiting surface exposed antigens available for antibody recognition (201). Changes in LOS structure, due to phase variation in lgtA, lgtC, or lgtD also modulate gonococcal susceptibility to normal human serum (NHS), greatly impacting the ability of gonococci to resist host defense factors (180). Modifications to gonococcal LOS can also occur through the addition of phosphoethanolamine (PEA) to not only the core oligosaccharide but also lipid A (13, 41, 123, 148, 215). The enzyme phosphoethanolamine transferase that is responsible for adding a positively charged PEA to the 4′position of lipid A is encoded by lptA (41). Recently it has been demonstrated that disruption of lptA expression increases gonococcal susceptibility not only to the cationic antimicrobial peptide polymixin B, but also to complement-mediated killing by NHS thus further influencing the interplay between the gonococcus and host defense mechanisms (111).
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