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Palabras clave – provistas por la editorial

Aeromonas hydrophila; LysR-family; ΔlahS; global regulator; virulence; Sclerotinia sclerotiorum; SsNsd1; compound appressorium; two-dimensional electrophoresis; proteomics analysis; differential expression proteins; cystic fibrosis; Pseudomonas aeruginosa; Burkholderia cepacia complex; small noncoding regulatory RNAs; pathogenicity; usg; truA; Salmonella enterica serovar Typhimurium; oxidative stress; intracellular survival; pathogenomics; coagulase-negative staphylococci; virulence factors; whole genome sequencing; autotransporter; covalent labeling; bacterial surface protein; SpyCatcher; topology mapping; virulence factor; Candida; host-pathogen interaction; biofilm formation; morphology; immune evasion; Trueperella pyogenes; pyolysin; infection; immune response; Actinomycetales; Bordetella pertussis; Hfq; omics analysis; T3SS; serum resistance; solute-binding proteins; phytoplasma; effector protein; apple; apple proliferation; bacteria; blood–brain barrier; blood–cerebrospinal fluid barrier; meningitis; outer membrane vesicles (OMVs); Candida albicans; antimicrobial peptides; complement; interspecies interactions; inter-kingdom protection; fungicidal activity; fluconazole; hyphae; antimicrobial peptide; EDTA; primary ciliary dyskinesia; anti-virulence; sputum; chronic infection; Enterobacterales; Klebsiella; Enterobacter; Citrobacter; antibiotic resistance; biofilm; SPATEs; UTIs; cytotoxicity; serine proteases; 5637 bladder cells; mucin; gelatin; actin; protease Lon; Dickeya solani; plant pathogen; motility; type III secretion system; resistance to stress; lon expression; pectinolytic enzymes; gene expression; manipulation; inflammation; persistence; replicative niche; actin proteolysis; metalloproteinases; protease ECP 32; grimelysin; protealysin; bacterial invasion; microbial virulence factors; bacterial pathogens; fungal pathogens