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endocarditis/proline

Холбоосыг санах ойд хадгалдаг
НийтлэлЭмнэл зүйн туршилтПатент
8 үр дүн

Impact of the high-affinity proline permease gene (putP) on the virulence of Staphylococcus aureus in experimental endocarditis.

Зөвхөн бүртгэлтэй хэрэглэгчид л нийтлэл орчуулах боломжтой
Нэвтрэх / Бүртгүүлэх
Staphylococcus aureus causes a wide variety of invasive human infections. However, delineation of the genes which are essential for the in vivo survival of this pathogen has not been accomplished to date. Using signature tag mutagenesis techniques and large mutant pool screens, previous

Identification and characterization of the PutP proline permease that contributes to in vivo survival of Staphylococcus aureus in animal models.

Зөвхөн бүртгэлтэй хэрэглэгчид л нийтлэл орчуулах боломжтой
Нэвтрэх / Бүртгүүлэх
Staphylococcus aureus is an important pathogen of humans and other animals, causing bacteremia, abscesses, endocarditis, and other infectious syndromes. A signature-tagged mutagenesis (STM) system was adapted for use in studying the genes required for in vivo survival of S. aureus. An STM library

Abiotrophia defectiva adhere to saliva-coated hydroxyapatite beads via interactions between salivary proline-rich-proteins and bacterial glycerlaldehyde-3-phosphate dehydrogenase

Зөвхөн бүртгэлтэй хэрэглэгчид л нийтлэл орчуулах боломжтой
Нэвтрэх / Бүртгүүлэх
Abiotrophia defectiva is a species of nutritionally variant streptococci that is found in human saliva and dental plaques and that has been associated with infective endocarditis. In our previous study, we found that A. defectiva could bind specifically to saliva-coated hydroxyapatite beads (SHA).

Bartonella tribocorum sp. nov., a new Bartonella species isolated from the blood of wild rats.

Зөвхөн бүртгэлтэй хэрэглэгчид л нийтлэл орчуулах боломжтой
Нэвтрэх / Бүртгүүлэх
Two Bartonella strains from blood of two wild rats (Rattus norvegicus) living in a rural environment were isolated. These strains were distinct from all previously known Bartonella species based on phenotypic and genotypic characteristics. This new species is distinguished by its trypsin-like

Defining antibody targets in Streptococcus oralis infection.

Зөвхөн бүртгэлтэй хэрэглэгчид л нийтлэл орчуулах боломжтой
Нэвтрэх / Бүртгүүлэх
Immunoblotting of sera from 12 neutropenic patients with Streptococcus oralis septicemia and 18 patients with endocarditis due to viridans group streptococci revealed immunodominant S. oralis antigens at 85 and 180 kDa. The former cross-reacted with a mouse monoclonal antibody to hsp90. The latter

Streptococcus gordonii FSS2 Challisin affects fibrin clot formation by digestion of the αC region and cleavage of the N -terminal region of the Bβ chains of fibrinogen.

Зөвхөн бүртгэлтэй хэрэглэгчид л нийтлэл орчуулах боломжтой
Нэвтрэх / Бүртгүүлэх
Bacteria within endocarditis vegetations are encased in fibrin matrix that is resistant to resolution. We have previously shown that FSS2 Challisin, a serine protease from Streptococcus gordonii, is able to hydrolyse the Aα and Bβ chains of fibrinogen and has potent angiotensin converting enzyme

A single mutation in enzyme I of the sugar phosphotransferase system confers penicillin tolerance to Streptococcus gordonii.

Зөвхөн бүртгэлтэй хэрэглэгчид л нийтлэл орчуулах боломжтой
Нэвтрэх / Бүртгүүлэх
Tolerance is a poorly understood phenomenon that allows bacteria exposed to a bactericidal antibiotic to stop their growth and withstand drug-induced killing. This survival ability has been implicated in antibiotic treatment failures. Here, we describe a single nucleotide mutation (tol1) in a

Dipeptidylpeptidase IV of Streptococcus suis degrades the porcine antimicrobial peptide PR-39 and neutralizes its biological properties.

Зөвхөн бүртгэлтэй хэрэглэгчид л нийтлэл орчуулах боломжтой
Нэвтрэх / Бүртгүүлэх
Streptococcus suis is a major swine pathogen causing pathologies such as meningitis, sepsis, endocarditis, and arthritis. Several surface-bound and secreted proteases produced by S. suis have been identified and proposed as virulence factors. PR-39 is a proline/arginine-rich antimicrobial peptide
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