scispace - formally typeset
Journal ArticleDOI

Potential virulence factors of Proteus bacilli.

Antoni Rozalski, +2 more
- 01 Mar 1997 - 
- Vol. 61, Iss: 1, pp 65-89
TLDR
The genus Proteus, which contains bacteria considered now to belong to the opportunistic pathogens, has its most characteristic attribute, swarming growth, enabling them to colonize and survive in higher organisms.
Abstract
The object of this review is the genus Proteus, which contains bacteria considered now to belong to the opportunistic pathogens. Widely distributed in nature (in soil, water, and sewage), Proteus species play a significant ecological role. When present in the niches of higher macroorganisms, these species are able to evoke pathological events in different regions of the human body. The invaders (Proteus mirabilis, P. vulgaris, and P. penneri) have numerous factors including fimbriae, flagella, outer membrane proteins, lipopolysaccharide, capsule antigen, urease, immunoglobulin A proteases, hemolysins, amino acid deaminases, and, finally, the most characteristic attribute of Proteus, swarming growth, enabling them to colonize and survive in higher organisms. All these features and factors are described and commented on in detail. The questions important for future investigation of these facultatively pathogenic microorganisms are also discussed.

read more

Citations
More filters
Journal ArticleDOI

Mechanisms of polymyxin resistance: acquired and intrinsic resistance in bacteria

TL;DR: Current knowledge concerning the different strategies bacteria employ to resist the activities of polymyxins are summarized and increased understanding of these mechanisms is extremely vital and timely to facilitate studies of antimicrobial peptides and find new potential drugs targeting clinically relevant Gram-negative bacteria.
Journal ArticleDOI

Complicated Catheter-Associated Urinary Tract Infections Due to Escherichia coli and Proteus mirabilis

TL;DR: Research focusing on the pathogenesis of CAUTIs will lead to a better understanding of the disease process and will subsequently lead to the development of new diagnosis, prevention, and treatment options.
Journal ArticleDOI

Structure of bacterial lipopolysaccharides.

TL;DR: Bacterial lipopolysaccharides are the major components of the outer surface of Gram-negative bacteria and are often of interest in medicine for their immunomodulatory properties.
Journal ArticleDOI

Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37

TL;DR: The results indicate that proteolytic degradation of LL‐37 is a common virulence mechanism and that molecules which block this degradation could have therapeutic potential.
References
More filters
Journal ArticleDOI

The effect of protein and urine on uropathogen adhesion to polymer substrata

TL;DR: The results emphasize that fluid components, particularly proteins, and substratum surface tension influence bacterial adhesion to biomaterials.
Journal ArticleDOI

The structure of the O-specific polysaccharide chain of Proteus penneri strain 16 lipopolysaccharide.

TL;DR: It was concluded that P. penneri strain 16 anti-(O-specific polysaccharide) antiserum with lipopolysaccharides from several other Proteus strains and the role of 3,6-dideoxy-3-(R)-3-hydroxybutyramido-D-galactose in the serological specificity of P. Penneri strains 16 are discussed.
Journal ArticleDOI

Identification of the promotors directing in vivo expression of hemolysin genes in Proteus vulgaris and Escherichia coli

TL;DR: Elevated hemolytic activity caused by upstream Tn5 insertions in pVU763-709 resulted from increased transcription from this promotor, and the E. coli hly C upstream region contained three separate promotors directing in vivo hly transcription, while the corresponding transcription of the P. vulgaris hly operon originated from a single distinct promotor.
Journal ArticleDOI

Structural investigation of the lipopolysaccharide from Proteus mirabilis R45 (Re-chemotype):

TL;DR: In this article, five phosphorylated saccharides were isolated from the deacylated then N-acetylated lipopolysaccharide (LPS) of Proteus mirabilis R45 (Re-chemotype) by anion-exchange chromatography.
Journal ArticleDOI

Proteinases of Proteus spp.: purification, properties, and detection in urine of infected patients.

TL;DR: The proteinase purified from the urinary tract pathogen P. mirabilis-infected patients was resistant to inhibitors of both serine and thiol proteinases but strongly inhibited by metal chelators, although it was not affected by phosphoramidon, an inhibitor of the thermolysin group of bacterial metalloproteinases.
Related Papers (5)