High-affinity interaction between gram-negative flagellin and a cell surface polypeptide results in human monocyte activation

Infection and Immunity

Volumn 68, Issue 10, 2000, Pages 5525-5529

  McDermott, P F ^a   Ciacci Woolwine, F ^a   Snipes, J A ^a   Mizel, S B ^a  

^a WAKE FOREST SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CELL SURFACE PROTEIN; FLAGELLIN; POLYPEPTIDE; RECEPTOR; TRYPSIN; TUMOR NECROSIS FACTOR ALPHA;

AMINO TERMINAL SEQUENCE; ANIMAL EXPERIMENT; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CYTOKINE PRODUCTION; GENETIC CONSERVATION; HUMAN; HUMAN CELL; LEUKOCYTE ACTIVATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PSEUDOMONAS AERUGINOSA; SALMONELLA ENTERICA; SALMONELLA ENTERITIDIS; SALMONELLA TYPHIMURIUM;

CELLS, CULTURED; COMPLEMENTARITY DETERMINING REGIONS; FLAGELLIN; HUMAN; MONOCYTES; PEPTIDES; PSEUDOMONAS AERUGINOSA; RECEPTORS, CELL SURFACE; RECOMBINANT PROTEINS; SALMONELLA; SUPPORT, U.S. GOV'T, P.H.S.; TRYPSIN; TUMOR NECROSIS FACTOR;

EID: 0033796984     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.68.10.5525-5529.2000     Document Type: Article

References (14)

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6. The flagellar filament protein
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11. Monocyte deactivation - Rationale for a new therapeutic strategy in sepsis
12. Covalent structure of three phase-1 flagellar filament proteins of Salmonella
13. Preparation and analysis of DNA
14. Salmonella typhi flagella are potent inducers of proinflammatory cytokine secretion by human monocytes