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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.

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Citations
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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.
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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
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Journal ArticleDOI

Mechanisms of bacterial virulence.

TL;DR: It is evident from the resulting overview of experimental findings that knowledge concerning virulence of extracellular parasites outweighs that collected for both facultative and obligate intracellular parasites.
Book ChapterDOI

Bacterial Adherence to Cell Surface Sugars

TL;DR: Bacterial adherence to animal cell surfaces is of interest because of its relation to pathogenicity and the insight it provides into determinants of intercellular recognition, and the design of more effective adherence inhibitors that may help to prevent certain bacterial infections.
Journal ArticleDOI

Proteus mirabilis amino acid deaminase: cloning, nucleotide sequence, and characterization of aad.

TL;DR: A gene encoding an amino acid deaminase of uropathogenic Proteus mirabilis was identified by screening a genomic library hosted in Escherichia coli DH5 alpha for amino acids activity and did not share significant amino acid sequence similarity with any other polypeptide in the PIR or SwissProt database.
Journal ArticleDOI

Attachment of Proteus mirabilis to human urinary sediment epithelial cells in vitro is different from that of Escherichia coli.

TL;DR: Differences in adhesion characteristics of E. coli and P. mirabilis may relate to the differences in clinical appearance of urinary tract infections produced by the two organisms.
Journal ArticleDOI

Proteus mirabilis MR/P fimbrial operon: Genetic organization, nucleotide sequence, and conditions for expression

TL;DR: The mrp gene cluster encoded by 7,293 bp predicts eight polypeptides that share > or = 25% amino acid identity with at least one other enteric fimbrial gene product encoded by the pap, fim, smf, fan, or mrk gene clusters.
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