Candida albicans is an opportunistic fungus that is part of the normal microflora commonly found in the human digestive tract and the normal mucosa or skin of healthy individuals. However, in immunocompromised individuals, it becomes a serious health concern and a threat to their lives and is ranked as the leading fungal infection in humans worldwide. As existing treatments for this infection are non-specific or under threat of developing resistance, there is a dire necessity to find new targets for designing specific drugs to defeat this fungus. Some authors reported the presence of the transglutaminase activity in Candida and Saccharomyces, but its identity remains unknown. We report here the phenotypic effects produced by the inhibition of transglutaminase enzymatic activity with cystamine, including growth inhibition of yeast cells, induction of autophagy in response to damage caused by cystamine, alteration of the normal yeast division pattern, changes in cell wall, and inhibition of the yeast-to-mycelium transition. The latter phenomenon was also observed in the C. albicans ATCC 26555 strain. Growth inhibition by cystamine was also determined in other Candida strains, demonstrating the importance of transglutaminase in these species. Finally, we identified enolase 1 as the cell wall protein responsible for TGase activity. After studying the inhibition of enzymatic activities with anti-CaEno1 antibodies and through bioinformatics studies, we suggest that the enolase and transglutaminase catalytic sites are localized in different domains of the protein. The aforementioned data indicate that TGase/Eno1 is a putative target for designing new drugs to control C. albicans infection.

We have established the chemical structure of (+)-bassianolone (3), the antimicrobial compound precursor of cephalosporolides E and F, and that of the furan metabolite 4 from the entomopathogenic fungus Beauveria bassiana.

Candida species are a natural commensal of humans and when the immune system is compromised it can cause candidiasis. C. albicans is the main etiological agent of candidiasis, representing nearly 60% of the total cases worldwide. The cell wall provides protection against several physical and chemical aggressions and is responsible for the different shapes displayed by C. albicans. The cell wall is not a static structure, but a dynamic one, having great plasticity to allow different cell morphologies, molecular remodeling and changes in the cell wall composition as a result from adaptation to the surrounding environment. It is mainly composed of chitin, β-glucan and mannoproteins. Therefore, the cell wall components are putative targets for the discovery and development of new drugs. The cell wall reprograming in response to several conditions, including a host carbon source, blood, serum, high temperature, acidic environment, and morphogenesis, have a direct impact on the mannoprotein content and might be involved in adherence, drug resistance and virulence of C. albicans. In this chapter, we performed an analysis of the proteins that have been identified in the C. albicans cell wall by our group and others, which allowed the identification of proteins from different intracellular compartments.

Campylobacter is a major foodborne pathogen and its antimicrobial resistance (AMR) has been described worldwide. The main objective of this study was to determine the occurrence and AMR of Campylobacter spp. isolated from broilers throughout the supply chain in Valencia, Spain. A total of 483 samples were included in the analysis: 430 from the slaughterhouse (chicken carcass and neck skin) and 53 from the point of sale (retail broiler and packaging). Taking into account the origin of the sample, the prevalence of Campylobacter spp. was 19% in carcass, 28.2% in neck skin, 36.7% in retail broiler, and 80% in packaging isolates. The prevalence of different species in the analyzed samples was 21.1% and 4.8% for Campylobacter jejuni and Campylobacter coli , respectively. AMR profiling of 125 Campylobacter isolates revealed that 122 (97.6%) of the isolates were resistant to one or more antimicrobials. C. jejuni samples presented high resistance to nalidixic acid and ciprofloxacin, 96.1% and 90.2% respectively, whereas C. coli showed 87% of resistance to both antimicrobials. Both species were resistant to tetracycline ( C. jejuni 84.3% and C. coli 60.9%) and 26.1% of C. coli was resistant to streptomycin. These results showed no significant difference in the frequency of AMR ( p ≥ 0.05) among isolates originated from different points in the food-processing chain at slaughterhouses and retail establishments. In contrast, three main patterns were detected: quinolone–tetracycline (64%), quinolone-only (17.6%), and quinolone–tetracycline–aminoglycosides (8%). Additionally, 12.8% of the isolates presented multidrug resistance, with significantly higher levels detected among C. coli (30.4%) isolates compared with C. jejuni (8.8%) and all the three strains were resistant to all six antibiotics tested. Therefore, these results indicate that broilers could be a source of antimicrobial-resistant Campylobacter in humans and consequently pose a risk to public health.

Following synthesis of its individual components, the cell wall of Candida albicans is assembled extracellularly in two steps. First, a viscoelastic composite is formed by noncovalent interactions between mannoproteins and other wall components. Second, the initial network is consolidated by formation of covalent cross-linkages among the wall polymers. In both processes, specific proteins may regulate the final yeast or mycelial morphology. These proteins might carry out part of what could be called a morphogenetic code. Experimental results have shown that some mannoproteins form supramolecular complexes. They are secreted independently, but released together from cell walls by hydrolases. In C. albicans cell walls a transglutaminase activity has been detected that could be responsible for the formation of covalent bonds between structural proteins. Key words: fungal cell wall, construction, morphogenesis, protein interactions, noncovalent linkages, covalent linkages.