Candida albicans Growth Studies: A Hypothesis for the Pathogenesis of Candida Infections in Burns

Neely, Alice N.; Orloff, Mary M.; Holder, Ian Alan

doi:10.1097/00004630-199205000-00004

Cited by 5 publications

(1 citation statement)

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“…Activation of this and of other interrelated cascades that are triggered by this system (complement, fibrinolysis, and arachidonic cascades) can have a variety of negative immunologic consequences for the host. Proteolytic activity may also play a key role in providing a suitable environment that strongly affects the final outcome of Candida infections in burn patients (379), who are more susceptible to fatal candidiasis than are normal individuals. In vitro, at least Sap2p hydrolyzes mucin, and it may contribute in vivo to penetration of the gastrointestinal mucin barrier and provide access to underlying cells (84).…”

Section: Hydrolytic Enzymes and Proteins With Extracellular Targetsmentioning

confidence: 99%

Cell Wall and Secreted Proteins ofCandida albicans: Identification, Function, and Expression

Chaffin

López-Ribot

Casanova

et al. 1998

Microbiol Mol Biol Rev

664

344

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SUMMARY The cell wall is essential to nearly every aspect of the biology and pathogenicity of Candida albicans. Although it was intially considered an almost inert cellular structure that protected the protoplast against osmotic offense, more recent studies have demonstrated that it is a dynamic organelle. The major components of the cell wall are glucan and chitin, which are associated with structural rigidity, and mannoproteins. The protein component, including both mannoprotein and nonmannoproteins, comprises some 40 or more moieties. Wall proteins may differ in their expression, secretion, or topological location within the wall structure. Proteins may be modified by glycosylation (primarily addition of mannose residues), phosphorylation, and ubiquitination. Among the secreted enzymes are those that are postulated to have substrates within the cell wall and those that find substrates in the extracellular environment. Cell wall proteins have been implicated in adhesion to host tissues and ligands. Fibrinogen, complement fragments, and several extracellular matrix components are among the host proteins bound by cell wall proteins. Proteins related to the hsp70 and hsp90 families of conserved stress proteins and some glycolytic enzyme proteins are also found in the cell wall, apparently as bona fide components. In addition, the expression of some proteins is associated with the morphological growth form of the fungus and may play a role in morphogenesis. Finally, surface mannoproteins are strong immunogens that trigger and modulate the host immune response during candidiasis.

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Section: Hydrolytic Enzymes and Proteins With Extracellular Targetsmentioning

confidence: 99%

Cell Wall and Secreted Proteins ofCandida albicans: Identification, Function, and Expression

Chaffin

López-Ribot

Casanova

et al. 1998

Microbiol Mol Biol Rev

664

344

View full text Add to dashboard Cite

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Emerging and Reemerging Microbial Threats

Henderson

Hirvela²

1996

Arch Surg

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The incidence of nosocomial fungal infections had been increasing steadily for the past 25 years. Although they were once believed to be of little clinical consequence, there is now compelling evidence that fungal agents represent a bona fide microbial threat with substantial morbidity and high mortality. Reporting on a series of 30447 nosocomial fungal infections that occurred in the decade from 1980 to 1990, Beck-Sague and Jarvis noted increases in incidence from 90% to 175%. Infection rates rose from 2.0 per 1000 discharges to as high as 6.6 infections per 1000 discharges. Fungal infections increased at all major anatomic sites, including surgical wounds, lung, urinary tract, and bloodstream. Candida species accounted for 78.3% of nosocomial fungal infections, while torulopsis species and aspergillus species accounted for 7.3% and 1.3%, respectively.

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The role ofCandida albicans secreted aspartic proteinase in the development of candidoses

1996

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Although Candida albicans infections in humans are increasingly frequent, our understanding of the host-parasite relationship is limited. The secreted aspartic proteinase of C. albicans was first described in 1965 and has proved to be a major factor in virulence. This enzyme belongs to the class of aspartic proteinases which includes pepsin and renin in humans. Although found in some fungi, secreted aspartic proteinase is rare in these organisms. While the existence of several isoenzymes may not be fully established, it is now obvious that at least seven different genes encode for secreted aspartic proteinase. Within Candida cells it is located in membrane-bound vesicles. Upon fusion of these subcellular structures within the plasma membrane, the enzyme is released to the environment. In the context of human mucosal diseases it is responsible both for adhesion and invasion. Strains from HIV-infected patients with oral candidosis generally exhibit higher enzymatic activity than control strains. In future secreted aspartic proteinase may prove a prime target for new types of antimycotics.

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Candida albicans Growth Studies: A Hypothesis for the Pathogenesis of Candida Infections in Burns

Cited by 5 publications

References 0 publications

Cell Wall and Secreted Proteins ofCandida albicans: Identification, Function, and Expression

Cell Wall and Secreted Proteins ofCandida albicans: Identification, Function, and Expression

Emerging and Reemerging Microbial Threats

The role ofCandida albicans secreted aspartic proteinase in the development of candidoses

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