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C3 binds preferentially to long-chain lipopolysaccharide during alternative pathway activation by Salmonella montevideo

Journal Article · · J. Immunol.; (United States)
OSTI ID:6778305
The population of LPS molecules on Salmonella montevideo that bind C3 during alternative pathway activation in serum was studied. LPS molecules of Salmonella are composed of lipid A:core oligosaccharide (one copy per molecule), substituted by an O-polysaccharide (O-PS) side chain, which is a linear polymer of 0 to >60 O-antigen repeat units containing mannose. A mutant of S. montevideo called SL5222 that inserts galactose only into core oligosaccharide and mannose only into O-antigen sub-units was grown with (/sup 3/H)mannose and (/sup 14/C)galactose, so that LPS molecules bearing large numbers of O-antigen subunits have high /sup 3/H to /sup 14/C ratios, whereas molecules with few O-antigen subunits have lower /sup 3/H to /sup 14/C ratios. The authors postulate that preferential attachment of C3 to long-chain LPS in SL5222 results because long-chain LPS molecules sterically hinder shorter chain LPS molecules from macromolecules. This study provides direct proof that the O-PS of LPS sterically hinders access of large molecules to the outer membrane and indicates that the LPS coat of these bacteria functions as a barrier against large protein molecules.
Research Organization:
National Institutes of Health, Bethesda, MD
OSTI ID:
6778305
Journal Information:
J. Immunol.; (United States), Journal Name: J. Immunol.; (United States) Vol. 136:2; ISSN JOIMA
Country of Publication:
United States
Language:
English