N-linked glycosylation at Asn3 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

Infection and Immunity

Volumn 73, Issue 8, 2005, Pages 4478-4487

  Liu, Dongxu ^a   Cramer, Cort C ^a   Scafidi, Jennifer ^a   Davis III, Alvin E ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ASPARAGINE; BACTERIUM LIPOPOLYSACCHARIDE; CARBOHYDRATE DERIVATIVE; COMPLEMENT COMPONENT C1S INHIBITOR; ENDOTOXIN; LIPID A; LYSINE; MESSENGER RNA; TUMOR NECROSIS FACTOR ALPHA;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; BINDING AFFINITY; BINDING SITE; GLYCOSYLATION; GRAM NEGATIVE BACTERIUM; HUMAN; MACROPHAGE; MOLECULAR INTERACTION; MOUSE; NONHUMAN; PRIORITY JOURNAL; SALMONELLA ENTERICA; SEPTIC SHOCK;

AMINO ACID SUBSTITUTION; ANIMALS; ASPARAGINE; CERCOPITHECUS AETHIOPS; COMPLEMENT C1 INACTIVATOR PROTEINS; COS CELLS; GLYCOSYLATION; HUMANS; LIPID A; MICE; MUTATION; PROTEIN STRUCTURE, TERTIARY; SALMONELLA TYPHIMURIUM; SERPINS;

EID: 23344454258     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.73.8.4478-4487.2005     Document Type: Article

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