N-Linked Glycosylation at Asn(3) and the Positively Charged Residues within the Amino-Terminal Domain of the C1 Inhibitor Are Required for Interaction of the C1 Inhibitor with Salmonella enterica Serovar Typhimurium Lipopolysaccharide and Lipid A

The C1 inhibitor (C1INH), a plasma complement regulatory protein, prevents endotoxin shock, at least partially via the direct interaction of its amino-terminal heavily glycosylated nonserpin region with gram-negative bacterial lipopolysaccharide (LPS). To further characterize the potential LPS-bindi...

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Bibliographic Details
Main Authors: Liu, Dongxu, Cramer, Cort C., Scafidi, Jennifer, Davis, Alvin E.
Format: Artigo
Language:Inglês
Published: American Society for Microbiology 2005
Subjects:
Molecular Pathogenesis
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC1201182/
https://ncbi.nlm.nih.gov/pubmed/16040958
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/IAI.73.8.4478-4487.2005
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