Neisserial lipooligosaccharide is a target for complement component C4b: inner core phosphoethanolamine residues define C4b linkage specificity
S Ram, AD Cox, JC Wright, U Vogel, S Getzlaff… - Journal of Biological …, 2003 - ASBMB
We identified Neisseria meningitidis lipooligosaccharide (LOS) as an acceptor for
complement component C4b (C4b). Phosphoethanolamine (PEA) residues on the second
heptose (HepII) residue in the LOS core structure formed amide linkages with C4b. PEA at
the 6-position of HepII (6-PEA) was more efficient than 3-PEA in binding C4b. Strains
bearing 6-PEA bound more C4b than strains with 3-PEA and were more susceptible to
complement-mediated killing in serum bactericidal assays. Deleting 3-PEA from a strain that …
complement component C4b (C4b). Phosphoethanolamine (PEA) residues on the second
heptose (HepII) residue in the LOS core structure formed amide linkages with C4b. PEA at
the 6-position of HepII (6-PEA) was more efficient than 3-PEA in binding C4b. Strains
bearing 6-PEA bound more C4b than strains with 3-PEA and were more susceptible to
complement-mediated killing in serum bactericidal assays. Deleting 3-PEA from a strain that …
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