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Some Listeria species are important human and animal pathogens that can be found in contaminated food and produce a variety of virulence factors involved in their pathogenicity. Listeria strains exhibiting multidrug resistance are known to be progressively increasing and that is why continuous monitoring is needed. Effective therapy against pathogenic Listeria requires identification of the bacterial strain involved, as well as determining its virulence factors, such as antibiotic resistance and sensitivity. The present study describes the use of liquid chromatography–electrospray ionization tandem mass spectrometry (LC–ESI–MS/MS) to do a global shotgun proteomics characterization for pathogenic Listeria species. This method allowed the identification of a total of 2990 non-redundant peptides, representing 2727 proteins. Furthermore, 395 of the peptides correspond to proteins that play a direct role in Listeria pathogenicity; they were identified as virulence factors, toxins and anti-toxins, or associated with either antibiotics (involved in antibiotic-related compounds production or resistance) or resistance to toxic substances. The proteomic repository obtained here can be the base for further research into pathogenic Listeria species and facilitate the development of novel therapeutics for these pathogens.
Ana Abril; Mónica Carrera; Karola Böhme; Jorge Barros-Velázquez; Pilar Calo-Mata; Angeles Sánchez-Pérez; Tomás Villa. Proteomic Characterization of Antibiotic Resistance in Listeria and Production of Antimicrobial and Virulence Factors. International Journal of Molecular Sciences 2021, 22, 8141 .
AMA StyleAna Abril, Mónica Carrera, Karola Böhme, Jorge Barros-Velázquez, Pilar Calo-Mata, Angeles Sánchez-Pérez, Tomás Villa. Proteomic Characterization of Antibiotic Resistance in Listeria and Production of Antimicrobial and Virulence Factors. International Journal of Molecular Sciences. 2021; 22 (15):8141.
Chicago/Turabian StyleAna Abril; Mónica Carrera; Karola Böhme; Jorge Barros-Velázquez; Pilar Calo-Mata; Angeles Sánchez-Pérez; Tomás Villa. 2021. "Proteomic Characterization of Antibiotic Resistance in Listeria and Production of Antimicrobial and Virulence Factors." International Journal of Molecular Sciences 22, no. 15: 8141.
The present review represents an update on the fundamental role played by the Rho factor, which facilitates the process of Rho-dependent transcription termination in the prokaryotic world; it also provides a summary of relevant mutations in the Rho factor and the insights they provide into the functions carried out by this protein. Furthermore, a section is dedicated to the putative future use of Rho (the ‘taming’ of Rho) to facilitate biotechnological processes and adapt them to different technological contexts. Novel bacterial strains can be designed, containing mutations in the rho gene, that are better suited for different biotechnological applications. This process can obtain novel microbial strains that are adapted to lower temperatures of fermentation, shorter production times, exhibit better nutrient utilization, or display other traits that are beneficial in productive Biotechnology. Additional important issues reviewed here include epistasis, the design of TATA boxes, the role of small RNAs, and the manipulation of clathrin-mediated endocytosis, by some pathogenic bacteria, to invade eukaryotic cells. • It is postulated that controlling the action of the prokaryotic Rho factor could generate major biotechnological improvements, such as an increase in bacterial productivity or a reduction of the microbial-specific growth rate. • The review also evaluates the putative impact of epistatic mechanisms on Biotechnology, both as possible responsible for unexpected failures in gene cloning and more important for the genesis of new strains for biotechnological applications • The use of clathrin-coated vesicles by intracellular bacterial microorganisms is included too and proposed as a putative delivery mechanism, for drugs and vaccines.
Tomás G. Villa; Ana G. Abril; Angeles Sánchez-Pérez. Mastering the control of the Rho transcription factor for biotechnological applications. Applied Microbiology and Biotechnology 2021, 105, 4053 -4071.
AMA StyleTomás G. Villa, Ana G. Abril, Angeles Sánchez-Pérez. Mastering the control of the Rho transcription factor for biotechnological applications. Applied Microbiology and Biotechnology. 2021; 105 (10):4053-4071.
Chicago/Turabian StyleTomás G. Villa; Ana G. Abril; Angeles Sánchez-Pérez. 2021. "Mastering the control of the Rho transcription factor for biotechnological applications." Applied Microbiology and Biotechnology 105, no. 10: 4053-4071.
