Evidence for degradation of gastrointestinal mucin by Candida albicans secretory aspartyl proteinase

Colina, Ana Rosa; Aumont, Francine; Deslauriers, N; Belhumeur, Pierre; Repentigny, Louis de

doi:10.1128/iai.64.11.4514-4519.1996

Cited by 132 publications

(55 citation statements)

References 56 publications

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“…Facilitating tissue penetration by the degradation of mucin 74 Epithelial damage through E-cadherin degradation 75 Defense proteins Immune evasion Degradation of immunoglobulins, lactoferrin, lactoperoxidase, etc. 11,76 Components and regulators of the complement system…”

Section: Host Invasionmentioning

confidence: 99%

Extracellular proteinases of Candida species pathogenic yeasts

Rapała‐Kozik

Bocheńska

Zając

et al. 2018

Molecular Oral Microbiology

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The increased incidence of severe disseminated infections caused by the opportunistic yeast-like fungi Candida spp. highlights the urgent need for research into the major virulence factors of these pathogens-extracellular aspartic proteinases of the candidapepsin and yapsin families. Classically, these enzymes were considered to be generally destructive factors that damage host tissues and provide nutrients for pathogen propagation. However, in recent decades, novel and more specific functions have been suggested for extracellular candidal proteinases. These include contributions to cell wall maintenance and remodeling, the formation of polymicrobial biofilms, adhesion to external protective barriers of the host, the deregulation of host proteolytic cascades (such as the complement system, blood coagulation and the kallikrein-kinin system), a dysregulated host proteinase-inhibitor balance, the inactivation of host antimicrobial peptides, evasion of immune responses and the induction of inflammatory mediator release from host cells. Only a few of these activities recognized in Candida albicans candidapepsins have been also confirmed in other Candida species, and characterization of Candida glabrata yapsins remains limited.

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Section: Host Invasionmentioning

confidence: 99%

Extracellular proteinases of Candida species pathogenic yeasts

Rapała‐Kozik

Bocheńska

Zając

et al. 2018

Molecular Oral Microbiology

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“…To facilitate their mobility in protective mucus layers certain bacteria, fungi and viruses secrete enzymes that hydrolyze mucins [78][79][80]. Therefore, many research groups evaluated the effect of different mucolytic agents, which either degrade actin, DNA or mucin, on the mobility of NANs and nanospheres in (CF) mucus [37,49,50,67,81].…”

Section: Mucolytic Agentsmentioning

confidence: 99%

Extracellular barriers in respiratory gene therapy

Sanders

Rudolph

Braeckmans

et al. 2009

Advanced Drug Delivery Reviews

200

187

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Respiratory gene therapy has been considered for the treatment of a broad range of pulmonary disorders. However, respiratory secretions form an important barrier towards the pulmonary delivery of therapeutic nucleic acids. In this review we will start with a brief description of the biophysical properties of respiratory mucus and alveolar fluid. This must allow the reader to gain insights into the mechanisms by which respiratory secretions may impede the gene transfer efficiency of nucleic acid containing nanoparticles (NANs). Subsequently, we will summarize the efforts that have been done to understand the barrier properties of respiratory mucus and alveolar fluid towards the respiratory delivery of therapeutic nucleic acids. Finally, new and current strategies that can overcome the inhibitory effects of respiratory secretions are discussed.

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“…Therefore, any attempts to determine potential targets of the Sap family in vivo have been mainly based on Sap2 activity in vitro . Sap2 has very broad spectrum of activity and is known to degrade many human proteins at mucosal sites including extracellular matrix and host surface proteins such as keratin, collagen, vimentin, fibronectin, laminin and mucin (Ray et al ., 1990; Ogrydziak, 1993; Colina et al ., 1996; Hube, 1996; Morschhäuser et al ., 1997). The efficient removal of host barriers in vivo would not only provide nutrients for the cells, but would also reveal potential binding sites to enhance C. albicans attachment, colonization and penetration of host tissues and possibly promote dissemination of C .…”

Section: Possible Functions and Targets Of Sap Proteinases In Vivomentioning

confidence: 99%

Candida albicans proteinases and host/pathogen interactions

et al. 2004

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SummaryCandida infections are common, debilitating and often recurring fungal diseases and a problem of significant clinical importance. Candida albicans , the most virulent of the Candida spp., can cause severe mucosal and life-threatening systemic infections in immunocompromised hosts. Attributes that contribute to C. albicans virulence include adhesion, hyphal formation, phenotypic switching and extracellular hydrolytic enzyme production. The extracellular hydrolytic enzymes, especially the secreted aspartyl proteinases (Saps), are one of few gene products that have been shown to directly contribute to C. albicans pathogenicity. Because C. albicans is able to colonize and infect almost every tissue in the human host, it may be crucial for the fungus to possess a number of similar but independently regulated and functionally distinct secreted proteinases to provide sufficient flexibility in order to survive and promote infection at different niche sites. The aim of this review is to explore the functional roles of the C. albicans proteinases and how they may contribute to the host/ pathogen interaction in vivo .

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Evidence for degradation of gastrointestinal mucin by Candida albicans secretory aspartyl proteinase

Abstract: A zone of extracellular digestion of the mucin layer around Candida albicans blastoconidia was observed by transmission electron microscopy in the jejunum of mice inoculated intragastrically (G. T.

Cited by 132 publications

References 56 publications

Extracellular proteinases of Candida species pathogenic yeasts

Extracellular proteinases of Candida species pathogenic yeasts

Extracellular barriers in respiratory gene therapy

Candida albicans proteinases and host/pathogen interactions

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