Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 3 de 3
Filter
Add more filters










Database
Type of study
Language
Publication year range
1.
Cell Mol Life Sci ; 60(12): 2622-36, 2003 Dec.
Article in English | MEDLINE | ID: mdl-14685687

ABSTRACT

Enterococci, traditionally viewed as Gram-positive commensal bacteria inhabiting the alimentary canals of humans and animals, are now acknowledged to be organisms capable of causing life-threatening infections in humans, especially in the nosocomial environment. The existence of enterococci in such a dual role is facilitated, at least in part, by its intrinsic and acquired resistance to virtually all antibiotics currently in use. Beginning with the initial identification of a 'streptococci of fecal origin' in the late 19th century, enterococci have been studied for over a century now. A number of comprehensive reviews during this time have addressed various aspects of enterococci, including classification, biology, virulence, antibiotic resistance and so on. This review specifically addresses the important advances in the field of enterococcal research that have occurred since the beginning of the 21st century. Most notable among these developments have been the insights into enterococcal genomes and pathogenicity.


Subject(s)
Enterococcus/genetics , Adhesins, Bacterial/genetics , Adhesins, Bacterial/physiology , Animals , Bacterial Proteins/physiology , Cell Wall/chemistry , Cytotoxins/genetics , Cytotoxins/physiology , Enterococcus/pathogenicity , Enterococcus/physiology , Gram-Positive Bacterial Infections/metabolism , Humans
2.
Infect Immun ; 69(7): 4366-72, 2001 Jul.
Article in English | MEDLINE | ID: mdl-11401975

ABSTRACT

Enterococcus faecalis bacteria isolated from patients with bacteremia, endocarditis, and urinary tract infections more frequently express the surface protein Esp than do fecal isolates. To assess the role of Esp in colonization and persistence of E. faecalis in an animal model of ascending urinary tract infection, we compared an Esp(+) strain of E. faecalis to its isogenic Esp-deficient mutant. Groups of CBA/J mice were challenged transurethrally with 10(8) CFU of either the parent or mutant strain, and bacteria in the urine, bladder, and kidneys were enumerated 5 days postinfection. Significantly higher numbers of bacteria were recovered from the bladder and urine of mice challenged with the parent strain than from the bladder and urine of mice challenged with the mutant. Colonization of the kidney, however, was not significantly different between the parent and mutant strains. Histopathological evaluations of kidney and bladder tissue done at 5 days postinfection did not show marked histopathological changes consistent with inflammation, mucosal hyperplasia, or apoptosis, and there was no observable difference between the mice challenged with the parent and those challenged with the mutant. We conclude that, while Esp does not influence histopathological changes associated with acute urinary tract infections, it contributes to colonization and persistence of E. faecalis at this site.


Subject(s)
Bacterial Proteins/physiology , Enterococcus faecalis/pathogenicity , Gram-Positive Bacterial Infections/microbiology , Membrane Proteins/physiology , Urinary Tract Infections/microbiology , Animals , Bacterial Proteins/genetics , Disease Models, Animal , Enterococcus faecalis/genetics , Humans , Membrane Proteins/genetics , Mice , Mice, Inbred CBA , Phenotype , Rabbits
3.
Infect Immun ; 67(1): 193-200, 1999 Jan.
Article in English | MEDLINE | ID: mdl-9864215

ABSTRACT

We report the identification of a new cell wall-associated protein of Enterococcus faecalis. Studies on the distribution of the gene encoding this novel surface protein, Esp, reveal a significant (P < 0.001) enrichment in infection-derived E. faecalis isolates. Interestingly, the esp gene was not identified in any of 34 clinical E. faecium isolates or in 4 other less pathogenic enterococcal species tested. Analysis of the structural gene among various E. faecalis isolates reveals the existence of alternate forms of expression of the Esp protein. The deduced primary structure of the Esp protein from strain MMH594, inferred to be 1,873 amino acids (aa) with a predicted mass of approximately 202 kDa, reveals a core region consisting of repeat units that make up 50% of the protein. Esp bears global organizational similarity to the Rib and C alpha proteins of group B streptococci. Identity among Esp, Rib, and C alpha proteins is strikingly localized to a stretch of 13 aa within repeats of similar length. The high degree of conservation of this 13-residue sequence suggests that it plays an important role in the natural selection for this trait among infection-derived E. faecalis and group B streptococcal isolates.


Subject(s)
Antigens, Bacterial , Bacterial Proteins/genetics , Enterococcus faecalis/genetics , Genes, Bacterial , Gram-Positive Bacterial Infections/microbiology , Membrane Proteins/genetics , Adolescent , Adult , Amino Acid Sequence , Antigens, Surface/chemistry , Bacterial Proteins/biosynthesis , Bacterial Proteins/chemistry , Child , Child, Preschool , Clone Cells , Conserved Sequence , Enterococcus faecalis/chemistry , Enterococcus faecalis/isolation & purification , Gene Expression Regulation, Bacterial , Genetic Variation , Humans , Membrane Proteins/biosynthesis , Membrane Proteins/chemistry , Molecular Sequence Data , Tandem Repeat Sequences
SELECTION OF CITATIONS
SEARCH DETAIL