The present work describes LC-ESI-MS/MS MS (liquid chromatography-electrospray ionization-tandem mass spectrometry) analyses of tryptic digestion peptides from phages that infect mastitis-causing Staphylococcus aureus isolated from dairy products. A total of 1933 nonredundant peptides belonging to 1282 proteins were identified and analyzed. Among them, 79 staphylococcal peptides from phages were confirmed. These peptides belong to proteins such as phage repressors, structural phage proteins, uncharacterized phage proteins and complement inhibitors. Moreover, eighteen of the phage origin peptides found were specific to S. aureus strains. These diagnostic peptides could be useful for the identification and characterization of S. aureus strains that cause mastitis. Furthermore, a study of bacteriophage phylogeny and the relationship among the identified phage peptides and the bacteria they infect was also performed. The results show the specific peptides that are present in closely related phages and the existing links between bacteriophage phylogeny and the respective Staphylococcus spp. infected.
Ana Abril; Mónica Carrera; Karola Böhme; Jorge Barros-Velázquez; Benito Cañas; José-Luis Rama; Tomás Villa; Pilar Calo-Mata. Proteomic Characterization of Bacteriophage Peptides from the Mastitis Producer Staphylococcus aureus by LC-ESI-MS/MS and the Bacteriophage Phylogenomic Analysis. Foods 2021, 10, 799 .
AMA StyleAna Abril, Mónica Carrera, Karola Böhme, Jorge Barros-Velázquez, Benito Cañas, José-Luis Rama, Tomás Villa, Pilar Calo-Mata. Proteomic Characterization of Bacteriophage Peptides from the Mastitis Producer Staphylococcus aureus by LC-ESI-MS/MS and the Bacteriophage Phylogenomic Analysis. Foods. 2021; 10 (4):799.
Chicago/Turabian StyleAna Abril; Mónica Carrera; Karola Böhme; Jorge Barros-Velázquez; Benito Cañas; José-Luis Rama; Tomás Villa; Pilar Calo-Mata. 2021. "Proteomic Characterization of Bacteriophage Peptides from the Mastitis Producer Staphylococcus aureus by LC-ESI-MS/MS and the Bacteriophage Phylogenomic Analysis." Foods 10, no. 4: 799.
RNA viruses, in general, exhibit high mutation rates; this is mainly due to the low fidelity displayed by the RNA-dependent polymerases required for their replication that lack the proofreading machinery to correct misincorporated nucleotides and produce high mutation rates. This lack of replication fidelity, together with the fact that RNA viruses can undergo spontaneous mutations, results in genetic variants displaying different viral morphogenesis, as well as variation on their surface glycoproteins that affect viral antigenicity. This diverse viral population, routinely containing a variety of mutants, is known as a viral ‘quasispecies’. The mutability of their virions allows for fast evolution of RNA viruses that develop antiviral resistance and overcome vaccines much more rapidly than DNA viruses. This also translates into the fact that pathogenic RNA viruses, that cause many diseases and deaths in humans, represent the major viral group involved in zoonotic disease transmission, and are responsible for worldwide pandemics.
T. G. Villa; Ana G. Abril; S. Sánchez; T. de Miguel; A. Sánchez-Pérez. Animal and human RNA viruses: genetic variability and ability to overcome vaccines. Archives of Microbiology 2020, 203, 443 -464.
AMA StyleT. G. Villa, Ana G. Abril, S. Sánchez, T. de Miguel, A. Sánchez-Pérez. Animal and human RNA viruses: genetic variability and ability to overcome vaccines. Archives of Microbiology. 2020; 203 (2):443-464.
Chicago/Turabian StyleT. G. Villa; Ana G. Abril; S. Sánchez; T. de Miguel; A. Sánchez-Pérez. 2020. "Animal and human RNA viruses: genetic variability and ability to overcome vaccines." Archives of Microbiology 203, no. 2: 443-464.
Staphylococcus aureus constitutes a major food-borne pathogen, as well as one of the main causative agents of mastitis in dairy ruminants. This pathogen can produce a variety of extracellular toxins; these include the shock syndrome toxin 1 (TSST-1), exfoliative toxins, staphylococcal enterotoxins (SE), hemolysins, and leukocidins. S. aureus expresses many virulence proteins, involved in evading the host defenses, hence facilitating microbial colonization of the mammary glands of the animals. In addition, S. aureus exotoxins play a role in the development of both skin infections and mastitis. Indeed, if these toxins remain in dairy products for human consumption, they can cause staphylococcal food poisoning (SFP) outbreaks. As a result, there is a need for procedures to identify the presence of exotoxins in human food, and the methods used must be fast, sensitive, reliable, and accurate. It is also essential to determine the best medical therapy for human patients suffering from S. aureus infections, as well as establishing the relevant veterinary treatment for infected ruminants, to avoid economic losses in the dairy industry. This review summarizes the role of S. aureus toxins in the development of mastitis in ruminants, their negative effects in the food and dairy industries, and the different methods used for the identification of these toxins in food destined for human consumption.
