Nothing Special   »   [go: up one dir, main page]

Orth et al., 2010 - Google Patents

EspP, a serine protease of enterohemorrhagic Escherichia coli, impairs complement activation by cleaving complement factors C3/C3b and C5

Orth et al., 2010

View PDF @Full View
Document ID
18214668419566433081
Author
Orth D
Ehrlenbach S
Brockmeyer J
Khan A
Huber G
Karch H
Sarg B
Lindner H
Würzner R
Publication year
Publication venue
Infection and immunity

External Links

Snippet

Hemolytic-uremic syndrome (HUS) is a life-threatening disorder characterized by hemolytic anemia, thrombocytopenia, and renal insufficiency. It is caused mainly by infections with enterohemorrhagic Escherichia coli (EHEC). Recently, Shiga toxin 2, the best-studied …
Continue reading at journals.asm.org (PDF) (other versions)

Classifications

    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/43—Enzymes; Proenzymes; Derivatives thereof
    • A61K38/46—Hydrolases (3)
    • A61K38/48—Hydrolases (3) acting on peptide bonds (3.4)
    • A61K38/4813—Exopeptidases (3.4.11. to 3.4.19)
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/43—Enzymes; Proenzymes; Derivatives thereof
    • A61K38/46—Hydrolases (3)
    • A61K38/48—Hydrolases (3) acting on peptide bonds (3.4)
    • A61K38/482—Serine endopeptidases (3.4.21)
    • A61K38/4826—Trypsin (3.4.21.4) Chymotrypsin (3.4.21.1)
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53—Immunoassay; Biospecific binding assay
    • G01N33/569—Immunoassay; Biospecific binding assay for micro-organisms, e.g. protozoa, bacteria, viruses
    • G01N33/56911—Bacteria
    • G01N33/56916—Enterobacteria, e.g. shigella, salmonella, klebsiella, serratia
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • A61K38/1703—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • A61K38/1709—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/164—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria

Similar Documents

Publication Publication Date Title
Orth et al. EspP, a serine protease of enterohemorrhagic Escherichia coli, impairs complement activation by cleaving complement factors C3/C3b and C5
Abreu et al. How Escherichia coli circumvent complement-mediated killing
Jusko et al. Staphylococcal proteases aid in evasion of the human complement system
Lamont et al. Subgingival colonization by Porphyromonas gingivalis
Abreu et al. The serine protease Pic from enteroaggregative Escherichia coli mediates immune evasion by the direct cleavage of complement proteins
Katz et al. Hydrolysis of epithelial junctional proteins by Porphyromonas gingivalis gingipains
Fraga et al. Immune evasion by pathogenic Leptospira strains: the secretion of proteases that directly cleave complement proteins
Irmscher et al. Kallikrein cleaves C3 and activates complement
Lasica et al. The type IX secretion system (T9SS): highlights and recent insights into its structure and function
Puklo et al. Analysis of neutrophil‐derived antimicrobial peptides in gingival crevicular fluid suggests importance of cathelicidin LL‐37 in the innate immune response against periodontogenic bacteria
Terao et al. Multifunctional glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pyogenes is essential for evasion from neutrophils
Jusko et al. A metalloproteinase karilysin present in the majority of Tannerella forsythia isolates inhibits all pathways of the complement system
Leishman et al. Cardiovascular disease and the role of oral bacteria
Mysak et al. Porphyromonas gingivalis: major periodontopathic pathogen overview
Tribble et al. Bacterial invasion of epithelial cells and spreading in periodontal tissue
Cameron Identification of a Treponema pallidum laminin-binding protein
Gómez et al. Staphylococcus aureus protein A activates TNFR1 signaling through conserved IgG binding domains
Franco et al. Cpa, the outer membrane protease of Cronobacter sakazakii, activates plasminogen and mediates resistance to serum bactericidal activity
Lathem et al. Potentiation of C1 esterase inhibitor by StcE, a metalloprotease secreted by Escherichia coli O157: H7
Honda-Ogawa et al. Cysteine proteinase from Streptococcus pyogenes enables evasion of innate immunity via degradation of complement factors
Rubio et al. Linkage of neutrophil serine proteases and decreased surfactant protein-A (SP-A) levels in inflammatory lung disease
Kuo et al. Degradation of complement 3 by streptococcal pyrogenic exotoxin B inhibits complement activation and neutrophil opsonophagocytosis
Potempa et al. Binding of complement inhibitor C4b-binding protein contributes to serum resistance of Porphyromonas gingivalis
Sarker et al. Molecular basis of early stages of Clostridium difficile infection: germination and colonization
Guentsch et al. Cleavage of IgG1 in gingival crevicular fluid is associated with the presence of P orphyromonas gingivalis