Estonian
Albanian
Arabic
Armenian
Azerbaijani
Belarusian
Bengali
Bosnian
Catalan
Czech
Danish
Deutsch
Dutch
English
Estonian
Finnish
Français
Greek
Haitian Creole
Hebrew
Hindi
Hungarian
Icelandic
Indonesian
Irish
Italian
Japanese
Korean
Latvian
Lithuanian
Macedonian
Mongolian
Norwegian
Persian
Polish
Portuguese
Romanian
Russian
Serbian
Slovak
Slovenian
Spanish
Swahili
Swedish
Turkish
Ukrainian
Vietnamese
Български
中文(简体)
中文(繁體)

pneumococcal infections/protease

Link salvestatakse lõikelauale
Leht 1 alates 40 tulemused
Immunization of mice with recombinant IgA1 protease of Neisseria meningitidis or several structural derivatives thereof protects the animals infected with a variety of deadly pathogens, including N. meningitidis serogroups A, B, and C and 3 serotypes of Streptococcus pneumonia. In sera of rabbits
Invasive pneumococcal diseases incur significant mortality, morbidity and economic costs. The most effective strategy currently available to reduce the burden of these diseases is vaccination. In this study, we evaluated the protective efficacy of immunizing mice with caseinolytic protease (ClpP)
Streptococcus pneumoniae resides on the mucosal surface of the upper respiratory tract and is ready to spread and trigger clinical diseases. Hence the vaccine that can eliminate the nasopharyngeal colonization was thought to be an ideal protective strategy against pneumococcal invasive diseases.
Streptococcus pneumoniae is a pathogenic bacterium that can cause severe invasive diseases, such as pneumonia, otitis media and meningitis. The pro-inflammatory cytokine, IL-1β, has been reported to play important role in host defense against S. pneumoniae. The mechanism of IL-1β maturation and
Intranasal delivery of pneumococcal protein vaccines would be a promising way to prevent invasive pneumococcal infection. Using an invasive infection model by intranasal inoculation of pneumococci, we demonstrated that immunizing mice intranasally with a mixture of ClpP (the caseinolytic protease)
OBJECTIVE Immune response to many vaccinations is impaired in human immunodeficiency virus (HIV) positive patients. METHODS A total of n = 131 HIV positive patients were vaccinated against influenza, pneumococcal disease, hepatitis A and B, with n = 82 patients (62.6%) receiving 2 or more
Mannose-binding lectin (MBL) and ficolin are complexed with MBL-associated serine proteases, key enzymes of complement activation via the lectin pathway, and act as soluble pattern recognition molecules in the innate immune system. Although numerous reports have revealed the importance of MBL in
Pneumococcal polysaccharide-based vaccines are effective in preventing pneumococcus infection; however, some drawbacks preclude their widespread use in developing and undeveloped countries. Here, we evaluated the protective effects of ATP-dependent caseinolytic protease (ClpP), pneumolysin mutant
Streptococcus pneumoniae, a Gram-positive bacterial pathogen, causes pneumonia, meningitis, and septicemia. Innate immune responses are critical for the control and pathology of pneumococcal infections. It has been demonstrated that S. pneumoniae induces the production of type I interferons (IFNs)
A total of 256 S. pneumoniae strains, the causative agents of infectious processes with different localization, were studied for their virulence (in experiments on mice), neuraminidase and aldolase-protease activity (APA). In pneumococcal strains isolated 18-20 hours after intraperitoneal infection
The complement system plays a key role in host defense against pneumococcal infection. Three different pathways, the classical, alternative and lectin pathways, mediate complement activation. While there is limited information available on the roles of the classical and the alternative activation

Production of immunoglobulin A protease by Streptococcus pneumoniae from animals.

Ainult registreeritud kasutajad saavad artikleid tõlkida
Logi sisse
Human isolates of Streptococcus pneumoniae tested by traditional immunochemical methods produce a protease that cleaves human immunoglobulin A1 (IgA1) into Fab and Fc fragments. The protease may be an important virulence factor, but studies of its pathogenetic significance have been hampered by lack
The blp locus of a type 6A strain of Streptococcus pneumoniae encodes a two-peptide bacteriocin, pneumocin MN, which mediates intraspecies competition during mouse nasopharyngeal colonization. This locus is regulated by a quorum-sensing mechanism consisting of a dedicated two-component regulatory

Pseudomonas aeruginosa Protease IV Exacerbates Pneumococcal Pneumonia and Systemic Disease.

Ainult registreeritud kasutajad saavad artikleid tõlkida
Logi sisse
Pneumonia is a pulmonary disease affecting people of all ages and is consistently a leading cause of childhood mortality and adult hospitalizations. Streptococcus pneumoniae and Pseudomonas aeruginosa are major lung pathogens commonly associated with community-acquired and nosocomial pneumonia.

Contribution of the ATP-dependent protease ClpCP to the autolysis and virulence of Streptococcus pneumoniae.

Ainult registreeritud kasutajad saavad artikleid tõlkida
Logi sisse
The ATP-dependent caseinolytic proteases (Clp) are fundamental for stress tolerance and virulence in many pathogenic bacteria. The role of ClpC in the autolysis and virulence of Streptococcus pneumoniae is controversial. In this study, we tested the role of ClpC in a number of S. pneumoniae strains
Liitu meie
facebooki lehega

Kõige täiuslikum ravimtaimede andmebaas, mida toetab teadus

  • Töötab 55 keeles
  • Taimsed ravimid, mida toetab teadus
  • Maitsetaimede äratundmine pildi järgi
  • Interaktiivne GPS-kaart - märgistage ürdid asukohas (varsti)
  • Lugege oma otsinguga seotud teaduspublikatsioone
  • Otsige ravimtaimi nende mõju järgi
  • Korraldage oma huvisid ja hoidke end kursis uudisteuuringute, kliiniliste uuringute ja patentidega

Sisestage sümptom või haigus ja lugege ravimtaimede kohta, mis võivad aidata, tippige ürdi ja vaadake haigusi ja sümptomeid, mille vastu seda kasutatakse.
* Kogu teave põhineb avaldatud teaduslikel uuringutel

Google Play badgeApp Store badge