Ana G. Abril; Tomas Gonzalez-Villa; Jorge Barros-Velázquez; Benito Cañas; Angeles Sánchez-Pérez; Pilar Calo-Mata; Mónica Carrera. Staphylococcus aureus Exotoxins and Their Detection in the Dairy Industry and Mastitis. Toxins 2020, 12, 537 .
AMA StyleAna G. Abril, Tomas Gonzalez-Villa, Jorge Barros-Velázquez, Benito Cañas, Angeles Sánchez-Pérez, Pilar Calo-Mata, Mónica Carrera. Staphylococcus aureus Exotoxins and Their Detection in the Dairy Industry and Mastitis. Toxins. 2020; 12 (9):537.
Chicago/Turabian StyleAna G. Abril; Tomas Gonzalez-Villa; Jorge Barros-Velázquez; Benito Cañas; Angeles Sánchez-Pérez; Pilar Calo-Mata; Mónica Carrera. 2020. "Staphylococcus aureus Exotoxins and Their Detection in the Dairy Industry and Mastitis." Toxins 12, no. 9: 537.
The present work focuses on LC-ESI-MS/MS (liquid chromatography-electrospray ionization-tandem mass spectrometry) analysis of phage-origin tryptic digestion peptides from mastitis-causing Streptococcus spp. isolated from milk. A total of 2,546 non-redundant peptides belonging to 1,890 proteins were identified and analyzed. Among them, 65 phage-origin peptides were determined as specific Streptococcus spp. peptides. These peptides belong to proteins such as phage repressors, phage endopeptidases, structural phage proteins, and uncharacterized phage proteins. Studies involving bacteriophage phylogeny and the relationship between phages encoding the peptides determined and the bacteria they infect were also performed. The results show how specific peptides are present in closely related phages, and a link exists between bacteriophage phylogeny and the Streptococcus spp. they infect. Moreover, the phage peptide M∗ATNLGQAYVQIM∗PSAK is unique and specific for Streptococcus agalactiae. These results revealed that diagnostic peptides, among others, could be useful for the identification and characterization of mastitis-causing Streptococcus spp., particularly peptides that belong to specific functional proteins, such as phage-origin proteins, because of their specificity to bacterial hosts.
Ana Abril; Mónica Carrera; Karola Böhme; Jorge Barros-Velázquez; Benito Cañas; Jose L. R. Rama; Tomás G. Villa; Pilar Calo-Mata. Characterization of Bacteriophage Peptides of Pathogenic Streptococcus by LC-ESI-MS/MS: Bacteriophage Phylogenomics and Their Relationship to Their Host. Frontiers in Microbiology 2020, 11, 1241 .
AMA StyleAna Abril, Mónica Carrera, Karola Böhme, Jorge Barros-Velázquez, Benito Cañas, Jose L. R. Rama, Tomás G. Villa, Pilar Calo-Mata. Characterization of Bacteriophage Peptides of Pathogenic Streptococcus by LC-ESI-MS/MS: Bacteriophage Phylogenomics and Their Relationship to Their Host. Frontiers in Microbiology. 2020; 11 ():1241.
Chicago/Turabian StyleAna Abril; Mónica Carrera; Karola Böhme; Jorge Barros-Velázquez; Benito Cañas; Jose L. R. Rama; Tomás G. Villa; Pilar Calo-Mata. 2020. "Characterization of Bacteriophage Peptides of Pathogenic Streptococcus by LC-ESI-MS/MS: Bacteriophage Phylogenomics and Their Relationship to Their Host." Frontiers in Microbiology 11, no. : 1241.
