Antifungal activity of the Enterococcus faecalis peptide EntV requires protease cleavage and disulfide bond formation

Keyphrases

• C.albicans 100%
• Enterococcus Faecalis 100%
• Disulfide Bond Formation 100%
• Protease Cleavage 100%
• Antifungal Activity 100%
• DsbA 80%
• E. Faecalis 60%
• Disulfide Bond 40%
• Virulence 40%
• Candida Albicans (C. albicans) 40%
• Gelatinase 40%
• Cysteine 20%
• Therapeutic Potential 20%
• Amino Acids 20%
• Genetic Modification 20%
• Microbiome 20%
• Thioredoxin 20%
• Antimicrobial Resistance 20%
• Disease Prevention 20%
• Post-translational Modification 20%
• Fungi 20%
• Protein Post-translational Modification 20%
• Public Health Risk 20%
• Commensal 20%
• Biofilm Formation 20%
• Gram-positive Bacteria 20%
• Centers for Disease Control 20%
• Active Form 20%
• Two-species 20%
• Serine Protease 20%
• Infections In Immunocompromised Hosts 20%
• Chemical Treatment 20%
• Chemical Genetics 20%
• Bacteriocin 20%
• Gaps in Knowledge 20%
• Secreted Enzymes 20%
• Antifungal Resistance 20%
• Redox-active 20%
• Treatment Modification 20%
• Global Public Health 20%
• Antifungal Properties 20%
• Pathobiont 20%
• Hyphal Morphogenesis 20%

Immunology and Microbiology

• Peptides 100%
• Disulfide Bond 100%
• Candida albicans 100%
• Enterococcus faecalis 100%
• Antifungal Activity 100%
• DsbA 57%
• Protein Processing 28%
• Infection 28%
• Cysteine 14%
• Secretion (Process) 14%
• Microbiome 14%
• Serine 14%
• Biofilm 14%
• Amino Acid 14%
• Immunocompromised Patient 14%
• Prevalence 14%
• Morphogenesis 14%
• Gram-Positive Bacteria 14%
• DNA Modification 14%
• Commensal 14%
• Antifungal Resistance 14%
• Antibiotic Resistance 14%