نتایج جستجو برای: ompa
تعداد نتایج: 966 فیلتر نتایج به سال:
The mechanism of membrane insertion and folding of a beta-barrel membrane protein has been studied using the outer membrane protein A (OmpA) as an example. OmpA forms an eight-stranded beta-barrel that functions as a structural protein and perhaps as an ion channel in the outer membrane of Escherichia coli. OmpA folds spontaneously from a urea-denatured state into lipid bilayers of small unilam...
اسینتوباکتر بومانی یکی از مهمترین عوامل عفونت های بیمارستانی و عفونت های کسب شده از اجتماع است که می تواند عامل عفونت های مهمی همچون باکتریمی، عفونت های تنفسی، عفونت های ادراری، ذات الریه، اندوکاردیت و عفونت های زخم و پوستی باشد. عوامل زیادی از جمله آنزیم ها، اگزو توکسین ها، سیدروفور و پروتئین های غشای خارجی در بیماریزایی این باکتری نقش دارند. از عوامل بیماریزایی مهم در این باکتری، وجود پروتئین...
Steady-state and time-resolved fluorescence measurements on each of five native tryptophan residues in full-length and truncated variants of E. coli outer-membrane protein A (OmpA) have been made in folded and denatured states. Tryptophan singlet excited-state lifetimes are multiexponential and vary among the residues. In addition, substantial increases in excited-state lifetimes accompany OmpA...
Shigella flexneri is an intracellular pathogen that deploys an arsenal of virulence factors promoting host cell invasion, intracellular multiplication and intra- and inter-cellular dissemination. We have previously reported that the interaction between apyrase (PhoN2), a periplasmic ATP-diphosphohydrolase, and the C-terminal domain of the outer membrane (OM) protein OmpA is likely required for ...
Vibrio cholerae, the causative agent of the diarrhoeal disease cholera, survives in aquatic environments. The bacterium has developed a survival strategy to grow and survive inside Acanthamoeba castellanii. It has been shown that V. cholerae expresses outer membrane proteins as virulence factors playing a role in the adherence to interacted host cells. This study examined the role of outer memb...
The aim of this project was to study how outer membrane proteins contribute to serum resistance in A. actinomycetemcomitans and A. aphrophilus. Genes encoding Omp100 (A. actinomycetemcomitans) and OmpA (A. actinomycetemcomitans and A. aphrophilus) were knocked out through homologous recombination. Serum resistance was tested by incubating the bacterial strains in normal human serum (NHS; 50%) f...
BACKGROUND Genital chlamydia infection is the most commonly diagnosed sexually transmitted infection in the UK. C. trachomatis genital infections are usually caused by strains which fall into two pathovars: lymphogranuloma venereum (LGV) and the genitourinary genotypes D-K. Although these genotypes can be discriminated by outer membrane protein gene (ompA) sequencing or multi-locus sequence typ...
Outer membrane protein A (OmpA) is located in the membrane of Escherichia coli and other gram-negative bacteria and plays a multifunctional role in bacterial physiology and pathogenesis. In enterohemorrhagic E. coli (EHEC), especially serotype O157:H7, OmpA interacts with cultured human intestinal cells and likely acts as an important component to stimulate the immune response during infection....
Escherichia coli is an important pathogen that causes meningitis in neonates. The development of bacteremia preceding the traversal across the blood-brain barrier is a prerequisite for this pathogen that obviously must survive the bactericidal activity of serum. Here we report that outer membrane protein A (OmpA) of Escherichia coli contributes to serum resistance by binding to C4b binding prot...
Multiple elements controlling adherence of enterohemorrhagic Escherichia coli O157:H7 to HeLa cells.
Adherence of enterohemorrhagic Escherichia coli (EHEC) to the intestinal epithelium is essential for initiation of infection. Intimin is the only factor demonstrated to play a role in intestinal colonization by EHEC O157:H7. Other attempts to identify additional adhesion factors in vitro have been unsuccessful, suggesting that expression of these factors is under tight regulation. We sought to ...
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