Streptococcus spp. are major mastitis pathogens present in dairy products, which produce a variety of virulence factors that are involved in streptococcal pathogenicity. These include neuraminidase, pyrogenic exotoxin, and M protein, and in addition they might produce bacteriocins and antibiotic-resistance proteins. Unjustifiable misuse of antimicrobials has led to an increase in antibiotic-resistant bacteria present in foodstuffs. Identification of the mastitis-causing bacterial strain, as well as determining its antibiotic resistance and sensitivity is crucial for effective therapy. The present work focused on the LC–ESI–MS/MS (liquid chromatography–electrospray ionization tandem mass spectrometry) analysis of tryptic digestion peptides from mastitis-causing Streptococcus spp. isolated from milk. A total of 2706 non-redundant peptides belonging to 2510 proteins was identified and analyzed. Among them, 168 peptides were determined, representing proteins that act as virulence factors, toxins, anti-toxins, provide resistance to antibiotics that are associated with the production of lantibiotic-related compounds, or play a role in the resistance to toxic substances. Protein comparisons with the NCBI database allowed the identification of 134 peptides as specific to Streptococcus spp., while two peptides (EATGNQNISPNLTISNAQLNLEDKNK and DLWC*NM*IIAAK) were found to be species-specific to Streptococcus dysgalactiae. This proteomic repository might be useful for further studies and research work, as well as for the development of new therapeutics for the mastitis-causing Streptococcus strains.
Ana G. Abril; Mónica Carrera; Karola Böhme; Jorge Barros-Velázquez; José-Luis R. Rama; Pilar Calo-Mata; Angeles Sánchez-Pérez; Tomás G. Villa. Proteomic Characterization of Antibiotic Resistance, and Production of Antimicrobial and Virulence Factors in Streptococcus Species Associated with Bovine Mastitis. Could Enzybiotics Represent Novel Therapeutic Agents Against These Pathogens? Antibiotics 2020, 9, 1 .
AMA StyleAna G. Abril, Mónica Carrera, Karola Böhme, Jorge Barros-Velázquez, José-Luis R. Rama, Pilar Calo-Mata, Angeles Sánchez-Pérez, Tomás G. Villa. Proteomic Characterization of Antibiotic Resistance, and Production of Antimicrobial and Virulence Factors in Streptococcus Species Associated with Bovine Mastitis. Could Enzybiotics Represent Novel Therapeutic Agents Against These Pathogens? Antibiotics. 2020; 9 (6):1.
Chicago/Turabian StyleAna G. Abril; Mónica Carrera; Karola Böhme; Jorge Barros-Velázquez; José-Luis R. Rama; Pilar Calo-Mata; Angeles Sánchez-Pérez; Tomás G. Villa. 2020. "Proteomic Characterization of Antibiotic Resistance, and Production of Antimicrobial and Virulence Factors in Streptococcus Species Associated with Bovine Mastitis. Could Enzybiotics Represent Novel Therapeutic Agents Against These Pathogens?" Antibiotics 9, no. 6: 1.
Ana G. Abril; Mónica Carrera; Karola Böhme; Jorge Barros-Velázquez; José-Luis R. Rama; Pilar Calo-Mata; Angeles Sánchez-Pérez; Tomás G. Villa. Proteomic Characterization of Antibiotic Resistance, and Production of Antimicrobial and Virulence Factors in Streptococcus Species Associated with Bovine Mastitis. Could Enzybiotics Represent Novel Therapeutic Agents Against These Pathogens? Antibiotics 2020, 9, 302 .
AMA StyleAna G. Abril, Mónica Carrera, Karola Böhme, Jorge Barros-Velázquez, José-Luis R. Rama, Pilar Calo-Mata, Angeles Sánchez-Pérez, Tomás G. Villa. Proteomic Characterization of Antibiotic Resistance, and Production of Antimicrobial and Virulence Factors in Streptococcus Species Associated with Bovine Mastitis. Could Enzybiotics Represent Novel Therapeutic Agents Against These Pathogens? Antibiotics. 2020; 9 (6):302.
Chicago/Turabian StyleAna G. Abril; Mónica Carrera; Karola Böhme; Jorge Barros-Velázquez; José-Luis R. Rama; Pilar Calo-Mata; Angeles Sánchez-Pérez; Tomás G. Villa. 2020. "Proteomic Characterization of Antibiotic Resistance, and Production of Antimicrobial and Virulence Factors in Streptococcus Species Associated with Bovine Mastitis. Could Enzybiotics Represent Novel Therapeutic Agents Against These Pathogens?" Antibiotics 9, no. 6: 302.
RNA polymerases (RNAPs) carry out transcription in the three domains of life, Bacteria, Archaea, and Eukarya. Transcription initiation is highly regulated by a variety of transcription factors, whose number and subunit complexity increase during evolution. This process is regulated in Bacteria by the σ factor, while the three eukaryotic RNAPs require a complex set of transcription factors (TFs) and a TATA-binding protein (TBP). The archaeal transcription system appears to be an ancestral version of the eukaryotic RNAPII, requiring transcription factor B (TFB), TBP, and transcription factor E (TFE). The function of the bacterial sigma (σ) factor has been correlated to the roles played by the eukaryotic RNAP II and the archaeal RNAP. In addition, σ factors, TFB, and TFIIB all contain multiple DNA binding helix-turn-helix (HTH) structural motifs; although TFIIB and TFB display two HTH domains, while the bacterial σ factor spans 4 HTH motifs. The sequence similarities and structure alignments of the bacterial σ factor, eukaryotic TFIIB, and archaeal TFB evidence that these three proteins are homologs.Key Points• Transcription initiation is highly regulated by TFs.• Transcription is finely regulated in all domains of life by different sets of TFs.• Specific TFs in Bacteria, Eukarya and Archaea are homologs.
Ana Abril; Jose Luis R. Rama; A. Sánchez-Pérez; Tomás G. Villa. Prokaryotic sigma factors and their transcriptional counterparts in Archaea and Eukarya. Applied Microbiology and Biotechnology 2020, 104, 4289 -4302.
AMA StyleAna Abril, Jose Luis R. Rama, A. Sánchez-Pérez, Tomás G. Villa. Prokaryotic sigma factors and their transcriptional counterparts in Archaea and Eukarya. Applied Microbiology and Biotechnology. 2020; 104 (10):4289-4302.
Chicago/Turabian StyleAna Abril; Jose Luis R. Rama; A. Sánchez-Pérez; Tomás G. Villa. 2020. "Prokaryotic sigma factors and their transcriptional counterparts in Archaea and Eukarya." Applied Microbiology and Biotechnology 104, no. 10: 4289-4302.
A bacterial strain, designated BC09T, was isolated from a contaminated sample of condensed milk. Phylogenetic analyses based on 16S rRNA gene sequences placed strain BC09T into the genus Bacillus with its closest relatives being Bacillus safensis and Bacillus australimaris with 100 and 99.9 % similarity, respectively. Analysis of the gyrB gene confirmed the closeness of strain BC09T with respect to the species B. safensis since it presented 97.8 and 95.2 % similarity values, respectively, to the type strains of B. safensis and B. australimaris. DNA–DNA hybridization confirmed these results showing averages of 67 and 56 %, respectively, between strain BC09T and the type strains of B. safensis and B. australimaris. Average nucleotide identity blast values obtained for BC09T compared to the closest relative type strains were 95.7 and 67.6 %, respectively, and predicted DNA–DNA hybridization values were 93.1 and 51.9 %, respectively. However, strain BC09T differs from the type strains of its closest relatives in several phenotypic characteristics. MK-7 was the only menaquinone detected and iso-C15:0 and anteiso-C15:0 were the major fatty acids. The polar lipid profile consisted of diphosphatidylglycerol, phosphatidylglycerol, two unidentified phospholipids, two unidentifed glycolipids, three unidentified lipids and one unidentifed phosphoglycolipid. Meso-diaminopimelic acid was detected in the peptidoglycan. The G+C content was 40.9 mol%. Phylogenetic, chemotaxonomic and phenotypic analyses showed that strain BC09T represents a new subspecies of B. safensis, for which the name Bacillus safensis subsp. osmophilus subsp. nov. is proposed. The type strain is BC09T (=LMG 30124T, =CECT 9344T).
Ana Abril; Jose Luis R. Rama; Lucia Feijoo-Siota; Pilar Calo-Mata; Sergio Salazar; Alvaro Peix; Encarna Velázquez; Tomás G. Villa. Bacillus safensis subsp. osmophilus subsp. nov., isolated from condensed milk, and description of Bacillus safensis subsp. safensis subsp. nov. International Journal of Systematic and Evolutionary Microbiology 2019, 69, 189 -195.
AMA StyleAna Abril, Jose Luis R. Rama, Lucia Feijoo-Siota, Pilar Calo-Mata, Sergio Salazar, Alvaro Peix, Encarna Velázquez, Tomás G. Villa. Bacillus safensis subsp. osmophilus subsp. nov., isolated from condensed milk, and description of Bacillus safensis subsp. safensis subsp. nov. International Journal of Systematic and Evolutionary Microbiology. 2019; 69 (1):189-195.
Chicago/Turabian StyleAna Abril; Jose Luis R. Rama; Lucia Feijoo-Siota; Pilar Calo-Mata; Sergio Salazar; Alvaro Peix; Encarna Velázquez; Tomás G. Villa. 2019. "Bacillus safensis subsp. osmophilus subsp. nov., isolated from condensed milk, and description of Bacillus safensis subsp. safensis subsp. nov." International Journal of Systematic and Evolutionary Microbiology 69, no. 1: 189-195.